Academic literature on the topic 'Bioactive Peptide Products'
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Journal articles on the topic "Bioactive Peptide Products"
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Grünewald, Jan, and Mohamed A. Marahiel. "Chemoenzymatic and Template-Directed Synthesis of Bioactive Macrocyclic Peptides." Microbiology and Molecular Biology Reviews 70, no. 1 (March 2006): 121–46. http://dx.doi.org/10.1128/mmbr.70.1.121-146.2006.
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SUMMARY Non-ribosomally synthesized peptides have compelling biological activities ranging from antimicrobial to immunosuppressive and from cytostatic to antitumor. The broad spectrum of applications in modern medicine is reflected in the great structural diversity of these natural products. They contain unique building blocks, such as d-amino acids, fatty acids, sugar moieties, and heterocyclic elements, as well as halogenated, methylated, and formylated residues. In the past decades, significant progress has been made toward the understanding of the biosynthesis of these secondary metabolites by nonribosomal peptide synthetases (NRPSs) and their associated tailoring enzymes. Guided by this knowledge, researchers genetically redesigned the NRPS template to synthesize new peptide products. Moreover, chemoenzymatic strategies were developed to rationally engineer nonribosomal peptides products in order to increase or alter their bioactivities. Specifically, chemical synthesis combined with peptide cyclization mediated by nonribosomal thioesterase domains enabled the synthesis of glycosylated cyclopeptides, inhibitors of integrin receptors, peptide/polyketide hybrids, lipopeptide antibiotics, and streptogramin B antibiotics. In addition to the synthetic potential of these cyclization catalysts, which is the main focus of this review, different enzymes for tailoring of peptide scaffolds as well as the manipulation of carrier proteins with reporter-labeled coenzyme A analogs are discussed.
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Khaldi, Nora. "Bioinformatics approaches for identifying new therapeutic bioactive peptides in food." Functional Foods in Health and Disease 2, no. 10 (October 15, 2012): 325. http://dx.doi.org/10.31989/ffhd.v2i10.80.
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The traditional methods for mining foods for bioactive peptides are tedious and long. Similar to the drug industry, the length of time to identify and deliver a commercial health ingredient that reduces disease symptoms can take anything between 5 to 10 years. Reducing this time and effort is crucial in order to create new commercially viable products with clear and important health benefits. In the past few years, bioinformatics, the science that brings together fast computational biology, and efficient genome mining, is appearing as the long awaited solution to this problem. By quickly mining food genomes for characteristics of certain food therapeutic ingredients, researchers can potentially find new ones in a matter of a few weeks. Yet, surprisingly, very little success has been achieved so far using bioinformatics in mining for food bioactives. The absence of food specific bioinformatic mining tools, the slow integration of both experimental mining and bioinformatics, and the important difference between different experimental platforms are some of the reasons for the slow progress of bioinformatics in the field of functional food and more specifically in bioactive peptide discovery. In this paper I discuss some methods that could be easily translated, using a rational peptide bioinformatics design, to food bioactive peptide mining. I highlight the need for an integrated food peptide database. I also discuss how to better integrate experimental work with bioinformatics in order to improve the mining of food for bioactive peptides, therefore achieving a higher success rates.Keywords: bioactive peptides, bioinformatics, mining food, therapeutic properties, food proteins, functional food.
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Hayes, Maria. "Bioactive Peptides in Preventative Healthcare: An Overview of Bioactivities and Suggested Methods to Assess Potential Applications." Current Pharmaceutical Design 27, no. 11 (April 27, 2021): 1332–41. http://dx.doi.org/10.2174/1381612827666210125155048.
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Food derived bioactive peptides can be generated from various protein sources and usually consist of between 2-30 amino acids with bulky, side-chain aromatic amino acids preferred in the ultimate and penultimate positions at the C-terminal end of the amino acid chain. They are reported to impart a myriad of preventative health beneficial effects to the consumer once ingested and these include heart health benefits through inhibition of enzymes including renin (EC 3.4.23.15) and angiotensin- I-converting enzyme (ACE-1; EC 3.4.15.1) within the renin angiotensin aldosterone system (RAAS) anti-inflammatory (due to inhibition of ACE-I and other enzymes) and anti-cancer benefits, prevention of type-2 diabetes through inhibition of dipeptidyl peptidase IV (DPP-IV), bone and dental strength, antimicrobial and immunomodulatory effects and several others. Peptides have also reported health benefits in the treatment of asthma, neuropathic pain, HIV and wound healing. However, the structure, amino acid composition and length of these peptides, along with the quantity of peptide that can pass through the gastrointestinal tract and often the blood-brain barrier (BBB), intact and reach the target organ, are important for the realisation of these health effects in an in vivo setting. This paper aims to collate recent important research concerning the generation and detection of peptides in the laboratory. It discusses products currently available as preventative healthcare peptide options and relevant legislation barriers to place a food peptide product on the market. The review also highlights useful in silico computer- based methods and analysis that may be used to generate specific peptide sequences from proteins whose amino acid sequences are known and also to determine if the peptides generated are unique and bioactive. The topic of food-derived bioactive peptides for health is of great interest to scientific research and industry due to evolving drivers in food product innovation, including health and wellness for the elderly, infant nutrition and optimum nutrition for sports athletes and the humanisation of pets. This paper provides an overview of what is required to generate bioactive peptide containing hydrolysates, what methods should be used in order to characterise the beneficial health effects of these hydrolysates and the active peptide sequences, potential applications of bioactive peptides and legislative requirements in Europe and the United States. It also highlights success stories and barriers to the development of peptide-containing food products that currently exist.
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Hidayah, Nur, and Sandy Ardiansyah. "The Potential of Bioactive Peptides from Animal Protein Sources as a Mental Health Problems Prevention." AGRITROPICA : Journal of Agricultural Sciences 4, no. 2 (December 28, 2021): 114–21. http://dx.doi.org/10.31186/j.agritropica.4.2.114-121.
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Protein is one of the substances of nutrition macro that is needed by the body are known to contain bioactive peptides. Protein sources can be from vegetables and animals, based on research an animal protein sources more complete, balanced, easily digested and absorbed than vegetable protein sources. Some sources of animal protein (milk, eggs, meat, and products derived and processed) were reported that contain of bioactive peptides. Bioactive peptide has effect as antimicrobial, antithrombotic, antihypertensive, opioid, immunomodulatory, binder minerals, antioxidants, and prevent mental health disorder. The purpose of this paper is to review the peptide bioactive, relationship of mental health with peptide bioactive, and prevention of mental helath problems with bioactive peptide from animal protein sources. Peptides bioactive is an organic substance that is formed by amino acids (2-30 pieces) with the bond of the peptide and the weight of the molecule is small (unit Dalton). Mental health is the condition of the welfare (well-being) of an individual that is aware of its ability to own, can cope with the pressure of life which is normal, can work in a productive and can give a contribution to the community. Peptides bioactive shows such as opioids and inhibit the activity of the enzyme prolyl endopeptidase (PEP, EC 3.4.21.26) that play a role important in the treatment of disorders of the mind because work on the system nerve central (CNS) and can give the effect of a positive on motivation, behavior, stress, control the intake of food or the perception of the sense of pain. Some proteins of animal that has been proven to be able to prevent mental health problems namely, bovine, yogurt, and fresh milk. Still a lot of opportunities in the business of exploration of the source of the protein animal in producing the product peptide bioactive for commercial.
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Nurdiani, Rahmi, Todor Vasiljevic, Tanoj K. Singh, Osaana N. Donkor, Asep A. Prihanto, and Titis S. Kusuma. "Stability of an anticancer peptide isolated from Flathead by-products during in vitro gastrointestinal digestion." Functional Foods in Health and Disease 12, no. 4 (April 29, 2022): 198. http://dx.doi.org/10.31989/ffhd.v12i4.904.
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Background: Several peptides from seafood have shown effective anticancer activities. Nonetheless, one of the most significant challenges in developing fish peptides as functional food ingredients is proving their efficacy as anticancer agents. This study was aimed to evaluate the anticancer capacity and stability of a purified peptide (H. Met-Gly-Pro-Pro-Gly-Leu-Ala-Gly-Ala-Pro-Gly-Glu-Ala-Gly-Arg.OH) during a simulated gastrointestinal (GI) digestion.Methods: The anticancer activity of the peptide(s) before, during, and after GI digestion was analyzed against colon cancer cells (HT-29). Changes in cell morphology were assessed using an inverted microscope, while the degree of apoptosis was observed using a Muse Cell Analyzer.Results: Results showed little or no hydrolysis of the bioactive peptide by pepsin was observed, indicating the peptide was resistant to digestion in gastric conditions. The growth of HT-29 cells was significantly inhibited (P < 0.05) by the un-digested peptide and peptide(s) present in the digesta that was yielded by gastric and gastrointestinal digestion up to 28.89%, 29.68%, and 38.3%, respectively. HT-29 cells treated with pepsin and pancreatin digested peptides showed the highest cell death (3.54±2.30%).Conclusion: Overall, the findings showed that the purified peptide has the potency to be used in cancer therapy via oral administration and/or incorporation in food(s) applications for the treatment of specific cancer.Keywords: bioactive peptide; digestion; fish by-products; hydrolysis
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Chelliah, Ramachandran, Shuai Wei, Eric Banan-Mwine Daliri, Fazle Elahi, Su-Jung Yeon, Akanksha Tyagi, Shucheng Liu, Inamul Hasan Madar, Ghazala Sultan, and Deog-Hwan Oh. "The Role of Bioactive Peptides in Diabetes and Obesity." Foods 10, no. 9 (September 18, 2021): 2220. http://dx.doi.org/10.3390/foods10092220.
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Bioactive peptides are present in most soy products and eggs and have essential protective functions. Infection is a core feature of innate immunity that affects blood pressure and the glucose level, and ageing can be delayed by killing senescent cells. Food also encrypts bioactive peptides and protein sequences produced through proteolysis or food processing. Unique food protein fragments can improve human health and avoid metabolic diseases, inflammation, hypertension, obesity, and diabetes mellitus. This review focuses on drug targets and fundamental mechanisms of bioactive peptides on metabolic syndromes, namely obesity and type 2 diabetes, to provide new ideas and knowledge on the ability of bioactive peptide to control metabolic syndromes.
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Li, Xiangyang, Manli Guo, Jingtian Chi, and Jiangang Ma. "Bioactive Peptides from Walnut Residue Protein." Molecules 25, no. 6 (March 12, 2020): 1285. http://dx.doi.org/10.3390/molecules25061285.
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Walnut residue is a kind of high-quality plant protein resource. The bioactive peptide prepared from walnut residue has excellent health care functions such as antioxidation and antihypertensive activity, but at present, walnut residue is often regarded as waste or low value feed, fertilizer and other materials. The uneconomical use of walnut residue has hindered the development of the walnut industry to some extent. Effective utilization of walnut residue protein to develop bioactive peptides and other products is of great significance to realize the comprehensive utilization of walnut residue, improve the added value of by-products, and change the current low utilization rate of walnut residue. In this paper, the preparation, purification and structure identification of walnut protein bioactive peptides are reviewed, and different functional walnut active peptides (WBPs) are introduced. The potential effects of these bioactivities on human health and their different uses in food, medicine and other industries are discussed. The purpose is to provide reference information for the effective utilization of walnut residue resources and the development of walnut industry.
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Aluko, Rotimi E. "Determination of Nutritional and Bioactive Properties of Peptides in Enzymatic Pea, Chickpea, and Mung Bean Protein Hydrolysates." Journal of AOAC INTERNATIONAL 91, no. 4 (July 1, 2008): 947–56. http://dx.doi.org/10.1093/jaoac/91.4.947.
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Abstract Within the primary structure of many pea and mung bean proteins are peptide sequences that can potentially be used in the formulation of therapeutic products for the treatment and prevention of human diseases. However, these peptide sequences need protease treatments before they can be released free of the parent proteins. Unlike chemical hydrolysis, enzymatic treatment enables more efficient tailoring of peptide products without formation of toxic by-products or destruction of amino acids. This review provides information on current methods that have been used to convert inactive pea and mung bean proteins into bioactive peptides. It focuses on 3 main bioactive properties, such as inhibitions of (1) angiotensin converting enzyme (ACE) activity; (2) calmodulin (CaM)-dependent enzymes; and (3) copper-chelating activity. ACE is an established marker for hypertension, high levels of some CaM-dependent enzymes are risk factors for various human diseases including cancer and Alzheimer's disease, and high vascular copper concentrations may potentiate atherosclerosis. Also reviewed are the production and evaluation of activity of hypoallergenic peptides that may offer protection against anaphylactic reactions. The 3 main proteins discussed are chickpea, mung bean, and field pea.
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Hubrich, Florian, Alessandro Lotti, Thomas A. Scott, and Jörn Piel. "Uncovering Novel Peptide Chemistry from Bacterial Natural Products." CHIMIA International Journal for Chemistry 75, no. 6 (June 30, 2021): 543–47. http://dx.doi.org/10.2533/chimia.2021.543.
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Nature has evolved a remarkable array of biosynthetic enzymes that install diverse chemistries into natural products (NPs), bestowing them with a range of important biological properties that are of considerable therapeutic value. This is epitomized by the ribosomally synthesized and post-translationally modified peptides (RiPPs), a class of peptide natural products that undergo extensive post-translational modifications to produce structurally diverse bioactive peptides. In this review, we provide an overview of our research into the proteusin RiPP family, describing characterized members and the maturation enzymes responsible for their unique chemical structures and biological activities. The diverse enzymology identified in the first two proteusin pathways highlights the enormous potential of the RiPP class for new lead structures and novel pharmacophore-installing maturases as biocatalytic tools for drug discovery efforts.
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Caliceti, C., A. L. Capriotti, D. Calabria, F. Bonvicini, R. Zenezini Chiozzi, C. M. Montone, S. Piovesana, et al. "Peptides from Cauliflower By-Products, Obtained by an Efficient, Ecosustainable, and Semi-Industrial Method, Exert Protective Effects on Endothelial Function." Oxidative Medicine and Cellular Longevity 2019 (February 6, 2019): 1–13. http://dx.doi.org/10.1155/2019/1046504.
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The large amount of cauliflower industry waste represents an unexplored source of bioactive compounds. In this work, peptide hydrolysates from cauliflower leaves were characterized by combined bioanalytical approaches. Twelve peptide fractions were studied to evaluate unexplored biological activities by effect-based cellular bioassays. A potent inhibition of intracellular xanthine oxidase activity was observed in human vascular endothelial cells treated with one fraction, with an IC50 = 8.3±0.6 μg/ml. A different fraction significantly induced the antioxidant enzyme superoxide dismutase 1 and decreased the tumor necrosis factor α-induced VCAM-1 expression, thus leading to a significant improvement in the viability of human vascular endothelial cells. Shotgun peptidomics and bioinformatics were used to retrieve the most probable bioactive peptide sequences. Our study shows that peptides from cauliflower waste should be recycled for producing valuable products useful for the prevention of endothelial dysfunction linked to atherogenesis progression.
Dissertations / Theses on the topic "Bioactive Peptide Products"
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Hong, Hanna [Verfasser], Tobias A. M. [Akademischer Betreuer] [Gutachter] Gulder, and Kathrin [Gutachter] Lang. "Total Synthesis of Novel Bioactive Cyclic Peptide Natural Products / Hanna Hong ; Gutachter: Tobias A. M. Gulder, Kathrin Lang ; Betreuer: Tobias A. M. Gulder." München : Universitätsbibliothek der TU München, 2016. http://d-nb.info/1132248590/34.
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El, Marrouni El Ghazaoui Abdellatif. "Synthesis of unusual alpha-amino acids and study of the effect of their incorporation into antimicrobial peptides. Total synthesis of biactive marine natural products and analogues thereof." Doctoral thesis, Universitat de Girona, 2012. http://hdl.handle.net/10803/80815.
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The principle theme of this thesis was the synthesis of bioactive compounds. To this end, this work was focus on two main projects. The first one, which was carried out in the Department of Chemistry of the University of Girona under the supervision of Dr Montserrat Heras, concerned the synthesis of new unnatural amino acids bearing a pyrimidine ring within their side chain for incorporation into the antimicrobial peptide BP100 following a rational design in order to improve its biological profile. On the other hand, the second chapter of this thesis was developed in collaboration with the Laboratoire de Chimie Organique (ESPCI-ParisTech, Paris, France) under the guidance of Pr Janine Cossy and Dr Arseniyadis. This chapter was centered on the total synthesis of three marine natural products with complex structures and interesting biological activities: acremolide B, (–) bitungolide F and lyngbouilloside.Aquesta tesi s'ha centrat en la preparació de nous compostos bioactius seguint dues estratègies diferents. El primer projecte es va portar a terme sota la supervisió de la Dra. Montserrat Heras del grup LIPPSO del Departament de Química i ha permés el desenvolupament de noves metodologies per la síntesi de nous aminoàcids no naturals. i el seu ús en la preparació d'anàlegs del pèptid antimicrobià BP100 amb l'objectiu de millorar-ne les propietats biològiques. El segon projecte és fruit de la col•laboració amb la Prof. Janine Cossy i el Dr. Stellios Arseniyadis del "Laboratoire de Chimie Organique" de l'Ecole Superieur de Physique et Chimie Industrielles (ESPCI-ParisTech, Paris, França). I ha permés posar a punt tres estratègies sintètiques convergents i versàtils per l’obtenció de tres productes naturals de gran complexitat estructural i interessants activitats biològiques – l'acremolide B, la bitungolide F i la lyngbouilloside – aïllats recentment del fons marí de diferents punts del món.
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PAN, CHENGQIAN. "Discovery of Novel Bioactive Compounds from a Rare Actinomycete Amycolatopsis sp. 26-4." Kyoto University, 2020. http://hdl.handle.net/2433/259019.
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Jacques, Isabelle. "Découverte et déchiffrage de nouvelles voies de biosynthèse dépendant des synthases de cyclodipeptides : les clés d’une diversité accrue de dicétopipérazines potentiellement bioactives." Thesis, Paris 11, 2015. http://www.theses.fr/2015PA114838/document.
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Malgré l’intérêt et la diversité des propriétés pharmacologiques des 2,5-dicétopipérazines (DKP), les voies de biosynthèse de ces molécules d’origine microbienne sont très peu connues. L’objectif de mes travaux de thèse a été i) de documenter de nouvelles voies de biosynthèse de DKP qui se caractérisent par la présence d’une synthase de cyclodipeptides (CDPS) travaillant souvent de concert avec une ou plusieurs enzymes de modification des cyclodipeptides et ii) d’explorer la diversité chimique codée par ces voies. Dans un premier temps, je me suis intéressée aux CDPS. Après la sélection par bioinformatique de candidats dans les bases de données génomiques, j’ai pu identifier 51 nouvelles CDPS actives et montrer que ces enzymes peuvent incorporer 17 des 20 acides aminés naturels. Par ailleurs, ce travail a permis de mieux caractériser la famille des CDPS, de définir l’existence de plusieurs sous-familles aux signatures fonctionnelles spécifiques et d’établir les premiers éléments d’un code de spécificité pour la synthèse de cyclodipeptides. Dans un second temps, je me suis attachée à caractériser les enzymes de modification associées aux nouvelles CDPS et, en particulier, les dioxygénases dépendant du Fe(II) et du 2-oxoglutarate (OG) qui sont très représentées dans ces voies. J’ai ainsi pu détecter une activité in vivo pour 11 OG et poursuivre la caractérisation in vitro pour l’une de ces OG, ce qui a permis de caractériser les DKP qu’elle synthétise et d’ainsi montrer la complexité des modifications chimiques introduites. L’ensemble de ces travaux a donc permis d’identifier et de caractériser de nouvelles voies de biosynthèse qui donnent accès à une diversité accrue de DKPDespite the interest and diversity of the pharmacological properties of 2,5-diketopiperazines (DKPs), the biosynthetic pathways of these microbial molecules are poorly documented. The aim of my doctoral work was i) to identify new DKP biosynthetic pathways that are characterized by the presence of a cyclodipeptide synthase (CDPS) often associated with one or more cyclodipeptide-tailoring enzymes and ii) to explore the chemical diversity encoded by these pathways. First of all, my study focused on CDPSs. After the bioinformatics-based selection of candidates, 51 novel CDPS were characterized, revealing the incorporation of 17 of the 20 proteinogenic amino acids. Moreover, this work has allowed a better characterization of the CDPS family, by showing the existence of several subfamilies with specific functional signatures and laying the foundations of a specificity conferring code for the synthesis of cyclodipeptides. Second, I characterized the tailoring enzymes associated with the newly identified CDPSs and, in particular, the Fe(II) and oxoglutarate dependent dioxygenases (OGs) that are highly represented in these pathways. I detected the in vivo activity for 11 OGs and characterized the in vitro activity for one of them, showing the complexity of the chemical modifications introduced into the cyclodipeptide. This work has led to identify and characterize novel biosynthetic pathways that provide access to a greater diversity of DKPs
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Sion, Ludivine. "Bio production à l’échelle pilote d’un hydrolysat peptidique à partir de sang entier bovin et porcin pour l’industrie du Petfood et l’alimentation animale : Identification et caractérisation des peptides actifs." Thesis, Lille, 2019. http://www.theses.fr/2019LIL1R023.
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Le sang brut issu des abattoirs est une source importante de protéines. Il est actuellement peu valorisé, essentiellement par séchage ou par récupération de molécules plasmatiques après séparation centrifuge du plasma et du cruor. Ce co-produit est principalement composé d’hémoglobine, protéine riche en peptides actifs, tels que les peptides antimicrobiens, après hydrolyse par la pepsine porcine. L’objectif est de proposer une nouvelle stratégie de valorisation du sang, sans séparation plasma-cruor, tout en conservant les peptides bioactifs historiquement identifiés lors de l’hydrolyse pepsique de l’hémoglobine purifiée. Cette nouvelle voie, mise au point puis optimisée à l’échelle laboratoire, a été technologiquement transférée à l’échelle pilote. L’hydrolyse pepsique du sang a été premièrement mise au point à la concentration de 1% (p/v) en hémoglobine. Cette hydrolyse a mis en évidence la coexistence des mécanismes enzymatiques de type zipper et one-by-one pour l’apparition de la population peptidique. Les conditions d’hydrolyses (concentration en hémoglobine, choix de la pepsine, rapport enzyme-substrat, acide et temps d’hydrolyse) ont été optimisées en fixant une décoloration complète de l’hydrolysat ainsi que la conservation de la population peptidique. L’hydrolysat bioactif ainsi obtenu présente des propriétés antimicrobiennes et antioxydantes. Son analyse par spectrométrie de masse a permis la caractérisation de cet hydrolysat en terme de peptides issus de l’hémoglobine. Il ne possède aucune masse supérieure à 10 kDa, lui procurant ainsi une bonne digestibilité: son utilisation en alimentation animale en tant que complément alimentaire apparaît prometteuseRaw blood from slaughterhouses is an important source of proteins. This co-product, currently undervalued, is mainly composed of hemoglobin, a protein rich in active peptides such as antimicrobial peptides, after hydrolysis by porcine pepsin.The aim of this thesis is to propose a new strategy for the valorization of whole blood, without plasma-cruor separation. Preservation of identified bioactive peptides by pepsic hydrolysis of purified hemoglobin is required. This new way of blood valorization, developed and then optimized at laboratory scale, has been technologically transferred on a pilot scale (80 L).The pepsic hydrolysis of 70% bovine 30% porcine blood was first developed at 1% (w/v) of hemoglobin (23°C, 200 mL). This hydrolysis has demonstrated the coexistence of zipper and one by one enzymatic mechanism for the appearance of the peptide population. Hydrolysis parameters (hemoglobin concentration, industrial grade pepsin, enzyme-substrate proportion, acid allowing the sustainability of the hydrolysis pH and hydrolysis time) were optimized by fixing a complete discoloration of the hydrolysate as well as the preservation of the peptide population.The bioactive hydrolysate thus obtained contains antimicrobial and antioxidant properties. Mass spectrometry analysis has shown the hydrolysate composition in terms of peptides derived from hemoglobin. No mass above 10 kDa have been found, providing it with a good digestibility: its use in pet food as a food supplement seems promising
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Kobbi, Sabrine. "Purification de la RuBisCO à partir de la Luzerne, hydrolyse enzymatique, identification, structure-fonction des peptides bioactifs et leur valorisation dans des produits alimentaires." Thesis, Lille 1, 2017. http://www.theses.fr/2017LIL10201.
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La luzerne est la plante la plus cultivée dans le monde et est une excellente source de protéines. Cependant, la RuBisCO a montré le plus d'intérêt. Cette protéine a été étiquetée comme la protéine la plus abondante sur terre, elle constitue environ 65% (p/p) des protéines solubles de la luzerne. Dans ce travail une nouvelle méthode a été mise en place pour la purification de la RuBisCO à partir de la poudre de luzerne 10% (p/v) en utilisant deux solvants différents et l’effet du pH. Premièrement, des méthodes d’analyse qualitative et quantitative ont été utilisées pour confirmer l’efficacité de la méthode de purification qui pourrait remplacer certains procédés industriels classiques. Puis, une hydrolyse pepsique a été réalisée sur la RuBisCO purifiée qui aboutit à une forte population peptidique bioactive. Les peptides finaux de 24h d’hydrolyse ont montré une meilleure activité antibactérienne ou antioxydante par rapport aux autres hydrolysats. 9 nouveaux peptides antibactériens ont été identifiés et caractérisés par SM et qui ont un CMI entre 2-6mM contre quatre espèces de bactéries: B subtilis, E coli, L innocua et M luteus. En plus, des fractions peptidiques antioxydantes ont également été identifiées dans ce travail. Et leur activité antioxydante a été évaluée par différents tests in vitro et in vivo sur l’huile de Colza. Enfin, l’addition du peptide RDRFL issu de l’hydrolyse pepsique de la RuBisCO a montré un effet positif sur la prolongation de la durée de conservation de la viande hachée et de la purée de tomateAlfalfa is an excellent source of protein. However, RuBisCO proteins showed most interest. Indeed, this protein has been labelled the most abundant on earth; it constitutes about 65% (w/w) of soluble leaf protein of Alfalfa. In this work, a new method was introduced for the purification of RuBisCO from alfalfa powder 10% (w /v), using two different solvents and pH effect. In a first step, the performance of the proposed RuBisCO recovery method was evaluated through qualitative and quantitative analysis and the results obtained showed that this new method could replace some conventional industrial processes. In a second step, enzymatic hydrolysis was carried out on the purified RuBisCO, which resulted in a large bioactive peptide population. The final peptides after 24h of hydrolysis showed better antibacterial or antioxidant activity compared to the other peptide hydrolysates. Nine new antibacterial peptides have been identified and characterized by MS and have a MIC of 2-6 mM against four species of bacteria: B subtilis, E coli, L innocua and M luteus. In addition, antioxidants peptide fractions were identified in this work, their antioxidant activity was evaluated by various in vitro and in vivo tests on oil of Colza. Finally, the addition of peptide RDRFL derived from the peptic hydrolysis of RuBisCO has a positive effect on the prolongation of the shelf life of minced meat and of tomato puree
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Henaux, Loïc. "Fractionnement d’un hydrolysat de protéines de saumon par électrodialyse avec empilement de membranes d’ultrafiltration afin de concentrer, isoler et identifier des peptides glucorégulateurs." Doctoral thesis, Université Laval, 2019. http://hdl.handle.net/20.500.11794/66671.
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Le diabète de type 2 (DT2) est un trouble multifactoriel complexe de l’homéostasie du glucose. Cette maladie, bien qu’elle possède une composante génétique, est principalement induite par des causes socio-environnementales comme de mauvaises habitudes alimentaires. En dépit des mesures hygiéno-diététiques et des traitements médicaux utilisés pour prévenir et traiter la maladie, le DT2 ne cesse de progresser. L’identification et la production de peptides bioactifs à partir de sources naturelles offrent une alternative intéressante aux médicaments de synthèse, dont les préoccupations concernant les effets secondaires ne cessent d’augmenter. Ainsi, en raison de leur abondance et leur richesse en molécule bioactive, les coproduits de la transformation du poisson offrent une source presque inépuisable de peptides bioactifs. En effet, lors d’études précédentes, il a été démontré que des protéines de morue et de saumon permettaient d’améliorer la santé cardio-métabolique in vivo, et d’améliorer la captation du glucose musculaire, de diminuer la production du glucose hépatique et l’inflammation. De plus, avec un nombre de plus en plus important d’individus à nourrir, l’industrie de la transformation doit augmenter sa production, et les déchets ne cessent de s’accumuler. Néanmoins, afin d’exercer leur effet bioactif, il est nécessaire de libérer ces peptides bioactifs des structures protéiques au sein desquelles ils sont imbriqués et sous forme inactive générant ainsi des hydrolysats complexes. Par la suite, une ou plusieurs étapes de séparation sont utilisées afin de concentrer ces peptides dans des fractions plus actives, par exemple en fractionnant ces hydrolysats complexes par électrodialyse avec membranes d’ultrafiltration. En effet, Il a été démontré l’efficacité de l’électrodialyse avec membranes d’ultrafiltration pour la génération de fractions améliorant, in vitro, la captation du glucose à partir d’hydrolysats de protéines de soya et de saumon. Ainsi, l’objectif principal de cette thèse était de concentrer et d’identifier des peptides bioactifs par le fractionnement d’un hydrolysat de protéines issu d’un coproduit de saumon iv par l’électrodialyse avec membranes d’ultrafiltration, et d’étudier l’impact de ces fractions et peptides sur le DT2. Lors de la première étude, il a été démontré qu’un empilement judicieux de membranes permettait de fractionner les peptides issus d’un hydrolysat de coproduit de saumon, en générant des fractions possédant des peptides avec des propriétés physico-chimiques (charge et masse) différentes. De plus, cet empilement de trois membranes d’ultrafiltration de seuils de coupure différents a permis de moduler la réponse in vitro de la captation du glucose. En effet, des peptides cationiques de plus haut poids moléculaire ont amélioré la captation du glucose dans une étude in vitro, alors que les peptides cationiques de plus faible poids moléculaire ont démontré un effet inhibiteur de la bioactivité. Finalement, l’analyse par spectrométrie de masse des fractions a permis de caractériser (temps de rétention et charge) 17 peptides cationiques et 21 peptides anioniques, potentiellement responsables de l’effet bioactif des fractions. Lors de la deuxième étude, le fractionnement par EDUF des fractions finales récupérées lors de la précédente séparation et l’étude in vitro de la bioactivité de ces fractions (captation du glucose, production du glucose hépatique et inflammation) ont permis d’identifier deux fractions très prometteuses, démontrant un effet sur ces trois bioactivités. De plus, l’analyse par spectrométrie de masse en tandem de ces fractions a permis d’identifier, à l’aide de base de données, la séquence peptidique de 24 peptides anioniques, potentiellement responsables de ces effets bioactifs. Finalement, lors de la troisième étude, basées sur l’analyse des spectres obtenus par spectrométrie de masse en tandem, 13 peptides ont été sélectionnés et synthétisés, puis testés individuellement pour leurs capacités à augmenter l’absorption du glucose au niveau de cellules musculaires, à diminuer la production de glucose hépatique et finalement à diminuer la réponse inflammatoire de macrophages. Ainsi, pour la première fois, quatre nouveaux peptides ont été identifiés à partir de coproduits de saumon, et leurs propriétés glucorégulatrices in vitro ont été démontrées.Type 2 diabetes (T2DM) is a complex multifactorial disorder of glucose homeostasis. This disease has a genetic basis but is mainly caused by socio-environmental behaviours, such as overeating and a lack of physical activity. Despite dietary measures and medical treatments used to prevent and treat the disease, T2D continues to progress. The identification and production of bioactive peptides from natural sources offer an interesting alternative to synthetic drugs, whose concerns about side effects are constantly increasing. Thus, because of their abundance and richness in bioactive molecules, fish processing co-products offer an almost inexhaustible source of bioactive peptides. Indeed, in previous studies, cod and salmon proteins have been shown to improve cardio-metabolic health in in vivo studies, and to improve muscle glucose uptake, decrease hepatic glucose production, and inflammation. In addition, with a growing number of people to feed, the processing industry is at its height, and waste continues to accumulate. Nevertheless, in order to exert their bioactive effect, it is necessary to release these bioactive peptides from native proteins. Subsequently, one or more separation, using for example electrodialysis with ultrafiltration membranes, are needed to concentrate these peptides and generate bioactive fractions. Indeed, it was previously demonstrated the effectiveness of electrodialysis with ultrafiltration membranes to generate bioactive fractions, from complex matrices, able to improve the glucose uptake in vitro, from soy and salmon protein hydrolysates. In this context, the main objective of this thesis was to concentrate and identify bioactive peptides, by fractionating a protein hydrolysate from a salmon co-product, by electrodialysis with ultrafiltration membranes, and to study the impact of these fractions and peptides on T2D. In the first study, results demonstrated that a triple size selective separation by EDUF allowed to generate peptide fractions with different physicochemical properties (charge and mass). Moreover, it was demonstrated that such a separation allowed to modulate the in vitro response of the fractions for glucose metabolism. Indeed, from a single EDUF separation, cationic peptides with higher molecular weights were concentrated and demonstrated to enhance their glucose uptake capacity. Whereas, cationic peptides with lower molecular weights have decreased the glucose uptake capacity. In addition, analyses by mass spectrometry of the vi fractions allowed to characterize (retention time and charge) 17 cationic peptides and 21 anionic peptides, potentially responsible for the bioactive effect of the fractions. In a second study, a second EDUF fractionation, using as feed solution the final fractions recovered during the previous separation was performed. The selectivity of the process was confirmed by liquid chromatography-mass spectrometry analyses. Moreover, in vitro study of the bioactivities (glucose uptake, hepatic glucose production and inflammation) effect of these fractions, led to the identification of two very promising fractions, demonstrating a simultaneous effect on all three bioactivities tested. In addition, the tandem mass spectrometry analysis of these fractions allowed the sequence identification of 24 anionic peptides, potentially responsible for these bioactive effects. Finally, in a third study, based on the analysis of the spectra obtained by tandem mass spectrometry, 13 peptides were selected and synthesized, then individually tested for their ability to increase glucose uptake in muscle cells, to reduce glucose production by hepatic cells, and to decrease the inflammatory response of macrophages. Thus, for the first time, four new peptides identified from salmon by-products, demonstrated in vitro glucoregulatory properties.
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Hedhili, Karima. "L’hydrolyse pepsique de l’hémoglobine bovine pure ou dans le cruor bovin (un coproduit d’abattoir) : modélisation des cinétiques d’apparition des peptides antibactériens obtenus et étude de leur valorisation." Thesis, Lille 1, 2014. http://www.theses.fr/2014LIL10075/document.
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L'hydrolyse pepsique de l’hémoglobine bovine purifiée ou à partir d'un coproduit des abattoirs : le cruor, peut être considérée comme une voie importante d'obtention de peptides antibactériens. Une étude cinétique nous a permis de maîtriser cette hydrolyse et de déterminer un modèle mathématique capable de prédire la concentration de chaque peptides antibactériens des deux familles de peptides α 1-32 et α 107-141 et ceux pour un intervalle de température de 15-37°C, de pH de 3,5-5,5 et de rapport enzyme/substrat de 1/5-1/20. Le calcul des énergies d'activation pour les différentes réactions impliquées dans le mécanisme était effectué grâce à l’équation d’Arrhenius qui a permis d’étudier l’effet de la température sur les différents coefficients cinétiques. L’effet du pH et du rapport E/S était également étudié et le modèle trouvé a démontré une augmentation linéaire de la vitesse d’hydrolyse en diminuant le pH (entre 3,5 et 5,5) et une vitesse invariable avec le rapport E/S (1/5-1/20). L'étude de la relation structure-fonction des peptides antibactériens α 1-32 et α 137-141 a été effectuée grâce à un suivie de la cinétique de K+ extracellulaire en présence de Lisrea innocua et le déterminant antibactérien minimal a été déterminé pour le peptide α 137-141. La possibilité de valoriser les peptides antibactérien α 1-32 et α 137-141 dans un emballage bioactif pour la conservation des aliments contre le développement de bactéries pathogènes a été étudiée par l'adsorption de ces peptides en surface d'un film de polyéthylène basse densité, traité avec le plasma froidThe pepsin hydrolysis of purified bovine hemoglobin or from a co-product of slaughterhouses: cruor, can be considered as an important route for obtaining antibacterial peptides. A kinetic study has allowed us to control the hydrolysis and to determine a mathematical model able to predict the concentration of each antibacterial peptides of two families of peptides α 1-32 and α 107-141 and those of an interval of temperature 15-37°C, of pH 3,5-5,5 and ratio enzyme/substrate of 1/5-1/20 . The calculation of activation energies for the different reactions involved in the mechanism was made by the Arrhenius equation, which was used to study the effect of temperature on the various kinetic coefficients. The effect of pH and ratio E / S was also studied and the model found showed a linear increase in the rate of hydrolysis decreasing the pH ( between 3,5 and 5,5 ) and an invariable speed with the ratio E / S ( 1/5-1/20 ). The study of the structure-function relationship of antibacterial peptides α 1-32 and α 137-141 was carried out thanks to a followed the kinetics of extracellular K + in the presence of Lisrea innocua and the minimal determinant antibacterial was determined for the peptide α 137-141. The possibility to recovery the antibacterial peptides α 1-32 and α 137-141 in to a bioactive food packaging against the growth of pathogenic bacteria has been studied by the adsorption of these peptides on the surface of a low density polyethylene film treated with cold plasma
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Durand, Rachel. "Valorisation d'hydrolysat de poisson pour la santé humaine : séparation des composés bioactifs par électrodialyse avec membranes d'ultrafiltration et évaluation de leurs activités biologiques impliquées dans le développement du syndrome métabolique." Doctoral thesis, Université Laval, 2019. http://hdl.handle.net/20.500.11794/66672.
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La valorisation des co-produits de poisson est un enjeu économique et environnemental. Depuis plusieurs années, des recherches ont montré que les co-produits de poisson contenaient des molécules actives pour la santé humaine comme des acides gras polyinsaturés et des peptides bioactifs. L’objectif principal de cette thèse était d’évaluer l’utilisation potentielle d’hydrolysats de laitance de hareng pour l’amélioration de la santé humaine, spécifiquement en agissant positivement sur certaines fonctions physiologiques associées au syndrome métabolique, et l’effet de leur séparation par électrodialyse avec membranes d’ultrafiltration (EDUF) sur la production de fractions bioactives. Dans un premier temps, il a été démontré qu’une supplémentation avec différents hydrolysats de laitance de hareng d’une diète riche en gras et en sucre chez des souris permettait de moduler certains paramètres physiologiques impliqués dans le développement du syndrome métaboliques (MetS) : amélioration de la tolérance au glucose, augmentation de l’apport énergétique total et protection de la population de Lactobacillus dans le microbiote intestinal. De plus, les hydrolysats ont aussi montré des activités antiinflammatoires in vitro à des concentrations de 1ng/ml et 100pg/ml. Dans un second temps, la faisabilité d’une séparation par EDUF de deux hydrolysats de laitance de hareng différents a été évaluée : le premier plus complexe était un mélange de molécules (lipides, acides nucléiques, peptides, acides aminés libres), alors que le second était principalement composé de peptides et d’acides aminés libres. Une nouvelle configuration utilisant quatre membranes d’ultrafiltrations (deux de 50kDa et deux de 20kDa) a permis un double fractionnement simultané des composés anioniques et cationiques en seulement une étape. Il a d’abord été montré que seuls les peptides chargés ainsi que les acides aminés libres pouvaient être séparés par EDUF alors que les lipides et les acides nucléiques ne migraient pas dans les fractions de récupérations. De plus, l’utilisation de membranes présentant deux tailles de pores distinctes a permis le fractionnement des hydrolysats en différentes classes de poids moléculaires. En effet, l’utilisation de membranes de 20kDa a permis la concentration de peptides de faibles poids moléculaires (< 600Da) et IV d’acides aminés libres, alors que les populations peptidiques des fractions obtenues avec les membranes de 50kDa présentaient des poids moléculaires supérieurs et plus variés. Dans un troisième temps, les bioactivités des fractions de récupérations et des hydrolysats de laitance de hareng ont été évaluées in vitro. Ainsi, la séparation du premier hydrolysat a permis l’obtention d’une fraction finale stimulant la captation du glucose in vitro et d’une fraction anionique antioxydante. Le fractionnement du second hydrolysat a permis quant à lui la production de deux fractions cationiques anti-inflammatoires ainsi que l’identification subséquente de deux séquences peptidiques bioactives. L’ensemble de cette thèse a donc démontré que les hydrolysats de laitance de hareng contenaient des composés actifs, comme des acides gras polyinsaturés et des peptides, modulant positivement certains paramètres physiologiques impliqués dans le MetS et pouvant ainsi permettre la diminution de son occurrence. De plus, la séparation des hydrolysats par EDUF a permis la production de fractions bioactives ainsi que l’identification de deux nouvelles séquences peptidiques anti-inflammatoires (IVPAS et FDKPVSPLL). Ces travaux ont démontré l’effet bénéfique pour la santé humaine des hydrolysats de laitance de hareng et de ses fractions, permettant d’envisager une valorisation plus efficace de ces coproduits de poisson par les industries de transformation dans les secteurs liés à la santé humaine.Fish by-product valorization is an economic and environmental issue. For several years, scientific researches have shown that fish by-products contained active molecules for human health, as polyunsaturated fatty acids and peptides. The aim of this thesis was to evaluate the potential use of herring milt hydrolysates for human health, especially by evaluating their potential actions in physiological parameters involved in the metabolic syndrome and the effect of their separation by electrodialysis with ultrafiltration membrane (EDUF) for the production of bioactive fractions. First, we have demonstrated that the supplementation of three different herring milt hydrolysates in a high fat high sucrose diet in mice was able to modulate some physiological functions involved in the metabolic syndrome: improvement of glucose tolerance, increase of the total energy intake and protection against the Lactobacillus disappearance in the gut microbiota. Moreover, the hydrolysates decreased the inflammation induction in macrophages stimulated with LPS at 1ng/ml and 100pg/ml. Secondly, we have evaluated the separation of two herring milt hydrolysates by EDUF: the first one was more complex with a mix of different molecules (lipids, nucleic acids and peptides) while the second one was mainly composed of peptides. A new configuration using four ultrafiltration membranes (two of 50kDa and two of 20kDa) allowed a simultaneous double separation of anionic and cationic compounds. It has been shown that only charged peptides and free amino acids were fractionated in EDUF, while the lipids and nucleic acids didn’t migrate to the recovery fractions. Moreover, the use of membranes with different cut-off allowed a separation of the hydrolysates in different molecular weight ranges. Indeed, the use of 20kDa membranes allowed the concentration of peptides with small molecular weights (<800Da) and free amino acids, while the recovery fractions obtained with the 50kDa membranes were composed oh peptide with higher molecular weights.Thirdly, the potential bioactivities of the recovery fractions and the herring milthydrolysates were evaluated in vitro. Hence, the separation of the first hydrolysate allowed the production of a final fraction increasing the glucose uptake and an antioxidant anionicfraction. While the separation of the second hydrolysate allowed the production of two antiinflammatory cationic fractions as well as the identification of two bioactive peptides sequences. All these results showed that milt herring hydrolysate contained bioactive compounds such as polyunsaturated fatty acids and peptides, improving some physiological functions involved in the MetS and may decrease its occurrence. More over, the separation of the hydrolysates by EDUF allowed the production of bioactive fractions and the identification of two new anti-inflammatory peptide sequences. This work demonstrated the existence of a beneficial effect of herring milt hydrolysate and its fractions for the human health, allowing a better valorization of this by-product of the food industry for the health sector.
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Petrov, Ravil Rashitovich. "Part I. Application of 2-Hydroxymethylacrylic Acid, a Product of Baylis-Hillman Reaction, for the Synthesis of Novel N-backbone-to-Side-Chain Cyclic Peptide Analogs: Strategies and Side Reactions Part II. Synthesis and Biological Activities of Chimeric Bioactive Peptides Featuring Amino Acids Coupled to 4-Anilino-N-Phenethyl-Piperidine." Diss., The University of Arizona, 2007. http://hdl.handle.net/10150/194330.
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During my research career in Prof. V.J.Hruby's laboratory I worked on two different projects. The first project, which was initiated by the author, was planned to serve the need of our laboratory for a novel method of peptide cyclization. This method was planned to use recent advances in Pd0-catalyzed asymmetric synthesis combined with the structural richness offered by the Baylis-Hillman chemistry which could open new ways to diverse areas of drug design, molecular immunology and chemotherapy. This approach would provide cyclic peptides featuring N-alkylated amino acids that would confer high resistance to degradation by proteases. Because of numerous synthetic problems imposed, this strategy was not of considerable current use in peptide synthesis, especially on solid supports. However, despite a substantial amount of effort invested, this method faced serious drawbacks such as multistep synthesis and side reactions when applied to solid supports. Moreover, recent introduction of microwave technology which has helped to solve a great number of problems has led to a renaissance in the classical lactam and thioester bond cyclizations which overshadowed our quest for a novel methodology. The second project was focused on application of 4-anilidopiperidines for the synthesis of chimeric bioactive peptides. It was an effort towards the development of novel analgesics with reduced toxicity and enhanced potency. This project linked small molecule and multimeric ligand designs that were ongoing in our laboratory at the time. Major accomplishments in this project were made possible by successful resolution of several research challenges. I was able to find a straightforward, convenient and economical approach for the synthesis of novel analogues on a solid support. These developments led to novel compounds which showed substantial increases in their binding affinity relative to corresponding opioid analogues. To illustrate, compounds PET25, 26, 27, 29, 30, 31, and 32 showed high bioactivity and sub-nanomolar binding affinity to opioid receptors. Most of the peptides generated in the second project are still being investigated for their biological activities by our colleagues at the Department of Pharmacology, but the results to date indicate that some highly potent novel compounds have been made.
Books on the topic "Bioactive Peptide Products"
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Camargo, Antonio C. M., Lilian Cruz, and Beatriz L. Fernandez. Bioactive Peptides Produced by Limited Proteolysis. Morgan & Claypool Life Science Publishers, 2012.
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Camargo, Antonio, and Emer Ferro. Bioactive Peptides Produced by Limited Proteolysis. Morgan & Claypool Life Science Publishers, 2012.
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Li, Yanyan, Sylvie Rebuffat, and Séverine Zirah. Lasso Peptides: Bacterial Strategies to Make and Maintain Bioactive Entangled Scaffolds. Springer, 2014.
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Li, Yanyan, Sylvie Rebuffat, and Séverine Zirah. Lasso Peptides: Bacterial Strategies to Make and Maintain Bioactive Entangled Scaffolds. Springer London, Limited, 2014.
Find full textBook chapters on the topic "Bioactive Peptide Products"
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Bockus, Andrew T., and R. Scott Lokey. "Bioactive and Membrane-Permeable Cyclic Peptide Natural Products." In Practical Medicinal Chemistry with Macrocycles, 101–32. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2017. http://dx.doi.org/10.1002/9781119092599.ch5.
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Harvey, Colin J. B., and Chaitan Khosla. "Precursor-Directed Biosynthesis of Polyketide and Nonribosomal Peptide Natural Products." In Modern Tools for the Synthesis of Complex Bioactive Molecules, 485–512. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2012. http://dx.doi.org/10.1002/9781118342886.ch14.
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Amorim, Fernanda Gobbi, Larissa Zambom Côco, Francielle Almeida Cordeiro, Bianca Prandi Campagnaro, and Rafaela Aires. "Dairy Products." In Bioactive Peptides from Food, 75–96. Boca Raton: CRC Press, 2022. http://dx.doi.org/10.1201/9781003106524-6.
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Azubuike-Osu, Sharon O., Flora-Glad C. Ekezie, Williams E. Ibegbunam, and Chibuike C. Udenigwe. "Allergic Effects of Bioactive Peptides Produced from Different Food Sources." In Bioactive Peptides, 363–93. First edition. | Boca Raton : CRC Press, 2021. | Series:: CRC Press, 2021. http://dx.doi.org/10.1201/9781003052777-17.
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Korhonen, Hannu J., and Pertti Marnila. "Milk Bioactive Proteins and Peptides." In Milk and Dairy Products in Human Nutrition, 148–71. Oxford: John Wiley & Sons, 2013. http://dx.doi.org/10.1002/9781118534168.ch8.
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Minj, Jagrani, Subrota Hati, Brij Pal Singh, and Shilpa Vij. "Biofunctional Yogurt and its Bioactive Peptides." In Engineering Practices for Milk Products, 135–75. Series statement: Innovations in agricultural and biological engineering: Apple Academic Press, 2019. http://dx.doi.org/10.1201/9780429264559-7.
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Fotie, Jean. "The Potential of Peptides and Depsipeptides from Terrestrial and Marine Organisms in the Fight against Human Protozoan Diseases." In Bioactive Natural Products, 279–320. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2015. http://dx.doi.org/10.1002/9783527684403.ch10.
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Le Gouic, Aurélien V., Pádraigín A. Harnedy, and Richard J. FitzGerald. "Bioactive Peptides from Fish Protein By-Products." In Bioactive Molecules in Food, 355–88. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-319-78030-6_29.
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Nourbakhsh, Himan, and Seid Mahdi Jafari. "Separation of Bioactive Peptides and Proteins from by-Products and Co-Products Through Membranes." In Food Bioactive Ingredients, 177–203. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-84643-5_6.
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Le Gouic, Aurélien V., Pádraigín A. Harnedy, and Richard J. FitzGerald. "Bioactive Peptides From Fish Protein By-Products." In Reference Series in Phytochemistry, 1–35. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-54528-8_29-1.
Full textConference papers on the topic "Bioactive Peptide Products"
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Reinoso, Zain Sanchez, Jacinthe Thibodeau, Laila Ben Said, Ismail Fliss, Laurent Bazinet, and Sergey Mikhaylin. "Bioactive Peptide Production from Slaughterhouse Blood Proteins: Impact of Pulsed Electric Fields and Ph on Enzyme Inactivation, Antimicrobial and Antioxidant Activities of Peptic Hydrolysates from Bovine and Porcine Hemoglobins." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/fsht2150.
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Slaughterhouse blood is a valuable by-product since multiple bioactive compounds can be derived out of it. Its solid fraction consists mainly of hemoglobin, which is a good source of antimicrobial and antioxidant peptides that can be released by peptic hydrolysis. Nevertheless, this method has limitations such as low yield, expensive cost of enzyme process, and non-eco-friendly production (high energy consumption and chemical reagents requested). Amount the alternative green technologies for protein valorization, pulsed electric field (PEF) stands out since it allows modifying the physicochemical properties of proteins, promoting the enzymatic hydrolysis, enzyme inactivation, and bioactivity enhancement. Thus, this study aimed to evaluate the effect of PEF on the pepsin inactivation and biological activities (antimicrobial and antioxidant) in hemoglobin hydrolysates. Bovine and porcine hemoglobins were hydrolyzed with pepsin for 3 h (37°C, pH 3.0) and treated with PEF (73 pulses, 23.8kV/cm, 90Hz) to inactivate the enzyme. The hydrolysis degree was evaluated, which did not show significant changes after PEF-inactivation of pepsin, whereas the peptide population analysis by RP-UPLC-MS/MS showed some changes in PEF-treated hydrolysates over time, which suggested a residual pepsin activity. Additionally, the impact of pH (3, 7, and 10) on bioactivity was studied. PEF-treatments did not show a significant impact on antimicrobial (antibacterial, antifungal, and anti-yeast activities) and antioxidant activities (DPPH and ORAC). However, higher pH fostered stronger anti-yeast activity (R. mucilaginosa) and DPPH‐scavenging capacity, whereas pH 7 fostered the antifungal activity (M. racemosus). Even though some changes were observed in the peptide population, no negative effects of PEF were found for biological activities. Thus, the utilization of hemoglobin from the meat industry combined with PEF-treatment fits the circular economy concept since derived peptides can be recycled to protect meat and other products against microbial growth and oxidation.
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Kumrungsee, Thanutchaporn, Norihisa Kato, Toshiro Matsui, and Yongshou Yang. "Plant and gut microbiota-derived protein metabolites and potential health functions." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/envt3719.
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Bioactive peptides can be obtained from protein hydrolysates through in vitro enzymatic hydrolysis, gastrointestinal digestion, and microbial fermentation. Recent emerging research suggests that prebiotic-stimulated gut microbiota also plays a role in generating bioactive peptides and amino acids in gut. In this study, we examined if enzymatic hydrolysis of soybean and wheat germ, plant materials often used in oil industry, can generate antihypertensive peptides and determined if prebiotic digestive enzymes can induce the production of gut microbiota-derived amino acids. In the first experiment, soybean and wheat germ were hydrolyzed by protease enzymes. Then, their hydrolysates were subjected to peptide isolation and identification. Identified peptides were subjected to test for their potential antihypertensive activities. For the second experiment, rodents were fed an Aspergillus-derived protease- or lipase-mixed diet for 2 weeks. Then, cecum contents were collected for bacteria and metabolite analyses. As a result, we found that His-Gly-Lys from soybean hydrolysate strongly inhibited angiotensin II-induced elevated intracellular Ca2+ concentration in vascular smooth muscle cells (VSMCs). Trp-Val and Trp-Ile from wheat germ hydrolysate were found to inhibit Ca2+-calmodulin (CaM)-dependent protein kinase II (CaMK II), a protein kinase promoting hypertension by inducing Ca2+ influx into VSMCs, in rat thoracic aorta rings. These findings suggest the potential of the plant-derived peptides in preventing hypertension and vascular-related diseases. In the second experiment, we found that the dietary protease and lipase increased Bifidobacterium and Lactobacillus probiotics and induced the production of probiotic-derived amino acids, taurine, ornithine, and γ-aminobutyric acid. Since these amino acids have versatile functions including in gut health modulation and brain functions, it can be hypothesized that the dietary prebiotic-digestive enzymes may be beneficial for gut health and brain functions. This study suggests the possibility of applying oil processing by-products in the production of functional food ingredients including bioactive peptides and amino acids.
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Toma, Agnes, Simona Savin, Teodora Ciucan, Elena Mihai, Catalina Sanda, Lucia Moldovan, and Anca Oancea. "Comparative Studies concerning Bioactive Peptides Obtained from Fish By-Products." In Priochem 2021. Basel Switzerland: MDPI, 2022. http://dx.doi.org/10.3390/chemproc2022007062.
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Jacobsen, Charlotte, Ann-Dorit Moltke Sorensen, and Dimitra Marinou. "Enzymatic production of antioxidative and antimicrobial hydrolysates from cod solid side-streams." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/qmqf3129.
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In the last decade, there has been an increased focus and interest in increasing the utilization of existing raw materials and reducing waste especially due to the increasing global population. In the cod filleting industry up to 60% (w/w) of the biomass end up as side-streams e.g., frame, head and gut, which are either used as low value products such as animal feed or are wasted. An example of animal feed is mink feed. However, in Denmark the mink production is closed due to COVID-19 and new utilization possibilities are needed. The cod side-stream used in this study is from Royal Greenland and is very fresh with the possibility of freezing right after production to maintain quality and increase shelf life before further production. Cod frames still contain meat after filleting and could be used as hydrolysates with bioactive properties such as antioxidative and/or antimicrobial activity for food or feed applications. Previous studies have shown that longer peptides (shorter hydrolysis time) potentially have antimicrobial properties and shorter peptides (longer hydrolysis time) have antioxidative properties. Therefore, an experiment was designed using three different types of proteases (Alcalase, Neutrase and Protamex) and different hydrolysis time (½h, 1, 2, 3 and 6h) to produce different hydrolysates. Produced hydrolysates were evaluated for their antioxidative and antimicrobial activities by in vitro antioxidant assay, radical scavenging (DPPH) and metal chelating activity, and by disc diffusion and minimal inhibitory concentration (MIC) assays, respectively. Furthermore, the hydrolysates were also characterized with respect to yield, protein content and degree of hydrolysis. The produced hydrolysates showed antioxidant properties. Highest DPPH activity was obtained with Protamex, where-as highest metal chelating activity surprisingly was obtained for a control (no enzyme added). Unfortunately, no antimicro-bial activity was detected for the produced hydrolysates independent of enzymes and hydrolysis time applied. BBI JU-funded WASEABI project.
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Shim, Youn Young, Clara Olivia, Xian-Guo Zou, Young Jun Kim, and Martin Reaney. "Stability of Novel Peptides (linusorbs) in Flaxseed Meal Fortified Gluten-free Bread." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/mfmf5716.
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Flaxseed meal is rich in water-soluble gums and, as such, can improve texture in gluten-free products. Flaxseed bioactive-antioxidant peptides, linusorbs (LOs, a.k.a. cyclolinopeptides), are a class of molecules that may contribute health-promoting effects. The effects of dough preparation, baking, and storage on flaxseed-derived LOs stability in doughs and baked products are unknown. Gluten-free (GF) bread dough and bread were prepared with flaxseed meal and the LO content was determined in the flaxseed meal, bread flour containing the flaxseed meal, bread dough, and bread. The LO content during storage (0, 1, 2, and 4 weeks) at different temperatures (−18 °C, 4 °C, and 22−23 °C) was determined by high-performance liquid chromatography-diode array detection (HPLC-DAD). The content of oxidized LOs like [1–9-NαC],[1(Rs,Ss)-MetO]-linusorb B2 (LO14) were substantially constant in flaxseed meal and flour produced from flaxseed meal under all conditions for up to four weeks. However, during GF-bread production LOs decreased. Due to microbial contamination dough could not be stored at either 4 or 21°C, and bread could only be stored for one week at 21°C. Up to four weeks of storage was possible for bread and dough at −18 °C and bread at 4 °C without the loss of LOs. The LOs change during processing and storage. The concentration of reduced LOs in flour and meal were much higher than measured in dough and bread. There was not a corresponding increase in oxidized LOs. The LOs in flaxseed meal-fortified bread were stable for products stored at low temperatures to preserve LOs. This study is the first of the impact of baking conditions on LOs content and quality.
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Varela, D., R. O’Hara, and A. C. Neves. "BY-PRODUCTS OF THE WHELK PROCESSING INDUSTRY AS VALUABLE SOURCE OF ANTIOXIDANT PEPTIDES." In World Conference on Waste Management. The International Institute of Knowledge Management, 2021. http://dx.doi.org/10.17501/26510251.2021.1103.
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The fish and shellfish industry processes 851,984 tonnes of fish per year worldwide. However, only 43% of that is consumed, and valuable proteins are processed as waste. Protein hydrolysates are widely used in food technology for their nutritional and functional properties. The goal of this project is to extract protein from whelk by-products derived from the shellfish processing industry and create protein hydrolysates that have marketable value. The by-products were divided into two types: raw (R) and cooked byproduct (C). The proteins were extracted using the pH shift method and quantified using the Bradford assay. It was possible to extract a maximum of 455 mg/g at a neutral pH, for which R had the highest protein yield. Proteins were also qualified using reverse phase high-performance liquid chromatography (RP-HPLC) that showed that R has more hydrophilic proteins while the C extracted protein showed more peaks in the hydrophobic phase. The Fourier-transform infrared spectroscopy (FTIR) indicated the presence of glutamine, tyrosine, and serine in the extracted proteins. Extracted proteins were then hydrolyzed using Alcalase and α-Chymotrypsin. It was possible to obtain higher degrees of hydrolysis (DH) using Alcalase. The hydrolysates were tested for antioxidant activity using the DPPH (2,2-diphenyl-1-picryl-hydrazyl-hydrate) free radical antioxidant assay. Alcalase hydrolysates showed to have overall lower IC50 for stabilization of the DPPH radical than α-Chymotrypsin, the lowest one being 13.92±1.57 µg/mL for the Alcalase hydrolyzed neutral proteins. The IC50 results obtained are significantly lower than the ones described in other studies using the same enzymes or other marine species. This can indicate that more heterogenous mixtures of by-product can originate extracted proteins that when hydrolyzed lead to higher radical scavenging activity, thus making shellfish industry by-product a sustainable and valuable source of antioxidant peptides. Keywords: Shellfish; Bioactive peptides; Protein extraction; Protein hydrolysates, Waste management, Nutraceuticals
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Senadheera, Tharindu, Deepika Dave, and Fereidoon Shahidi. "Integrated bioinformatics approach for identification of bioactive peptides from orange-footed (Cucumaria frondosa) sea cucumber hydrolysate by-products." In Virtual 2021 AOCS Annual Meeting & Expo. American Oil Chemists’ Society (AOCS), 2021. http://dx.doi.org/10.21748/am21.511.
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Ribeiro, A., C. Vilarinho, J. Araújo, and J. Carvalho. "Development of an Integrated Process for Eggshell Valorization." In ASME 2014 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2014. http://dx.doi.org/10.1115/imece2014-38836.
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The current global trend towards more stringent environmental standards, technical applicability and cost-effectiveness, became key factors in the selection of adsorbents. After demonstrating the performance of eggshell-derived adsorbent under a range of lab operating conditions, this work focused the adsorption efficiency of calcined eggshell powder (CEP), in the treatment of wastewaters from different industrial units. In order to do it, the removal of organic material, expressed as chemically oxygen demand (COD), was monitored in leachate wastewaters from sanitary landfill (LLWW) and in municipal residual wastewaters (MWW). Furthermore, the efficiency of alkaline metals removal, specifically from effluents of industrial unites from superficial treatments, was also assessed. A detailed study of the eggshell characteristics, before and after the adsorption process, was carried out, aiming at investigate the adsorption mechanism underlying the removal of different pollutants. Results demonstrate that adsorption of organic material and metals in the CEP, go around 84% of organic material removal in MWW and 81% in LLWW. Finally, a removal of 95% of aluminium (Al) from MWW, deriving from anodizing industrial plant, and a removal of 88% copper (Cu), 95% chromium (Cr) and 30% nickel (Ni) from effluents of superficial treatments produced in Ni/Cr plating plants, were also determined This suggests that CEP adsorbent is appropriated to wastewaters treatment with high contents of organic matter and heavy metals, from different aqueous systems or different industries. The application of this adsorbent in this methodology showed good cost-benefits ratio, proving that it can be an effective alternative to activated carbon. However, aiming the progress and sustainability of the whole eggshell valorisation, we are further optimizing, testing and developing new techniques and products to recover the organic fraction of the eggshell through the reclamation of several bioactive peptides derived from hydrolysis of different proteins that constitute these residues. These products are intended to be introduced in the food, cosmetic and pharmaceutical markets.
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Dalli, Jesmond, Ana Rodriguez, Bernd Spur, and Charles Serhan. "Structure elucidation and biological evaluations of sulfido-conjugated specialized pro-resolving mediators." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/mqgv6628.
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Inflammatory diseases are characterized by unabated inflammation that leads tissue destruction resulting in malaise. Whilst much is known on the mechanism that perpetuate inflammation, less is known about the molecules and pathways that coordinate the termination of inflammation and facilitate the repair and regeneration of damaged tissues. To evaluate the potential contribution of essential fatty acid-derived mediators in coordinating this life saving response we interrogated inflammatory exudates obtained following self-limited inflammatory challenge. Using radio-isotope tracking we found that the omega-3 fatty acid docosahexaenoic acid is utilized to produce novel bioactive molecules in these exudates. The structures of these molecules were elucidated using a range of physical techniques, demonstrating that these molecules were peptide lipid conjugated mediators and the stereochemistry of the functional groups was established using total organic synthesis. Investigations into their biosynthetic pathways demonstrated that the formation of their formation was initiated via the 14-lipoxygenation of DHA, that was then converted into an intermediate allylic epoxide and then conjugated to glutathione to yield the first mediator in the family which was coined as maresin conjugated in tissue regeneration (MCTR)1. This was then further converted to to 13-cysteinylglycinyl,14-hydroxy-docosahexaenoic acid (MCTR2) and 13-glycinyl,14-hydroxy-docosahexaenoic acid (MCTR3). Evaluation of the biological activities of these molecules demonstrated that they limited the recruitment of inflammatory cells to the sites of both sterile and infectious challenge. They reprogrammed biology towards a tissue protective phenotype and promoted the repair and regeneration of damaged tissues. Evaluation of the levels of these mediators in human peripheral blood demonstrated that the production of MCTR3 is significantly reduced in patients with rheumatoid arthritis that display signs of erosive joint disease. Together, these findings identify previously undescribed chemical signals that enhance host responses to limit inflammation, stimulate resolution of inflammation, and promote the restoration of function.
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Russo, Felipo Giovani Feitosa, and LEONARDO DE AZEVEDO CALDERÓN. "MINI REVISÃO DOS AVANÇOS DAS PATENTES ORIUNDOS DE ANUROS NO MUNDO E NO BRASIL NOS ÚLTIMOS 10 ANOS." In II Congresso Brasileiro de Biodiversidade Virtual. Revista Multidisciplinar de Educação e meio ambiente, 2022. http://dx.doi.org/10.51189/ii-conbiv/7116.
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Introdução: Os Anuros são uma ordem de vertebrados dotados de uma pele úmida que apresenta função de respiração, reprodução e defesa, sendo esta última a de maior relevância para os estudos de prospecção de novas drogas, pois a pele possui glândulas que secretam substâncias com diversas atividades biológicas. A partir dos estudos do italiano Vittorio Erspamer nos anos 60, foram extraídas e elucidadas diversas substâncias bioativas em especial moléculas e peptídeos bioativos, os quais apresentam ação antibacteriana, anticancerígena, antifúngica, neuromoduladores, antiprotozoários, ativadores da síntese do oxido nítrico etc. Assim, diversos projetos visando o desenvolvimento de produtos inovadores inspirados nestas moléculas. Objetivo: Neste resumo, busca-se avaliar a produção de patentes inspiradas em bioativos da pele de anuros nos últimos dez anos, realizando uma minuciosa busca na literatura a qual foi empregada a utilização da a ferramenta de busca Google Patentes, plataforma que relaciona dezessete escritórios de patentes das principais economias do mundo, estando entre tais escritórios o do Brasil, China, Estados unidos, Europa, Japão. Material e métodos: Foram utilizados os seguintes parâmetros de busca: a) definição do tema (patentes que envolviam anuros); b) escolha das palavras chaves (anura, frog, peptide, bioactive, secretion, skin); c) período das publicações (04/04/2012 a 04/04/2022); d) identificação patentes. Resultados: A busca apontou 898 patentes neste período, no entanto, apenas vinte e cinco patentes foram referentes a peptídeos. O país que mais se destacou nesta área foi a China com doze patentes. O Brasil, país que possui a maior diversidade de espécies de anuros do mundo, possuindo 1140 espécies já descritas, ficou entre os que menos geram patentes neste campo apresentando duas patentes, estando no mesmo patamar de Canada (2), Estados Unidos (2) e Japão (2). Conclusão: Este resultado está muito além do seu potencial proporcionalmente ao tamanho de sua biodiversidade. Logrando nos últimos dez anos apenas duas patentes com o número BR 102018014071-0A2 e BR 102018014079-5 A2, peptídeos de anuros, sendo estas depositadas em conjunto pelas universidades Federais do Mato Grosso, São João del Rei e Piauí.
Reports on the topic "Bioactive Peptide Products"
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López-Valverde, Nansi, Javier Aragoneses, Antonio López-Valverde, Cinthia Rodríguez, and Juan Manuel Aragoneses. Role in the osseointegration of titanium dental implants, of bioactive surfaces based on biomolecules: A systematic review and meta-analysis of in vivo studies. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, June 2022. http://dx.doi.org/10.37766/inplasy2022.6.0076.
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Review question / Objective: Does the bioactive surface of titanium dental implants, based on biomolecules, influence osseointegration?. The aim of our study was to evaluate the role and efficacy of bioactive surfaces in osseointegration. Our review study limited the research interest to titanium dental implants coated with a biomolecule, i.e., an organic molecule produced by a living organism. Condition being studied: In recent years, much attention has been paid to topographical modifications of dental implant surfaces, as well as to their coating with biologically active substances.a bioactive surface is one capable of achieving faster and higher quality osseointegration, shortening waiting times and solving situations of poor bone quality. Molecules that can be applied for bioactive purposes include bioceramics, ions and biomolecules. Collagen and bone morphogenetic protein have been suggested as bone stimulating agents. Biofunctionalization of the implant surface with a biomimetic active peptide has also been shown to result in a significant increase in bone-to-implant ratios and an increase in peri-implant bone density.
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Gurevitz, Michael, Michael E. Adams, Boaz Shaanan, Oren Froy, Dalia Gordon, Daewoo Lee, and Yong Zhao. Interacting Domains of Anti-Insect Scorpion Toxins and their Sodium Channel Binding Sites: Structure, Cooperative Interactions with Agrochemicals, and Application. United States Department of Agriculture, December 2001. http://dx.doi.org/10.32747/2001.7585190.bard.
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Integrated pest management in modern crop protection may combine chemical and biological insecticides, particularly due to the risks to the environment and livestock arising from the massive use of non-selective chemicals. Thus, there is a need for safer alternatives, which target insects more specifically. Scorpions produce anti-insect selective polypeptide toxins that are biodegradable and non-toxic to warm-blooded animals. Therefore, integration of these substances into insect pest control strategies is of major importance. Moreover, clarification of the molecular basis of this selectivity may provide valuable information pertinent to their receptor sites and to the future design of peptidomimetic anti-insect specific substances. These toxins may also be important for reducing the current overuse of chemical insecticides if they produce a synergistic effect with conventional pesticides. Based on these considerations, our major objectives were: 1) To elucidate the three-dimensional structure and toxic-site of scorpion excitatory, "depressant, and anti-insect alpha toxins. 2) To obtain an initial view to the sodium channel recognition sites of the above toxins by generating peptide decoys through a phage display system. 3) To investigate the synergism between toxins and chemical insecticides. Our approach was to develop a suitable expression system for toxin production in a recombinant form and for elucidation of toxin bioactive sites via mutagenesis. In parallel, the mode of action and synergistic effects of scorpion insecticidal toxins with pyrethroids were studied at the sodium channel level using electrophysiological methods. Objective 1 was achieved for the alpha toxin, LqhaIT Zilberberg et al., 1996, 1997; Tugarinov et al., 1997; Froy et al., 2002), and the excitatory toxin, Bj-xtrIT (Oren et al., 1998; Froy et al., 1999; unpublished data). The bioactive surface of the depressant toxin, LqhIT2, has been clarified and a crystal of the toxin is now being analyzed (unpublished). Objective 2 was not successful thus far as no phages that recognize the toxins were obtained. We therefore initiated recently an alternative approach, which is introduction of mutations into recombinant channels and creation of channel chimeras. Objective 3 was undertaken at Riverside and the results demonstrated synergism between LqhaIT or AaIT and pyrethroids (Lee et al., 2002). Furthermore, negative cross-resistance between pyrethroids and scorpion toxins (LqhaIT and AaIT) was demonstrated at the molecular level. Although our study did not yield a product, it paves the way for future design of selective pesticides by capitalizing on the natural competence of scorpion toxins to distinguish between sodium channels of insects and vertebrates. We also show that future application of anti-insect toxins may enable to decrease the amounts of chemical pesticides due to their synergism.