Academic literature on the topic 'Proteases; Peptidases; enzymes'
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Journal articles on the topic "Proteases; Peptidases; enzymes"
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Mamo, Jermen, and Fassil Assefa. "The Role of Microbial Aspartic Protease Enzyme in Food and Beverage Industries." Journal of Food Quality 2018 (July 3, 2018): 1–15. http://dx.doi.org/10.1155/2018/7957269.
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Proteases represent one of the three largest groups of industrial enzymes and account for about 60% of the total global enzymes sale. According to the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology, proteases are classified in enzymes of class 3, the hydrolases, and the subclass 3.4, the peptide hydrolases or peptidase. Proteases are generally grouped into two main classes based on their site of action, that is, exopeptidases and endopeptidases. Protease has also been grouped into four classes based on their catalytic action: aspartic, cysteine, metallo, and serine proteases. However, lately, three new systems have been defined: the threonine-based proteasome system, the glutamate-glutamine system of eqolisin, and the serine-glutamate-aspartate system of sedolisin. Aspartic proteases (EC 3.4.23) are peptidases that display various activities and specificities. It has two aspartic acid residues (Asp32 and Asp215) within their active site which are useful for their catalytic activity. Most of the aspartic proteases display best enzyme activity at low pH (pH 3 to 4) and have isoelectric points in the pH range of 3 to 4.5. They are inhibited by pepstatin. The failure of the plant and animal proteases to meet the present global enzyme demand has directed to an increasing interest in microbial proteases. Microbial proteases are preferred over plant protease because they have most of the characteristics required for their biotechnological applications. Aspartic proteases are found in molds and yeasts but rarely in bacteria. Aspartic protease enzymes from microbial sources are mainly categorized into two groups: (i) the pepsin-like enzymes produced byAspergillus,Penicillium,Rhizopus, andNeurosporaand (ii) the rennin-like enzymes produced byEndothiaandMucorspp., such asMucor miehei,M. pusillus, andEndothia parasitica. Aspartic proteases of microbial origin have a wide range of application in food and beverage industries. These include as milk-clotting enzyme for cheese manufacturing, degradation of protein turbidity complex in fruit juices and alcoholic liquors, and modifying wheat gluten in bread by proteolysis.
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Salvesen, Guy S., Gillian Murphy, and Hideaki Nagase. "The trap hypothesis: α2 and protease inhibition." Biochemist 28, no. 3 (June 1, 2006): 46–48. http://dx.doi.org/10.1042/bio02803046.
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In the 1970s, the Strangeways Laboratory in Cambridge consisted of a small number of groups collectively focused on the mechanisms of pathological connective-tissue damage. One of these groups, headed by Alan Barrett, was breaking ground on the destruction of the protein components of the matrix and was therefore heavily involved in identifying and categorizing newly emerging types of tissue-degrading enzymes. These enzymes, which Alan Barrett urges scientists to call peptidases, are also commonly called proteases or proteinases*. In the early 1970s, there were about 100 described human peptidases, a reasonable sampling of the 500–600 now known in humans in the post-genomic age. Approximately 2% of the human genome encodes peptidases, and roughly 1% encodes proteins with the ability to inhibit these enzymes. As the peptidases developed different catalytic mechanisms to solve the problem of cleaving the notoriously stable peptide bond, so the families of protease inhibitors acquired distinct strategies to regulate peptidase action. The strategies are usually directed towards blocking the peptidase active site directly or, less commonly, by allosteric mechanisms. But perhaps the most bizarre mechanism is that performed by members of the protein clan exemplified by the human protein 2-macroglobulin (α2).
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Wolke, Carmen, Alexander Teumer, Karlhans Endlich, Nicole Endlich, Rainer Rettig, Sylvia Stracke, Beate Fiene, et al. "Serum protease activity in chronic kidney disease patients: The GANI_MED renal cohort." Experimental Biology and Medicine 242, no. 5 (December 30, 2016): 554–63. http://dx.doi.org/10.1177/1535370216684040.
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Serum or plasma proteases have been associated with various diseases including cancer, inflammation, or reno-cardiovascular diseases. We aimed to investigate whether the enzymatic activities of serum proteases are associated with the estimated glomerular filtration rate (eGFR) in patients with different stages of chronic kidney disease (CKD). Our study population comprised 268 participants of the “Greifswald Approach to Individualized Medicine” (GANI_MED) cohort. Enzymatic activity of aminopeptidase A, aminopeptidase B, alanyl (membrane) aminopeptidase, insulin-regulated aminopeptidase, puromycin-sensitive aminopeptidase, leucine aminopeptidase 3, prolyl-endopeptidase (PEP), dipeptidyl peptidase 4 (DPP4), angiotensin I-converting enzyme, and angiotensin I-converting enzyme 2 (ACE2) proteases was measured in serum. Linear regression of the respective protease was performed on kidney function adjusted for age and sex. Kidney function was modeled either by the continuous Modification of Diet in Renal Disease (MDRD)-based eGFR or dichotomized by eGFR < 15 mL/min/1.73 m2 or <45 mL/min/1.73 m2, respectively. Results with a false discovery rate below 0.05 were deemed statistically significant. Among the 10 proteases investigated, only the activities of ACE2 and DPP4 were correlated with eGFR. Patients with lowest eGFR exhibited highest DPP4 and ACE2 activities. DPP4 and PEP were correlated with age, but all other serum protease activities showed no associations with age or sex. Our data indicate that ACE2 and DPP4 enzymatic activity are associated with the eGFR in patients with CKD. This finding distinguishes ACE2 and DPP4 from other serum peptidases analyzed and clearly indicates that further analyses are warranted to identify the precise role of these serum ectopeptidases in the pathogenesis of CKD and to fully elucidate underlying molecular mechanisms. Impact statement • Renal and cardiac diseases are very common and often occur concomitantly, resulting in increased morbidity and mortality. Understanding of molecular mechanisms linking both diseases is limited, available fragmentary data point to a role of the renin–angiotensin system (RAS) and, in particular, Ras-related peptidases. • Here, a comprehensive analysis of serum peptidase activities in patients with different stages of chronic kidney disease (CKD) is presented, with special emphasis given to RAS peptidases • The serum activities of the peptidases angiotensin I-converting enzyme 2 and dipeptidyl peptidase 4 were identified as closely associated with kidney function, specifically with the estimated glomerular filtration rate. The findings are discussed in the context of available data suggesting protective roles for both enzymes in reno-cardiac diseases. • The data add to our understanding of pathomechanisms underlying development and progression of CKD and indicate that both enzymes might represent potential pharmacological targets for the preservation of renal function.
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SHAN, Lu, Thomas MARTI, Ludvig M. SOLLID, Gary M. GRAY, and Chaitan KHOSLA. "Comparative biochemical analysis of three bacterial prolyl endopeptidases: implications for coeliac sprue." Biochemical Journal 383, no. 2 (October 8, 2004): 311–18. http://dx.doi.org/10.1042/bj20040907.
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Prolyl endopeptidases have potential for treating coeliac sprue, a disease of the intestine caused by proteolytically resistant peptides from proline-rich prolamins of wheat, barley and rye. We compared the properties of three similar bacterial prolyl endopeptidases, including the known enzymes from Flavobacterium meningosepticum (FM) and Sphingomonas capsulate (SC) and a novel enzyme from Myxococcus xanthus (MX). These enzymes were interrogated with reference chromogenic substrates, as well as two related gluten peptides (PQPQLPYPQPQLP and LQLQPFPQPQLPYPQPQLPYPQPQLPYPQPQPF), believed to play a key role in coeliac sprue pathogenesis. In vitro and in vivo studies were conducted to evaluate the activity, specificity and acid/protease stability of the enzymes. All peptidases were relatively resistant to acid, pancreatic proteases and membrane peptidases of the small intestinal mucosa. Although their activities against reference substrates were similar, the enzymes exhibited substantial differences with respect to chain length and subsite specificity. SC hydrolysed PQPQLPYPQPQLP well, but had negligible activity against LQLQPFPQPQLPYPQPQLPYPQPQLPYPQPQPF. In contrast, the FM and MX peptidases cleaved both substrates, although the FM enzyme acted more rapidly on LQLQPFPQPQLPYPQPQLPYPQPQLPYPQPQPF than MX. Whereas the FM enzyme showed a preference for Pro–Gln bonds, SC cleaved both Pro–Gln and Pro–Tyr bonds with comparable efficiency, and MX had a modest preference for Pro–(Tyr/Phe) sites over Pro–Gln sites. While a more comprehensive understanding of sequence and chain-length specificity may be needed to assess the relative utility of alternative prolyl endopeptidases for treating coeliac sprue, our present work has illustrated the diverse nature of this class of enzymes from the standpoint of proteolysing complex substrates such as gluten.
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Marokházi, Judit, Katalin Lengyel, Szilvia Pekár, Gabriella Felföldi, András Patthy, László Gráf, András Fodor, and István Venekei. "Comparison of Proteolytic Activities Produced by Entomopathogenic Photorhabdus Bacteria: Strain- and Phase-Dependent Heterogeneity in Composition and Activity of Four Enzymes." Applied and Environmental Microbiology 70, no. 12 (December 2004): 7311–20. http://dx.doi.org/10.1128/aem.70.12.7311-7320.2004.
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ABSTRACT Twenty strains (including eight phase variant pairs) of nematode-symbiotic and insect-pathogenic Photorhabdus bacteria were examined for the production of proteolytic enzymes by using a combination of several methods, including gelatin liquefaction, zymography coupled to native and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and activity measurement with two chromogen substrate types. Four protease activities (∼74, ∼55, ∼54, and ∼37 kDa) could be separated. The N-terminal sequences of three of the proteases were determined, and a comparison with sequences in databases allowed identification of these proteases as HEXXH metallopeptidases. Thus, the 74-kDa protease (described formerly as Php-B [J. Marokházi, G. Kóczán, F. Hudecz, L. Gráf, A. Fodor, and I. Venekei, Biochem. J. 379:633-640, 2004) is an ortholog of OpdA, a member the thimet oligopeptidase family, and the 55-kDa protease is an ortholog of PrtA, a HEXXH+H peptidase in clan MB (metzincins), while the 37-kDa protease (Php-C) belongs to the HEXXH+E peptidases in clan MA. The 54-kDa protease (Php-D) is a nonmetalloenzyme. PrtA and Php-C were zymographically detected, and they occurred in several smaller forms as well. OpdA could not be detected by zymography. PrtA, Php-C, and Php-D were secreted proteases; OpdA, in contrast, was an intracellular enzyme. OpdA activity was found in every strain tested, while Php-D was detected only in the Brecon/1 strain. There was significant strain variation in the secretion of PrtA and Php-C activities, but reduced activity or a lack of activity was not specific to secondary-phase variants. The presence of PrtA, OpdA, and Php-C activities could be detected in the hemolymph of Galleria melonella larvae 20 to 40 h postinfection. These proteases appear not to be directly involved in the pathogenicity of Photorhabdus, since strains or phase variants lacking any of these proteases do not show reduced virulence when they are injected into G. melonella larvae.
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Kryukov, V. S., S. V. Zinoviev, and R. V. Nekrasov. "Proteases in the diet of monogastric animals." Agrarian science 344, no. 1 (March 13, 2021): 30–38. http://dx.doi.org/10.32634/0869-8155-2021-344-1-30-38.
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There are many proteases, and about 2% of the human genome is involved in the regulation of their formation. The share of proteases involved in digestion accounts for only a small part. Despite this, the mechanisms of action of digestive proteases are less studied than carbohydrases and lipases. The incorporation of exogenous proteases into young animal feeds is often accompanied by improved utilization of protein and other nutrients. Exogenous proteases degrade inhibitors of the endogenous protease and lectins in feed. Alkaline proteases are of interest due to their broader substrate specificity and activity throughout the entire gastrointestinal tract. This group includes keratinases, which digest proteins inaccessible for cleavage by proteases and peptidases of animals. Keratinases digest agglutinins, glycinin and b-conglycinin and connective tissue proteins, which are resistant to the action of gastrointestinal enzymes and a number of exogenous proteases. The alleged reasons for the inconsistent results when using feed proteases are described. Their mediated positive effects not associated with proteolysis are indicated. It is advisable to use proteases with keratinolytic activity as fodder proteases.
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Massaoud, Mustafa K., Judit Marokh�zi, Andr�s Fodor, and Istv�n Venekei. "Proteolytic Enzyme Production by Strains of the Insect Pathogen Xenorhabdus and Characterization of an Early-Log-Phase-Secreted Protease as a Potential Virulence Factor." Applied and Environmental Microbiology 76, no. 20 (August 27, 2010): 6901–9. http://dx.doi.org/10.1128/aem.01567-10.
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ABSTRACT As a comparison to a similar study on Photorhabdus strains, 15 Xenorhabdus bacterial strains and secondary phenotypic variants of two strains were screened for proteolytic activity by five detection methods. Although the number and intensity of proteolytic activities were different, every strain was positive for proteolytic activity by several tests. Zymography following native PAGE detected two groups of activities with different substrate affinities and a higher and lower electrophoretic mobility that were distinguished as activity 1 and 2, respectively. Zymography following SDS-PAGE resolved three activities, which were provisionally named proteases A, B, and C. Only protease B, an ∼55-kDa enzyme, was produced by every strain. This enzyme exhibited higher affinity to the gelatin substrate than to the casein substrate. Of the chromogenic substrates used, three were hydrolyzed: furylacryloyl-Ala-Leu-Val-Tyr (Fua-ALVY), Fua-LGPA (LGPA is Leu-Gly-Pro-Ala) (a substrate for collagen peptidases), and succinyl-Ala-Ala-Pro-Phe-thiobenzyl (Succ-AAPF-SBzl). All but the Fua-LGPA-ase activity seemed to be from secreted enzymes. According to their substrate preference profiles and inhibitor sensitivities, at least six such proteolytic enzymes could be distinguished in the culture medium of Xenorhabdus strains. The proteolytic enzyme that was secreted the earliest, protease B and the Succ-AAPF-SBzl-hydrolyzing enzyme, appeared from the early logarithmic phase of growth. Protease B could also be detected in the hemolymph of Xenorhabdus-infected Galleria mellonella larvae from 15 h postinfection. The purified protease B hydrolyzed in vitro seven proteins in the hemolymph of Manduca sexta that were also cleaved by PrtA peptidase from Photorhabdus. The N-terminal sequence of protease B showed similarity to a 55-kDa serralysin type metalloprotease in Xenorhabdus nematophila, which had been identified as an orthologue of Photorhabdus PrtA peptidase.
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Suido, H., T. Eguchi, T. Tanaka, and M. Nakamura. "Identification of Periodontopathic Bacteria Based Upon their Peptidase Activities." Advances in Dental Research 2, no. 2 (November 1988): 304–9. http://dx.doi.org/10.1177/08959374880020021701.
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Black-pigmented Bacteroides (BPB) and spirochetes are associated with some forms of periodontal diseases. The enzymes produced by these bacteria may participate in the destruction of gingival and periodontal tissues. Certain proteases and peptidases are unique to Bacteroides gingivalis and Treponema denticola. Our purpose was to study the peptidases of periodontopathogens and to evaluate the use of unique peptidases for detection and identification of these bacteria. Bacteria used were BPB, Treponema, Fusobacterium, Capnocytophaga, Actinobacillus (Haemophilus), and Eikenella species. Twenty-five substrates, including mono-, di-, and tri-peptides of β-naphthylamide (β-NA) were employed for examination of peptidase activity. Clinically isolated BPB were obtained from 16 adult periodontitis patients. One hundred and ninety-three BPB strains were identified by conventional identification methods, and the peptidase activity was determined with N-Carbobenzoxy-glycyl-glycyl-L-arginine-β-naphthylamide (N-CBz-Gly-Gly-Arg-β-NA) used as a substrate. Among tested periodontopathic bacteria, only B. gingivalis and T. denticola could strongly hydrolyze some substrates such as N-CBz-Gly-Gly-Arg-β-NA and N-Benzoyl-L-valyl-glycyl-L-arginine-4-methoxy-(3-naphthylamide (Bz-Val-Gly-Arg-β-NA). In subgingival plaque samples, all patients showed BPB, and eight out of 16 patients possessed B. gingivalis by culture. One hundred and ten strains out of 193 BPB isolated were identified as B. gingivalis. Ninety-nine percent of these B. gingivalis strains identified showed N-CBz-Gly-Gly-Arg-β-NAhydrolyzing activity on a newly developed colorimetric plate assay. However, none of the other strains showed this activity in cultures of subgingival plaque which did not allow growth of spirochetes. Enzymes, such as N-CBz-Gly-Gly-Arg-peptidase and Bz-Val-Gly-Arg-peptidase, specific for B. gingivalis and T. denticola seem to be useful for rapid detection and identification of these bacteria.
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Sriranganadane, Dev, Utz Reichard, Karine Salamin, Marina Fratti, Olivier Jousson, Patrice Waridel, Manfredo Quadroni, Jean-Marc Neuhaus, and Michel Monod. "Secreted glutamic protease rescues aspartic protease Pep deficiency in Aspergillus fumigatus during growth in acidic protein medium." Microbiology 157, no. 5 (May 1, 2011): 1541–50. http://dx.doi.org/10.1099/mic.0.048603-0.
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In an acidic protein medium Aspergillus fumigatus secretes an aspartic endoprotease (Pep) as well as tripeptidyl-peptidases, a prolyl-peptidase and carboxypeptidases. In addition, LC-MS/MS revealed a novel glutamic protease, AfuGprA, homologous to Aspergillus niger aspergillopepsin II. The importance of AfuGprA in protein digestion was evaluated by deletion of its encoding gene in A. fumigatus wild-type D141 and in a pepΔ mutant. Either A. fumigatus Pep or AfuGprA was shown to be necessary for fungal growth in protein medium at low pH. Exoproteolytic activity is therefore not sufficient for complete protein hydrolysis and fungal growth in a medium containing proteins as the sole nitrogen source. Pep and AfuGprA constitute a pair of endoproteases active at low pH, in analogy to A. fumigatus alkaline protease (Alp) and metalloprotease I (Mep), where at least one of these enzymes is necessary for fungal growth in protein medium at neutral pH. Heterologous expression of AfuGprA in Pichia pastoris showed that the enzyme is synthesized as a preproprotein and that the propeptide is removed through an autoproteolytic reaction at low pH to generate the mature protease. In contrast to A. niger aspergillopepsin II, AfuGprA is a single-chain protein and is structurally more similar to G1 proteases characterized in other non-Aspergillus fungi.
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Heywood, Astra, and Iain L. Lamont. "Cell envelope proteases and peptidases of Pseudomonas aeruginosa: multiple roles, multiple mechanisms." FEMS Microbiology Reviews 44, no. 6 (August 17, 2020): 857–73. http://dx.doi.org/10.1093/femsre/fuaa036.
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ABSTRACT Pseudomonas aeruginosa is a Gram-negative bacterium that is commonly isolated from damp environments. It is also a major opportunistic pathogen, causing a wide range of problematic infections. The cell envelope of P. aeruginosa, comprising the cytoplasmic membrane, periplasmic space, peptidoglycan layer and outer membrane, is critical to the bacteria's ability to adapt and thrive in a wide range of environments. Over 40 proteases and peptidases are located in the P. aeruginosa cell envelope. These enzymes play many crucial roles. They are required for protein secretion out of the cytoplasm to the periplasm, outer membrane, cell surface or the environment; for protein quality control and removal of misfolded proteins; for controlling gene expression, allowing adaptation to environmental changes; for modification and remodelling of peptidoglycan; and for metabolism of small molecules. The key roles of cell envelope proteases in ensuring normal cell functioning have prompted the development of inhibitors targeting some of these enzymes as potential new anti-Pseudomonas therapies. In this review, we summarise the current state of knowledge across the breadth of P. aeruginosa cell envelope proteases and peptidases, with an emphasis on recent findings, and highlight likely future directions in their study.
Dissertations / Theses on the topic "Proteases; Peptidases; enzymes"
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Schroeder, Ewald. "Structural studies of #mu#-calpain, a novel calpain substrate, and a papain-leupeptin complex." Thesis, University of Oxford, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.386677.
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Guillemin, Sandrine. "Extraction aqueuse d'huile de colza assistée par hydrolyse enzymatique : optimisation de la réaction, caractérisation de l'émulsion et étude de procédés de déstabilisation." Thesis, Vandoeuvre-les-Nancy, INPL, 2006. http://www.theses.fr/2006INPL073N/document.
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En réponse aux attentes actuelles des consommateurs pour des produits de haute qualité nutritionnelle et environnementale, et face aux impératifs industriels conduisant à minimiser les risques et l’impact environnemental lors de l’extraction à l'hexane de l’huile de la graine de colza, l’étude de l’extraction aqueuse avec assistance enzymatique de cette huile a été reprise avec 2 objectifs principaux : déterminer les enzymes et mélanges d'enzymes adaptés à la meilleure déstructuration du tissu adipeux végétal, et d'autre part étudier les propriétés et la déstabilisation de l'émulsion formée. De l'optimisation de ces 2 séquences du process dépendent les rendements finaux en huile de l'extraction et les propriétés du tourteau, qui constituent les clés économiques de l'émergence de cette nouvelle technologie. Pour cela, après caractérisation physicochimique des constituants de la graine, protéases et polysaccharides hydrolases ont été testées seules ou en combinaison afin d’optimiser le rendement en huile libre et en huile contenue dans l’émulsion engendrée lors de l’extraction et obtenue par centrifugation. Après caractérisation de l’émulsion (rhéologie, diffusion statique de la lumière, pH, conductivité), des tests de déstabilisation physicochimiques ou thermo-mécaniques ont été mis en œuvre afin de séparer les constituants de l’émulsion formée, et obtenir ainsi la libération de l'huile. Les tests réalisés ont permis de retenir trois procédés de déstabilisation: l’addition de talcs, l’inversion de phase par addition d’huile exogène en présence de NaCl dans la phase aqueuse, et les cycles de congélation/décongélation. Afin d’apporter les premiers éléments de l’optimisation de ce dernier procédé, une étude par planification expérimentale a été mise en œuvreConsumer's concerns about the quality and environmental impact of the products as well as the industrial requirements regarding the risk assessment and the environmental and health repercussions of the solvent extraction of rapeseed oil using hexane led us to work on the optimisation of the aqueous enzymatic extraction of this oil. The study has been carried out to determine the best combination of enzymes able to achieve the disruption of the vegetal adipose tissue, and to characterize the emulsion obtained after centrifugation. The final objective was to maximize the yields of the oil extraction and to obtain adequate nutritional properties of the cake. After the physicochemical characterization of the rapeseed raw material, several proteases and polysaccharide hydrolases have been tested individually and in combination in order to optimize the removal of free oil and the emulsion oil yield occurring during the aqueous extraction process. The physicochemical properties of the emulsion have been determined: rheological properties, pH, conductivity, spectroscopy by Short Angles Light Scattering). Thereafter some physicochemical and thermo-mechanical treatments have been carried out to destabilize the oil-in-water emulsion obtained after the centrifugation, which contained a large part of the total oil of the reaction mixture. Three destabilization processes appeared particularly interesting to increase the free oil removal from the emulsion: talc addition before centrifugation, phase inversion by addition of exogenous oil in presence of NaCl in the aqueous phase, and freezing/thawing cycles. Finally, an optimisation trial of the freezing/thawing process using a Doehlert experimental design has been done as an example
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Duffeck, Carlos Eduardo. "Prospecção de queratinases microbianas : produção e caracterização bioquímica funcional /." São José do Rio Preto, 2020. http://hdl.handle.net/11449/192738.
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Orientador: Ronivaldo Rodrigues da SilvaResumo: Atualmente, a avicultura é um dos setores de grande impacto na economia brasileira. Nos últimos anos, tem sido observado um aumento na produção de frangos de corte, fazendo com que este segmento da indústria gere toneladas de queratina com o descarte de penas. Isso aponta para a necessidade de degradar este material que emerge como um problema ambiental. Neste cenário, as enzimas queratinolíticas têm despertado interesse biotecnológico devido a peculiar capacidade para a degradação de queratina e a possibilidade de aplicar o hidrolisado protéico para suplementação de ração animal e uso como biofertilizantes. Desta forma, neste trabalho, nós propomos prospectar queratinases pela bactéria Citrobacter diversus e o fungo Coriolopsis byrsina e, em seguida, investigar as características bioquímicas destas enzimas, a fim de propor aplicação na degradação de penas de frango. Em nossos resultados, a bactéria C. diversus foi capaz de degradar quase completamente as penas de frango (0,5%) em meio submerso após 36 h de fermentação. O estudo com o extrato enzimático mostrou máxima atividade caseinolítica a pH 9-10,5 e 50-55 ºC, e queratinolítica a pH 8,5-9,5 e 50 ºC. Em destaque, conforme a estabilidade em incubação por 1 h a 50ºC, foi detectado aproximadamente 50% e 100% da atividade queratinolítica e caseinolítica, respectivamente. Sob estabilidade a pH por 48 h a 4ºC, o extrato enzimático manteve maior atividade na faixa de pH 6-8. A atividade caseinolítica foi inibida por EDTA e PMSF,... (Resumo completo, clicar acesso eletrônico abaixo)
Abstract: Currently, poultry is one of the sectors of great impact on the Brazilian economy. In recent years, there has been an increase in the production of broilers, causing this segment of the industry to generate tons of keratin with the disposal of feathers. This points to the need to degrade this material, which emerges as an environmental problem. In this scenario, keratinolytic enzymes have aroused biotechnological interest due to the peculiar capacity for the degradation of keratin and the possibility of applying protein hydrolyzate to supplement animal feed and use as biofertilizers. Thus, in this work we propose to prospect keratinases for the bacterium Citrobacter diversus and the fungus Coriolopsis byrsina and, next, to investigate the biochemical characteristics of these enzymes, in order to propose application in the degradation of chicken feathers. In our results, the bacterium C. diversus was able to degrade chicken feathers almost completely (0.5%) in submerged medium after 36 h. The study with the enzymatic extract showed maximum caseinolytic activity at pH 9-10.5 and 50-55 ºC, and keratinolytic activity at pH 8.5-9.5 and 50 ºC. Notably, after enzyme pre-incubation for 1 h at 50 ºC, approximately 50% and 100% of keratinolytic and caseinolytic activity were detected, respectively. Under pH stability for 48 h at 4ºC, the enzyme extract maintained greater activity in the pH 6-8 range. Caseinolytic activity was inhibited by EDTA and PMSF, and keratinolytic activity was i... (Complete abstract click electronic access below)
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Sells, Earlphia. "Role of Tissue Kallikrein-Related Peptidase 6 in Colon Cancer Invasion." Diss., The University of Arizona, 2015. http://hdl.handle.net/10150/605219.
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Growing evidence indicates that serine proteases known as kallikreins are associated with malignancy and may have potential diagnostic/prognostic applications in cancer. Kallikreins are the largest group of serine proteases. Kallikrein enzymes are often involved in proteolytic cascades through their function in degradation of extracellular matrix proteins and promotion of angiogenesis. Kallikrein 6 (KLK6) is a member of the family of fifteen highly conserved secreted trypsin- or chemotrypsin-like serine proteases. Over-expression of KLK6 has been observed in different pathophysiological states such as neurodegenerative diseases, inflammation and various cancers, including colorectal cancer. In Chapter 3 we elucidated the miRNA-based mechanism of regulation of invasion in metastatic colorectal cancer over-expressing KLK6. We developed HCT116 colon stable isogenic cell lines with knockdown of KLK6 expression using short-hairpin interference RNA (shKLK6 clones). The shKLK6 clones had decreased expression and secretion of KLK6 protein with a minimal effect on cell growth and viability in cell culture. SCID mice injected with shKLK6-3 clone 3 cells exhibited a statistically significant increase in the survival rates (P=0.005), decrease in the incidence of distant metastases and a shift in the location of the metastatic foci closer to the cell's injection site. Levels of KLK6 protein secreted into the bloodstream were significantly lower in animals injected with shKLK6-3 clone 3 compared to HCT116 control clone 1 (P < 0.04). Through bioinformatics analyses we identified and validated three miRNAs, which are important in post-translational modification of bioactive proteins, proliferation, migration and p38 MAPK signaling pathway. In Chapter 4 we developed Caco-2 colon stable isogenic cell lines with expressing enzymatically active or mutant KLK6 protein (Caco-2 stable clones). We employed these cell lines to investigate the importance of KLK6 enzymatic activity of initiation of cell invasion using in vitro and in vivo models.
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Frey, Jonathan Packard. "Peptidase and protease enzymes of dairy lactobacilli and barley malt." 1985. http://catalog.hathitrust.org/api/volumes/oclc/13725193.html.
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Thesis (Ph. D.)--University of Wisconsin--Madison, 1985.Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references.
Books on the topic "Proteases; Peptidases; enzymes"
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Glaxo-UCLA Colloquium on Cellular Proteases and Control Mechanisms (1988 Lake Tahoe, Calif.). Cellular proteases and control mechanisms: Proceedings of a Glaxo-UCLA Colloquium on Cellular Proteases and Control Mechanisms, held at Lake Tahoe, California, February 21-26, 1988. Edited by Hugli T. E. New York: Liss, 1989.
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Cellular proteases and control mechanisms: Proceedings of a Glaxo-UCLA Colloquium on Cellular Proteases and Control Mechanisms, held at Lake Tahoe, California, ... symposia on molecular and cellular biology). Liss, 1989.
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(Editor), Uwe Lendeckel, and Nigel M. Hooper (Editor), eds. Proteases in Tissue Remodelling of Lung and Heart (Proteases in Biology and Disease). Springer, 2003.
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Proteases in tissue remodeling of lung and heart. New York, NY: Kluwer Academic/Plenum Publishers, 2004.
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Uwe, Lendeckel, and Hooper N. M, eds. Proteases in tissue remodelling of lung and heart. New York: Kluwer Academic/Plenum Publishers, 2003.
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6
J, Beynon R., and Bond Judith S, eds. Proteolytic enzymes: A practical approach. 2nd ed. Oxford: Oxford University Press, 2001.
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7
J, Beynon R., and Bond Judith S, eds. Proteolytic enzymes: A practical approach. 2nd ed. Oxford: Oxford University Press, 2001.
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8
(Editor), John N. Abelson, Melvin I. Simon (Editor), and Alan J. Barrett (Editor), eds. Proteolytic Enzymes: Serine and Cysteine Peptidases, Volume 244 (Methods in Enzymology). Academic Press, 1994.
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Proteolytic Enzymes: Serine and Cysteine Peptidases, Volume 244 (Methods in Enzymology). Academic Press, 1994.
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Klaus, von der Helm (Editor), Bruce D. Korant (Editor), and John C. Cheronis (Editor), eds. Proteases as Targets for Therapy (HANDBOOK OF EXPERIMENTAL PHARMACOLOGY). Springer, 2000.
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1
Peng Loh, Y., and Niamh X. Cawley. "[9] Processing enzymes of pepsin family: Yeast aspartic protease 3 and pro-opiomelanocortin converting enzyme." In Proteolytic Enzymes: Aspartic and Metallo Peptidases, 136–46. Elsevier, 1995. http://dx.doi.org/10.1016/0076-6879(95)48011-0.
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Pfirrmann, Thorsten, and Per O. Ljungdahl. "Ssy5 Peptidase: A Chymotrypsin-Like Signaling Protease in Yeast." In Handbook of Proteolytic Enzymes, 3103–10. Elsevier, 2013. http://dx.doi.org/10.1016/b978-0-12-382219-2.00685-2.
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