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Автор: Grafiati
Опубліковано: 15 червня 2024

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1

Kim, Jae Hwan, Eun Young Jung, Yang Hee Hong, Song Hwan Bae, Jin Man Kim, Dong Ouk Noh, Tsutomu Nozaki, Toshitada Inoue, and Hyung Joo Suh. "Short Communication: Pet foods with yeast hydrolysate can reduce body weight and increase girth in beagle dogs." Canadian Journal of Animal Science 92, no. 2 (June 2012): 207–10. http://dx.doi.org/10.4141/cjas2011-123.

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Kim, J. H., Jung, E. Y., Hong, Y. H., Bae, S. H., Kim, J. M., Noh, D. O., Nozaki, T., Inoue, T. and Suh, H. J. 2012. Short Communication: Pet foods with yeast hydrolysate can reduce body weight and increase girth in beagle dogs. Can. J. Anim. Sci. 92: 207–210. Beagle dogs fed pet foods that included yeast hydrolysate (YH) were used in the present study to assess the possible use of YH as a functional anti-obesity ingredient in pet food. The change in weight and girth in the YH groups was significantly (P<0.05) lower than that in the control. Plasma malondialdehyde was significantly (P<0.05) lower in the YH groups compared with that in the control. Plasma levels of the reduced form of glutathione were significantly (P<0.05) higher in the YH groups than those in the control. Therefore, YH could be recommended as an anti-obesity functional feed source for dogs.
2

Khir Anuar, Muhammad Afiq, Nur Husna Haron Narashid, Madihah Md Salleh, and Adibah Yahya. "Conversion of chicken viscera into protein hydrolysate for palatant production." Malaysian Journal of Fundamental and Applied Sciences 13, no. 4 (December 26, 2017): 606–11. http://dx.doi.org/10.11113/mjfas.v0n0.615.

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Flavor and aroma cannot be separated in food industries. The manipulation of the ingredients to increase the taste has started since early civilization. Common example of the earliest application of ingredients to increase the savory taste of the food is soy sauce production. The process of digging out the aroma and flavor includes frying, stewing, grilling as well as fermenting. Nowadays, much complex savory system in food can be achieved through several processes such as Maillard reaction and protein hydrolysate production. The food produced will not only be tasty but healthy. This concept was first focusing on human food production. However, the increasing number of pet owner for about 10% annually since 2008 as reported by US Pet Owner Society demands the same concept to be implemented in pet food industries. Since most pet owners considered their pets as part of their family, the pet food source from 4D (dead, dying, disable and diseased) animals are unacceptable. Therefore, the pet food industries are competing with human food industries to get the clean source of meat for food as well for flavor production. An alternative to overcome this is by utilizing the viscera of the slaughtered chicken for palatant or flavor production. Aside from meat, bones and feathers, viscera are also abundantly being considered as waste and were not fully utilized. They are rich in protein. The protein can be recovered using suitable process and later turned into a value-added product such as flavor. There is a study available for converting the protein waste into protein hydrolysate via chemical and physical technique. However, only few reports are available for the conversion process via indigenous microbes and enzymes. It is believed that the indigenous microbes and enzymes (protease, peptinase) can be utilized for protein hydrolysate production which will later can be utilized as palatant. The palatant produced should have Sulphur-based aroma compound such as 2-methyl-3-furanthiol and 2-furfuryl-thiol which serve as precursors for chicken aroma.
3

Theysgeur, Sandy, Benoit Cudennec, Barbara Deracinois, Claire Perrin, Isabelle Guiller, Anne Lepoudère, Christophe Flahaut, and Rozenn Ravallec. "New Bioactive Peptides Identified from a Tilapia Byproduct Hydrolysate Exerting Effects on DPP-IV Activity and Intestinal Hormones Regulation after Canine Gastrointestinal Simulated Digestion." Molecules 26, no. 1 (December 30, 2020): 136. http://dx.doi.org/10.3390/molecules26010136.

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Like their owners, dogs and cats are more and more affected by overweight and obesity-related problems and interest in functional pet foods is growing sharply. Through numerous studies, fish protein hydrolysates have proved their worth to prevent and manage obesity-related comorbidities like diabetes. In this work, a human in vitro static simulated gastrointestinal digestion model was adapted to the dog which allowed us to demonstrate the promising effects of a tilapia byproduct hydrolysate on the regulation of food intake and glucose metabolism. Promising effects on intestinal hormones secretion and dipeptidyl peptidase IV (DPP-IV) inhibitory activity were evidenced. We identify new bioactive peptides able to stimulate cholecystokinin (CCK) and glucagon-like peptide 1 (GLP-1) secretions, and to inhibit the DPP-IV activity after a transport study through a Caco-2 cell monolayer.
4

Liu, Pan, Yi Zheng, Yingbo Yuan, Tong Zhang, Qingbin Li, Quanfeng Liang, Tianyuan Su, and Qingsheng Qi. "Valorization of Polyethylene Terephthalate to Muconic Acid by Engineering Pseudomonas Putida." International Journal of Molecular Sciences 23, no. 19 (September 20, 2022): 10997. http://dx.doi.org/10.3390/ijms231910997.

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Plastic waste is rapidly accumulating in the environment and becoming a huge global challenge. Many studies have highlighted the role of microbial metabolic engineering for the valorization of polyethylene terephthalate (PET) waste. In this study, we proposed a new conceptual scheme for upcycling of PET. We constructed a multifunctional Pseudomonas putida KT2440 to simultaneously secrete PET hydrolase LCC, a leaf-branch compost cutinase, and synthesize muconic acid (MA) using the PET hydrolysate. The final product MA and extracellular LCC can be separated from the supernatant of the culture by ultrafiltration, and the latter was used for the next round of PET hydrolysis. A total of 0.50 g MA was produced from 1 g PET in each cycle of the whole biological processes, reaching 68% of the theoretical conversion. This new conceptual scheme for the valorization of PET waste should have advantages over existing PET upcycling schemes and provides new ideas for the utilization of other macromolecular resources that are difficult to decompose, such as lignin.
5

Ratnayani, Ketut, Indriani Wisnu Susanto Panjaitan, and Ni Made Puspawati. "SCREENING POTENTIAL ANTIOXIDANT AND ANTIBACTERIAL ACTIVITIES OF PROTEIN HYDROLYSATES DERIVED FROM GERMINATED LABLAB BEAN, PIGEON PEA AND KIDNEY BEAN." Journal of Health Sciences and Medicine 1, no. 1 (February 1, 2017): 24. http://dx.doi.org/10.24843/jhsm.2017.v01.i01.p07.

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Abstract Protein hydrolysate contains a mixture of various lengths of short peptides chain and free amino acids that may excert biological activities. This research aims to screen potential antioxidant and antibacterial activities of protein hydrolysate produced from three kinds of germinated beans i.e. lablab bean (Lablab purpureus), pigeon pea (Cajanus cajan (L.) Millsp) and kidney bean (Phaseolus vulgaris) through enzymatic hydrolysis process. The steps of research included germination process of the beans prior to total protein isolation, enzymatic hydrolysis of total protein isolates using pancreatin enzyme, evaluation of in vitro antioxidant activity of the hydrolysates protein using DPPH (1,1-diphenyl-2-picryl hydrazyl) method, and antibaterial activity testing towards Eschericia coli and Staphyllococcus aureus bacteria. The results revealed that pancreatine enzyme was able to hydrolyse germinated protein of lablab bean, pigeon pea and kidney bean at the experiment condition applied with degree of hydrolysis 34.12%, 27.44%, and 30,93% respectively. It was also found that protein hydrolysates of lablab bean, pigeon pea, and kidney bean demonstrated antioxidant activity which percentage radical DPPH scavenging activity of 84.02%, 68.97% and 67.89 %. On the other hand, all of those protein hydrolysates did not show any antibacterial activity towards Eschericia coli and Staphyllococcus aureus bacteria.
6

Bi, Changhao, Xueli Zhang, Lonnie O. Ingram, and James F. Preston. "Genetic Engineering of Enterobacter asburiae Strain JDR-1 for Efficient Production of Ethanol from Hemicellulose Hydrolysates." Applied and Environmental Microbiology 75, no. 18 (July 17, 2009): 5743–49. http://dx.doi.org/10.1128/aem.01180-09.

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ABSTRACT Dilute acid pretreatment is an established method for hydrolyzing the methylglucuronoxylans of hemicellulose to release fermentable xylose. In addition to xylose, this process releases the aldouronate methylglucuronoxylose, which cannot be metabolized by current ethanologenic biocatalysts. Enterobacter asburiae JDR-1, isolated from colonized wood, was found to efficiently ferment both methylglucuronoxylose and xylose in acid hydrolysates of sweet gum xylan, producing predominantly ethanol and acetate. Transformation of E. asburiae JDR-1 with pLOI555 or pLOI297, each containing the PET operon containing pyruvate decarboxylase (pdc) and alcohol dehydrogenase B (adhB) genes derived from Zymomonas mobilis, replaced mixed-acid fermentation with homoethanol fermentation. Deletion of the pyruvate formate lyase (pflB) gene further increased the ethanol yield, resulting in a stable E. asburiae E1(pLOI555) strain that efficiently utilized both xylose and methylglucuronoxylose in dilute acid hydrolysates of sweet gum xylan. Ethanol was produced from xylan hydrolysate by E. asburiae E1(pLOI555) with a yield that was 99% of the theoretical maximum yield and at a rate of 0.11 g ethanol/g (dry weight) cells/h, which was 1.57 times the yield and 1.48 times the rate obtained with the ethanologenic strain Escherichia coli KO11. This engineered derivative of E. asburiae JDR-1 that is able to ferment the predominant hexoses and pentoses derived from both hemicellulose and cellulose fractions is a promising subject for development as an ethanologenic biocatalyst for production of fuels and chemicals from agricultural residues and energy crops.
7

Deb-Choudhury, Santanu, Emma N. Bermingham, Wayne Young, Matthew P. G. Barnett, Scott O. Knowles, Duane Harland, Stefan Clerens, and Jolon M. Dyer. "The effects of a wool hydrolysate on short-chain fatty acid production and fecal microbial composition in the domestic cat (Felis catus)." Food & Function 9, no. 8 (2018): 4107–21. http://dx.doi.org/10.1039/c7fo02004j.

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8

Castelvetro, Valter, Andrea Corti, Jacopo La Nasa, Francesca Modugno, Alessio Ceccarini, Stefania Giannarelli, Virginia Vinciguerra, and Monica Bertoldo. "Polymer Identification and Specific Analysis (PISA) of Microplastic Total Mass in Sediments of the Protected Marine Area of the Meloria Shoals." Polymers 13, no. 5 (March 5, 2021): 796. http://dx.doi.org/10.3390/polym13050796.

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Microplastics (MPs) quantification in benthic marine sediments is typically performed by time-consuming and moderately accurate mechanical separation and microscopy detection. In this paper, we describe the results of our innovative Polymer Identification and Specific Analysis (PISA) of microplastic total mass, previously tested on either less complex sandy beach sediment or less demanding (because of the high MPs content) wastewater treatment plant sludges, applied to the analysis of benthic sediments from a sublittoral area north-west of Leghorn (Tuscany, Italy). Samples were collected from two shallow sites characterized by coarse debris in a mixed seabed of Posidonia oceanica, and by a very fine silty-organogenic sediment, respectively. After sieving at <2 mm the sediment was sequentially extracted with selective organic solvents and the two polymer classes polystyrene (PS) and polyolefins (PE and PP) were quantified by pyrolysis-gas chromatography-mass spectrometry (Pyr-GC/MS). A contamination in the 8–65 ppm range by PS could be accurately detected. Acid hydrolysis on the extracted residue to achieve total depolymerization of all natural and synthetic polyamides, tagging of all aminated species in the hydrolysate with a fluorophore, and reversed-phase high performance liquid chromatography (HPLC) (RP-HPLC) analysis, allowed the quantification within the 137–1523 ppm range of the individual mass of contaminating nylon 6 and nylon 6,6, based on the detected amounts of the respective monomeric amines 6-aminohexanoic acid (AHA) and hexamethylenediamine (HMDA). Finally, alkaline hydrolysis of the residue from acid hydrolysis followed by RP-HPLC analysis of the purified hydrolysate showed contamination by polyethylene terephthalate (PET) in the 12.1–2.7 ppm range, based on the content of its comonomer, terephthalic acid.
9

Awosika, Temitola, and Rotimi E. Aluko. "Enzymatic Pea Protein Hydrolysates Are Active Trypsin and Chymotrypsin Inhibitors." Foods 8, no. 6 (June 10, 2019): 200. http://dx.doi.org/10.3390/foods8060200.

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In this work, we report the potency of enzymatic hydrolysates of pea proteins against trypsin and chymotrypsin. Pea protein concentrate was digested with each of alcalase, chymotrypsin, pepsin, and trypsin, followed by membrane separation of the protein hydrolysates into peptide fractions (<1, 1–3, 3–5, and 5–10 kDa). Peptide size profiling with size-exclusion gel chromatography indicated the narrowest size range (0.85–4.98 kDa) for alcalase. Trypsin activity was strongly (p < 0.05) inhibited by the ultrafiltration fractions (mean IC50 = 2.2 mg/mL) obtained from the trypsin hydrolysate when compared to the unfractionated hydrolysate (IC50 = 6.8 mg/mL). Similarly, ultrafiltration also enhanced trypsin inhibition by the alcalase-digested peptides with an IC50 of 21.4 mg/mL for the unfractionated hydrolysate in comparison to 3.1–4.7 mg/mL for the fractions. However, ultrafiltration did not enhance trypsin inhibitory activity of chymotrypsin-digested peptides, while the peptide separation reduced efficacy of pepsin-digested peptides. In contrast, chymotrypsin inhibition by all the enzymatic digests was significantly (p < 0.05) enhanced by ultrafiltration, especially peptide sizes >3 kDa. Kinetics of enzyme inhibition indicate peptides were bound to the enzyme active site in a competitive mode that led to reduced catalysis. We conclude that the pea peptides could function as useful tools to promote human health and as a preservative during food processing and storage.
10

Sun, Kekui, Zhaoqi Dai, Wenlong Hong, Jianying Zhao, Hang Zhao, Ji Luo, and Guangjie Xie. "Effects of Maillard Reaction on Volatile Compounds and Antioxidant Capacity of Cat Food Attractant." Molecules 27, no. 21 (October 25, 2022): 7239. http://dx.doi.org/10.3390/molecules27217239.

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In this study, self-made cat food attractant was prepared by Maillard reaction using hydrolysate of grass carp waste as raw material and glucose and cysteine hydrochloride as substrate. Its volatile compounds, antioxidant capacity, and pet palatability were investigated. The volatile compounds of attractants were analyzed using gas chromatography–mass spectrometry (GC-MS) which showed that alcohols and aldehydes were the most volatile in self-made attractants, accounting for 34.29% and 33.52%, respectively. Furthermore, Maillard reaction could significantly increase the antioxidant activity of self-made attractant, including scavenging activity on OH and DPPH free radicals as well as the chelating ability of Fe2+. The acceptance and palatability of two kinds of cat food were studied by adding 3% self-made or commercial attractants. The results of this study also found that both attractants could remarkably improve the intake rate of cat food. However, the self-made group was significantly less than the commercial group in first smell, first bite, and feeding rate, which might be because of the absence of umami ingredients and spices in self-made attractants.
11

Kotlyar, Miroslava, Diana Ibatullina, Maria Zinov’eva, Ksenia Shnaider, and Sania Zaripova. "Application of enzymatic hydrolyzate of chitosan as a plant growth promoter." E3S Web of Conferences 443 (2023): 01002. http://dx.doi.org/10.1051/e3sconf/202344301002.

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The natural polymer chitosan is widely used in various fields of agriculture, industry and medicine. The properties of a polymer largely depend on its molecular weight and supramolecular structure. In particular, to enhance the beneficial properties of chitosan, its low-molecular derivatives are obtained. The presented work shows the possibility of using enzymatic chitosan hydrolysates as a biostimulator of plants. It has been established that pretreatment of pea seeds (Pisum sativum) variety “Zhegalova 112” with solutions of chitosan hydrolyzate in all studied concentrations increases the seeds and soil germination. In the course of the work, the highest efficiency of chitosan hydrolysate was confirmed when growing pea seeds in the soil, namely higher soil germination, significantly faster growth of green biomass of plants, acceleration of leaf formation. A pronounced effect of chitosan hydrolysates on plants under stress conditions was discovered. So, cultivation of pretreated with chitosan hydrolysate cucumber seeds (Cucumis sativus) in an unsuitable period for growth promotes their germination. At the same time, seed germination is completely absent in the control group.
12

Ruiz, Raquel, Raquel Olías, Alfonso Clemente та Luis A. Rubio. "A Pea (Pisum sativum L.) Seed Vicilins Hydrolysate Exhibits PPARγ Ligand Activity and Modulates Adipocyte Differentiation in a 3T3-L1 Cell Culture Model". Foods 9, № 6 (16 червня 2020): 793. http://dx.doi.org/10.3390/foods9060793.

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Legume consumption has been reported to induce beneficial effects on obesity-associated metabolic disorders, but the underlying mechanisms have not been fully clarified. In the current work, pea (Pisum sativum L.) seed meal proteins (albumins, legumins and vicilins) were isolated, submitted to a simulated gastrointestinal digestion, and the effects of their hydrolysates (pea albumins hydrolysates (PAH), pea legumins hydrolysates (PLH) and pea vicilin hydrolysates (PVH), respectively) on 3T3-L1 murine pre-adipocytes were investigated. The pea vicilin hydrolysate (PVH), but not native pea vicilins, increased lipid accumulation during adipocyte differentiation. PVH also increased the mRNA expression levels of the adipocyte fatty acid-binding protein (aP2) and decreased that of pre-adipocyte factor-1 (Pref-1) (a pre-adipocyte marker gene), suggesting that PVH promotes adipocyte differentiation. Moreover, PVH induced adiponectin and insulin-responsive glucose transporter 4 (GLUT4) and stimulated glucose uptake. The expression levels of peroxisome proliferator-activated receptor γ (PPARγ), a key regulator of adipocyte differentiation, were up-regulated in 3T3-L1 cells treated with PVH during adipocyte differentiation. Finally, PVH exhibited PPARγ ligand activity. Lactalbumin or other pea hydrolysates (PAH, PLH) did not exhibit such effects. These findings show that PVH stimulates adipocyte differentiation via, at least in part, the up-regulation of PPARγ expression levels and ligand activity. These effects of PVH might be relevant in the context of the beneficial health effects of legume consumption in obesity-associated metabolic disorders.
13

Segarra, Sergi, Boguslawa Dziedzic, and Mariusz Dziedzic. "PSVIII-14 Improved Palatability and Digestibility in Dry Dog Food Using a Porcine Intestinal Mucosa Hydrolysate." Journal of Animal Science 101, Supplement_3 (November 6, 2023): 458–59. http://dx.doi.org/10.1093/jas/skad281.544.

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Abstract A proper diet for a dog is one that provides all the required nutrients and is highly digestible. In order for the ingredients to be delivered to the organism, this diet should be highly palatable. Currently, research is being conducted on the possibility of introducing new sources of animal protein, thus replacing traditional meat meals. A new source of protein, together with increasing the digestibility and palatability of dry pet food while maintaining the price of the recipe, is an expected success. Porcine intestinal mucosa hydrolysate (PIMH) products are high-quality, sustainable, and inexpensive protein sources obtained from porcine intestinal mucosa as byproduct of the heparin manufacturing process. PIMH are being used as alternative protein sources in several animal species. The present study aimed to determine the effects of incorporating 3% PIMH (Palbio HP, Bioiberica SAU, Palafolls, Spain) as replacement for poultry meal on digestibility and palatability of dog dry food. The palatability test was conducted on a professional, independent panel of dogs. The test lasted 4 days with 20 adult dogs. Apparent digestibility and feces quality were also assessed in a digestibility test under the supervision of veterinarians in a 10-day experiment. The tested diets which serve as reference of a commercial dry dog food (Control diet) and a diet in which 3% PIMH was incorporated as replacement for poultry meal (PIMH diet). Palatability evaluation was performed in a two-pan setting in which first choice and consumption ratio were quantified and compared over four days. A Chi square test was used for the statistical analysis and a P-value of &lt; 0.05 was considered statistically significant. An improvement in palatability was observed with the PIMH diet. More specifically, first choice results were greater during the four days of the study with PIMH (82%, 88%, 89% and 100%, respectively) compared with Control. Likewise, consumption ratio was also greater with PIMH over the four study days (84%, 87%, 86% and 93%, respectively). On the other hand, the PIMH diet showed a greater digestibility (77.98%) compared with the Control diet (73.95%), as well as a better feces score (0% unacceptable feces vs 4.2% in the Control group).In conclusion, using 3% Palbio HP PIMH in dry dog food as replacement for poultry meal leads to enhanced palatability and digestibility, while it has no negative impact on feces quality or diet costs.
14

Rizzello, Carlo Giuseppe, Anna Lavecchia, Valerio Gramaglia, and Marco Gobbetti. "Long-Term Fungal Inhibition by Pisum sativum Flour Hydrolysate during Storage of Wheat Flour Bread." Applied and Environmental Microbiology 81, no. 12 (April 10, 2015): 4195–206. http://dx.doi.org/10.1128/aem.04088-14.

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ABSTRACTIn order to identify antifungal compounds from natural sources to be used as ingredients in the bakery industry, water/salt-soluble extracts (WSE) from different legume flour hydrolysates obtained by the use of a fungal protease were assayed againstPenicillium roquefortiDPPMAF1. The agar diffusion assays allowed the selection of the pea (Pisum sativum) hydrolysate as the most active. As shown by the hyphal radial growth rate, the WSE had inhibitory activity towards several fungi isolated from bakeries. The MIC of the WSE was 9.0 mg/ml. Fungal inhibition was slightly affected by heating and variations in pH. The antifungal activity was attributed to three native proteins (pea defensins 1 and 2 and a nonspecific lipid transfer protein [nsLTP]) and a mixture of peptides released during hydrolysis. The three proteins have been reported previously as components of the defense system of the plant. Five peptides were purified from WSE and were identified as sequences encrypted in leginsulin A, vicilin, provicilin, and the nsLTP. To confirm antifungal activity, the peptides were chemically synthesized and tested. Freeze-dried WSE were used as ingredients in leavened baked goods. In particular, breads made by the addition of 1.6% (wt/wt) of the extract and fermented by baker's yeast or sourdough were characterized for their main chemical, structural, and sensory features, packed in polyethylene bags, stored at room temperature, and compared to controls prepared without pea hydrolysate. Artificially inoculated slices of a bread containing the WSE did not show contamination by fungi until at least 21 days of storage and behaved like the bread prepared with calcium propionate (0.3%, wt/wt).
15

Bollati, Carlotta, Ruoxian Xu, Giovanna Boschin, Martina Bartolomei, Fabrizio Rivardo, Jianqiang Li, Anna Arnoldi, and Carmen Lammi. "Integrated Evaluation of the Multifunctional DPP-IV and ACE Inhibitory Effect of Soybean and Pea Protein Hydrolysates." Nutrients 14, no. 12 (June 8, 2022): 2379. http://dx.doi.org/10.3390/nu14122379.

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Nowadays, notwithstanding their nutritional and technological properties, food bioactive peptides from plant sources garner increasing attention for their ability to impart more than one beneficial effect on human health. Legumes, which stand out thanks to their high protein content, represent valuable sources of bioactive peptides. In this context, this study focused on the characterization of the potential pleotropic activity of two commercially available soybean (SH) and pea (PH) protein hydrolysates, respectively. Since the biological activity of a specific protein hydrolysate is strictly correlated with its chemical composition, the first aim of the study was to identify the compositions of the SH and PH peptides. Peptidomic analysis revealed that most of the identified peptides within both mixtures belong to storage proteins. Interestingly, according to the BIOPEP-UWM database, all the peptides contain more than one active motive with known inhibitory angiotensin converting enzyme (ACE) and dipeptidyl-dipeptidases (DPP)-IV sequences. Indeed, the results indicated that both SH and PH inhibit DPP-IV and ACE activity with a dose-response trend and IC50 values equal to 1.15 ± 0.004 and 1.33 ± 0.004 mg/mL, and 0.33 ± 0.01 and 0.61 ± 0.05 mg/mL, respectively. In addition, both hydrolysates reduced the activity of DPP-IV and ACE enzymes which are expressed on the surface of human intestinal Caco-2 cells. These findings clearly support that notion that SH and PH may represent new ingredients with anti-diabetic and hypotensive effects for the development of innovative multifunctional foods and/or nutraceuticals for the prevention of metabolic syndrome.
16

Ratnayani, Ketut, Putu Ajeng Agustini, Ni Wayan Wisaniyasa, Ni Made Puspawati, and I. Nengah Wirajana. "Enzymatic Hydrolysis of Pigeon Pea Sprout Protein and its Potential to Generate Savory Taste." International Journal of Current Microbiology and Applied Sciences 12, no. 12 (December 10, 2023): 101–8. http://dx.doi.org/10.20546/ijcmas.2023.1212.013.

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The germination process is one way to improve the quality of legume protein, which will be used as a substrate in the production of protein hydrolysate. This study aims to hydrolyze pigeon pea (Cajanus cajan (L.) Millsp.) sprout protein concentrate by using alcalase enzymes to obtain protein hydrolysate which has the potential to generate a savory or umami taste. The research began with total protein extraction to generate pigeon pea sprout protein concentrate which was then used as a substrate in the hydrolysis process treated with variations ratio of the Enzyme to the Substrate (E/S ratio). Each protein hydrolysate obtained was characterized based on free α-amino content, soluble protein content, and sensory evaluation of the savory taste level. Protein hydrolysis results in the range of E/S ratio 0.1% - 1.5% showed that the E/S ratio 1.5% was able to produce the highest content of free α-amino (2.95±0.08 mg/mL) and soluble protein content (13.69±0.11 mg/mL). Besides that, the highest sensory evaluation score was obtained in the E/S ratio of 1.0%. This result shows that the protein hydrolysate of pigeon pea sprouts can be used as a natural flavor.
17

Sonnendecker, Christian. "PET-Recycling — mit Enzymen gegen die Plastikkrise." BIOspektrum 28, no. 6 (October 2022): 660–62. http://dx.doi.org/10.1007/s12268-022-1828-0.

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AbstractMass production of inert plastics based on mineral-oil has become a problem to our environment due to the lack of sustainable recycling options. PET however consists of hydrolysable ester bonds, which enables several strategies. One aspiring technology is based on the enzymatic hydrolysis of PET. The basic building blocks of the polymer can be recovered to close the recycling loop for PET.
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Shi, Jian-Jun, Yan Wang, Li-Rong Meng, Jing-Chun Zhu, Rui-Wen Shu, and Jie He. "Synthesis of rGO/TiO2/CdS Nanocomposites and its Enhanced Photoelectrochemical Performance in Determination of Parathion-Methyl." Nano 13, no. 05 (May 2018): 1850054. http://dx.doi.org/10.1142/s1793292018500546.

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A photoelectrochemical (PEC) sensor for the determination of organophosphate pesticides (OPs) was developed based on rGO/TiO2/CdS photoactive nanomaterials. The rGO/TiO2/CdS nanocomposites were prepared by solvothermal method and electrochemical deposition technique successively. The morphologies and structures of the as-prepared nanocomposites were extensively investigated by SEM and XRD. In alkaline condition, p-nitrophenol as the hydrolysate of parathion-methyl (PM) could be obtained by a simple hydrolyzation process. Under optimal conditions, the rGO/TiO2/CdS NPs modified ITO electrode exhibited a good PEC performance toward the hydrolysate of PM. The photocurrent intensity was enhanced with the increase of the concentration of the hydrolysate of PM. The proposed PEC method could detect PM in the range from 0.05[Formula: see text]nmol L[Formula: see text] to 10[Formula: see text]nmol L[Formula: see text] with a detection limit of 0.02[Formula: see text]nmol L[Formula: see text] ([Formula: see text]). Thus, the excellent performance of the rGO/TiO2/CdS nanocomposites serve as the matrix of the sensor, which provides a new way for the fabrication of high-sensitivity PEC sensing system.
19

Mouithys-Mickalad, Ange, Eric Schmitt, Monika Dalim, Thierry Franck, Nuria Martin Tome, Michel van Spankeren, Didier Serteyn, and Aman Paul. "Black Soldier Fly (Hermetia illucens) Larvae Protein Derivatives: Potential to Promote Animal Health." Animals 10, no. 6 (May 29, 2020): 941. http://dx.doi.org/10.3390/ani10060941.

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European legislation permits the inclusion of insect proteins in pet and aquaculture diets. Black soldier fly larvae (BSF) are one of the most actively produced species due to their low environmental impact and nutritional characteristics. BSF protein derivatives (proteins and protein hydrolysates) contain a substantial amount of low molecular weight peptides that are known to possess antioxidant potential. In this study, the in vitro antioxidant potential of commercial BSF proteins and protein hydrolysates was investigated for (1) radical scavenging activity, (2) myeloperoxidase activity modulation, and (3) neutrophil response modulation. Chickenmeal and fishmeal are commonly used in pet food and aquaculture formulations. Hence, both were used as industrial benchmarks during this study. The results indicate that fishmeal and chickenmeal are ineffective at suppressing the oxidative damage caused by neutrophil response and myeloperoxidase activity. Fishmeal and chickenmeal even exhibit pro-oxidant behavior in some of the models used during this study. On the other hand, it was found that BSF protein derivatives could be effective in protecting against the cellular damage resulting from neutrophil and myeloperoxidase activities. The outcomes of this study indicate that BSF protein derivatives could be potentially included in pet food and aquaculture feed formulations as health-promoting ingredients.
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Siriporn, B., P. Thongkorn, S. Waraporn, S. Wiriyaporn, S. Sinee, A. Chiramet, and E. A. Rotimi. "Antioxidant polypeptides derived from pigeon pea (Cajanus cajan (L) Mill sp.) by enzymatic hydrolysis." Food Research 8, Supplementary 2 (April 26, 2024): 182–89. http://dx.doi.org/10.26656/fr.2017.8(s2).146.

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Pigeon pea (Cajanus cajan (L) Mill sp.) seeds are rich sources of protein in the legume family and their consumption has been associated with the prevention of noncommunicated diseases, which is attributable to their content of bioactive components. Antioxidant protein hydrolysates were produced from pigeon pea protein isolate (PPI) by enzymatic hydrolysis using pancreatin and flavourzyme. The hydrolysates were analyzed for their physicochemical, molecular weight, amino acid composition, and in vitro antioxidant activities. The molecular weights of polypeptides in the hydrolysates were 8, 20, 25 and 48 kDa, which were determined after pancreatin or flavourzyme hydrolysis of the protein isolate for 4 h. Pancreatin-hydrolyzed pigeon pea protein (PPHP) contained high hydrophobic amino acids, especially isoleucine, leucine and valine, which were related to the high content of aromatic amino acids. The hydrolysates obtained from flavourzyme hydrolysis of pigeon pea proteins (PPHF) presented significantly higher capacities to scavenge ABTS˙+ and reduce Fe3 + better than that of PPI, while the PPI exhibited strong DPPH scavenging (98.4 mg trolox equivalent antioxidant capacity). The results indicated that the partial hydrolysis for PPI provided medium to high molecular weight of peptides. Therefore, PPHF could be a promising source of bioactive peptides and a potential ingredient for the formulation of functional foods against oxidative stress
21

Zhou, Heqi, Songbiao Shi, Qiuhong You, Kaikai Zhang, Yuchuan Chen, Dekai Zheng, and Jian Sun. "Polyethylene Terephthalate Hydrolases in Human Gut Microbiota and Their Implications for Human Health." Microorganisms 12, no. 1 (January 10, 2024): 138. http://dx.doi.org/10.3390/microorganisms12010138.

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Polyethylene terephthalate (PET), primarily utilized for food and beverage packaging, consistently finds its way into the human gut, thereby exerting adverse effects on human health. PET hydrolases, critical for the degradation of PET, have been predominantly sourced from environmental microbial communities. Given the fact that the human gut harbors a vast and intricate consortium of microorganisms, inquiry into the presence of potential PET hydrolases within the human gut microbiota becomes imperative. In this investigation, we meticulously screened 22,156 homologous sequences that could potentially encode PET hydrolases using the hidden Markov model (HMM) paradigm, drawing from 4984 cultivated genomes of healthy human gut bacteria. Subsequently, we methodically validated the hydrolytic efficacy of five selected candidate PET hydrolases on both PET films and powders composed of micro-plastics (MPs). Notably, our study also unveiled the influence of both diverse PET MP powders and their resultant hydrolysates on the modulation of cytokine expression in macrophages. In summary, our research underscores the ubiquitous prevalence and considerable potential of the human gut microbiota in PET hydrolysis. Furthermore, our study significantly contributes to the holistic evaluation of the potential health hazards posed by PET MPs to human well-being.
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Holý, Petr, and Eva Benešová. "From PET Bottles to Sweet Delicacies." Chemické listy 116, no. 1 (January 15, 2022): 61–64. http://dx.doi.org/10.54779/chl20220061.

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The treatment of waste PET bottles has become a pressing global issue over the last few decades, and many scientific teams are currently working on solutions to it. There are many different approaches of how to solve this problem. The present article outlines the possibility to process terephthalic acid, which is the hydrolysis product of polyethylene terephthalate, into vanillin, a compound widely used in the food industry. The work of British scientists who have succeeded in using genetic modification to produce a strain of E. coli RARE_pVanX capable of processing polyethylene terephthalate hydrolysates to the desired vanillin is presented in a broader context.
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Stanisavljevic, Nemanja, Goran Vukotic, Ferenc Pastor, Desanka Suznjevic, Zivko Jovanovic, Ivana Strahinic, Djordje Fira, and Svetlana Radovic. "Antioxidant activity of pea protein hydrolysates produced by batch fermentation with lactic acid bacteria." Archives of Biological Sciences 67, no. 3 (2015): 1033–42. http://dx.doi.org/10.2298/abs150130066s.

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Nine Lactobacillus strains known for surface proteinase activity were chosen from our collection and tested for their ability to grow in pea seed protein-based medium, and to hydrolyze purified pea proteins in order to produce peptides with antioxidant (AO) activity. Two strains, Lactobacillus rhamnosus BGT10 and Lactobacillus zeae LMG17315, exhibited strong proteolytic activity against pea proteins. The AO activity of the pea hydrolysate fraction, MW <10 kDa, obtained by the fermentation of purified pea proteins with Lactobacillus rhamnosus BGT10, was tested by standard spectrophotometric assays (DPPH, ABTS, Fe3+-reducing capacity) and the recently developed direct current (DC) polarographic assay. The low molecular weight fraction of the obtained hydrolysate was separated using ion exchange chromatography, while the AO activity of eluted fractions was determined by means of a sensitive DC polarographic assay without previous concentration of samples. Results revealed that the fraction present in low abundance that contained basic peptides possessed the highest antioxidant activity. Based on the obtained results, it can be concluded that Lactobacillus rhamnosus BGT10 should be further investigated as a candidate strain for large-scale production of bioactive peptides from legume proteins.
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Sato, Yasuhiro, Kenji Wakabayashi, Eishin Ogawa, Hiroko Kodama, and Masakazu Mimaki. "Low serum biotin in Japanese children fed with hydrolysate formula." Pediatrics International 58, no. 9 (June 15, 2016): 867–71. http://dx.doi.org/10.1111/ped.12937.

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El‑Lababidi, Nabil. "Extensive hydrolysates and their role in clinical practice." Pediatrie pro praxi 21, no. 4 (September 3, 2020): 238–42. http://dx.doi.org/10.36290/ped.2020.049.

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Saha, Nabanita, Martin Zatloukal, and Petr Saha. "Modification of polymers by protein hydrolysate?A way to biodegradable materials." Polymers for Advanced Technologies 14, no. 11-12 (November 2003): 854–60. http://dx.doi.org/10.1002/pat.406.

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27

Hidayat, Meilinah, Sijani Prahastuti, TeresaLiliana Wargasetia, Vincentius Ferdinand, Roro Wahyudianingsih, AndreanusAndaja Soemardji, SitiFarah Rahmawati, Nova Suliska, and Khomaini Hasan. "Role of pea protein hydrolysates as antinephrotoxicity." Journal of Reports in Pharmaceutical Sciences 8, no. 1 (2019): 55. http://dx.doi.org/10.4103/jrptps.jrptps_14_17.

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Soral-Śmietana, M., A. Świgoń, R. Amarowicz, and L. Sijtsma. "The solubility of trypsin pea protein hydrolysates." Nahrung / Food 42, no. 03-04 (August 1998): 217–18. http://dx.doi.org/10.1002/(sici)1521-3803(199808)42:03/04<217::aid-food217>3.3.co;2-u.

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29

Marinova, Margarita D., and Bozhidar P. Tchorbanov. "Preparation of Antioxidant Enzymatic Hydrolysates from Honeybee-Collected Pollen Using Plant Enzymes." Enzyme Research 2010 (January 9, 2010): 1–5. http://dx.doi.org/10.4061/2010/415949.

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Enzymatic hydrolysates of honeybee-collected pollen were prepared using food-grade proteinase and aminopeptidases entirely of plant origin. Bromelain from pineapple stem was applied (8 mAU/g substrate) in the first hydrolysis stage. Aminopeptidase (0.05 U/g substrate) and proline iminopeptidase (0.03 U/g substrate) from cabbage leaves (Brassica oleracea var. capitata), and aminopeptidase (0.2 U/g substrate) from chick-pea cotyledons (Cicer arietinum L.) were involved in the additional hydrolysis of the peptide mixtures. The degree of hydrolysis (DH), total phenolic contents, and protein contents of these hydrolysates were as follows: DH (about 20–28%), total phenolics (15.3–27.2 μg/mg sample powder), and proteins (162.7–242.8 μg/mg sample powder), respectively. The hydrolysates possessed high antiradical scavenging activity determined with DPPH (42–46% inhibition). The prepared hydrolysates of bee-collected flower pollen may be regarded as effective natural and functional dietary food supplements due to their remarkable content of polyphenol substances and significant radical-scavenging capacity with special regard to their nutritional-physiological implications.
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Verma, Nitin, Mukesh C. Bansal, and Vivek Kumar. "Pea peel waste: A lignocellulosic waste and its utility in cellulase production by Tricoderma reesei under solid state cultivation." BioResources 6, no. 2 (March 16, 2011): 1505–19. http://dx.doi.org/10.15376/biores.6.2.1505-1519.

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A wide variety of waste bioresources are available on our planet for conversion into bioproducts. In the biological systems, microorganisms are used to utilize waste as an energy source for the synthesis of valuable products such as biomass proteins and enzymes. The large quantities of byproducts generated during the processing of plant food involve an economic and environmental problem due to their high volumes and elimination costs. After isolation of the main constituent, there are abundant remains which represent an inexpensive material that has been undervalued until now. Pea peel waste is one of the undervalued, unused sources of energy that can serve as a potential source for cellulase production. Batch experiments have been performed, using pea peel waste as a carbon source for cellulase production under solid state cultivation by Trichoderma reesei. It was observed that 30 oC temperature and pH 5.0 are the most favorable conditions for cellulase production by T. reesei. FPase activity significantly increases by incorporation of whey as well as wheat starch hydrolysate in the basal salt media used in the production study. The present study describes the utility of pea peel waste, whey as well as wheat starch hydrolysate in cellulase production by T. reesei. The utilization of economically cheap, pea peel waste for cellulase production could be a novel, cost effective, and valuable approach in cellulase production as well as in solid waste management.
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Osman, Ali, Abdel-Rahaman M. Merwad, Azza H. Mohamed, and Mahmoud Sitohy. "Foliar Spray with Pepsin-and Papain-Whey Protein Hydrolysates Promotes the Productivity of Pea Plants Cultivated in Clay Loam Soil." Molecules 26, no. 9 (May 10, 2021): 2805. http://dx.doi.org/10.3390/molecules26092805.

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Papain and pepsin-hydrolyzed whey protein (PAH and PEH, respectively) were prepared and characterized for its degree of hydrolysis, chemical constituents (amino acid and peptides) and antioxidant activity. A field experiment was conducted at El Salheya El Gedida City, Sharqia, Egypt, during the seasons 2019 and 2020, to investigate the biological action of the foliar spray of PAH and PEH on the growth and yield of pea plants cultivated in a clay loam soil. Foliar application of the papain and pepsin-hydrolyzed whey protein (PAH and PEH, respectively) at 1000 and 2000 mg/L was applied three times after 25, 35 and 45 days from planting. All protein foliar spray treatments had significant positive effects on the uptake of N, P and K, simultaneously increasing the contents of all the photosynthetic pigments (Chlorophyll a, Chlorophyll b and Carotenoids) in a concentration-dependent manner. The most conspicuous increase was seen in Chlorophyll b (105% increase), followed by Carotenoids (91% increase). Generally, the favorable increases caused by the second level of application (2000 mg/L) were nearly 2–3 times that of the low level (1000 mg/L). Pod growth and formation indicators, e.g., no. of pod/plant, pod length and no. of seeds/pod, responded more evidently to the hydrolyzed than the intact form of whey protein treatments. Hydrolyzed whey protein foliar spray treatments achieved significantly higher increases in the global field yield components of Pisum sativum plants than the intact form, where peptic hydrolysates were significantly superior to papain hydrolysate. The treatment PEH (2000 mg/L) can be recommended as the most effective bio-stimulating foliar spray treatment for higher plant productivity when applied 25, 35 and 45 days after planting.
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Kawai, Fusako. "The Current State of Research on PET Hydrolyzing Enzymes Available for Biorecycling." Catalysts 11, no. 2 (February 3, 2021): 206. http://dx.doi.org/10.3390/catal11020206.

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This short paper reviews two groups of enzymes designated as polyethylene terephthalate (PET) hydrolases: one consists of thermophilic cutinases from thermophilic microorganisms (actinomycetes and a fungus) and the other consists of mesophilic cutinases, the representative of which is IsPETase from a mesophilic bacterium. From the viewpoint that PET hydrolysis requires a high temperature close to the glass transition temperature (65–70 °C in water) of PET, mesophilic cutinases are not suitable for use in the enzymatic recycling of PET since their degradation level is one to three orders of magnitude lower than that of thermophilic cutinases. Many studies have attempted to increase the thermostability of IsPETase by introducing mutations, but even with these modifications, the mesophilic cutinase does not reach the same level of degradation as thermophilic cutinases. In addition, this kind of trial contradicts the claim that IsPETase works at ambient temperature. As plastic pollution is an urgent environmental issue, scientists must focus on feasible thermophilic enzymes for the enzymatic processing of disposed PET, rather than on mesophilic cutinases. Thermophilic and mesophilic cutinases must be evaluated precisely and comparatively, based on their features that enable them to hydrolyze PET, with the aim of enzymatic PET disposal. The level of thermophilic cutinases has already reached their optimal level in PET biorecycling. The optimal level may be reached through the processing of PET waste, by amorphization and micronization into readily hydrolysable forms and the improvement of PET hydrolases by engineering higher degradation ability and low-cost production. Here I summarize the critical points in the evaluation of PET hydrolases and discuss the biorecycling of PET.
33

Michalczyk, Alicja Katarzyna, Sylwia Garbaczewska, Bolesław Morytz, Arkadiusz Białek, and Jerzy Zakrzewski. "Influence of Nitrogen Sources on D-Lactic Acid Biosynthesis by Sporolactobacillus laevolacticus DSM 442 Strain." Fermentation 7, no. 2 (May 14, 2021): 78. http://dx.doi.org/10.3390/fermentation7020078.

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The purpose of this study was to explore the possibility of replacing an expensive yeast extract contained in the fermentation medium for D-lactic acid (D-LA, R-lactic acid) biosynthesis with an alternative nitrogen source. The screening studies were conducted under stationary conditions and showed that pea seed hydrolysate was the most beneficial substrate in the process of D-LA biosynthesis by the strain Sporolactobacillus laevolacticus DSM 442 among the used inorganic and organic nitrogen sources, waste materials, food and agricultural products. After 96 h, 75.5 g/L D-LA was obtained in batch cultures in a medium containing pea seed hydrolysate, with an average productivity of 0.79 g/L/h, yield of 75.5%, and optical purity of 99.4%. In batch cultures fed once, in a medium with an analogous composition, 122.6 g/L D-LA was obtained after 120 h, and the average yield, productivity and optical purity were 87.6%, 1.021 g/L/h, and 99.6%, respectively. Moreover, the amount of D-LA obtained in the fermentation medium enriched with the above-mentioned cheap agricultural product was similar to the amounts obtained in the medium containing yeast extract in both stationary and bioreactor cultures. Our research shows that hydrolyzed pea seeds, which belong to the legume family, may be a promising nitrogen source for the production of D-LA on an industrial scale.
34

Mantareva, Vanya, Ivan Iliev, Inna Sulikovska, Mahmut Durmuş, and Tsanislava Genova. "Collagen Hydrolysate Effects on Photodynamic Efficiency of Gallium (III) Phthalocyanine on Pigmented Melanoma Cells." Gels 9, no. 6 (June 9, 2023): 475. http://dx.doi.org/10.3390/gels9060475.

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The conjugation of photosensitizer with collagen seems to be a very promising approach for innovative topical photodynamic therapy (PDT). The study aims to evaluate the effects of bovine collagen hydrolysate (Clg) on the properties of gallium (III) phthalocyanine (GaPc) on pigmented melanoma. The interaction of GaPc with Clg to form a conjugate (GaPc-Clg) showed a reduction of the intensive absorption Q-band (681 nm) with a blue shift of the maximum (678 nm) and a loss of shape of the UV-band (354 nm). The fluorescence of GaPc, with a strong emission peak at 694 nm was blue shifted due to the conjugation which lower intensity owing to reduce quantum yield (0.012 vs. 0.23, GaPc). The photo- and dark cytotoxicity of GaPc, Glg and GaPc-Clg on pigmented melanoma cells (SH-4) and two normal cell lines (BJ and HaCaT) showed a slight decrease of cytotoxicity for a conjugate, with low selectivity index (0.71 vs. 1.49 for GaPc). The present study suggests that the ability of collagen hydrolysate to form gels minimizes the high dark toxicity of GaPc. Collagen used for conjugation of a photosensitizer might be an essential step in advanced topical PDT.
35

Häberer, C. D., K. Diepvens, N. Geary, and W. Langhans. "Intragastric infusion of pea protein hydrolysate reduces food intake more than pea protein." Appetite 49, no. 1 (July 2007): 295. http://dx.doi.org/10.1016/j.appet.2007.03.081.

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36

Moreno, Cecilia, Luis Mojica, Elvira González de Mejía, Rosa María Camacho Ruiz, and Diego A. Luna-Vital. "Combinations of Legume Protein Hydrolysates Synergistically Inhibit Biological Markers Associated with Adipogenesis." Foods 9, no. 11 (November 17, 2020): 1678. http://dx.doi.org/10.3390/foods9111678.

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The objective was to investigate the anti-adipogenesis potential of selected legume protein hydrolysates (LPH) and combinations using biochemical assays and in silico predictions. Black bean, green pea, chickpea, lentil and fava bean protein isolates were hydrolyzed using alcalase (A) or pepsin/pancreatin (PP). The degree of hydrolysis ranged from 15.5% to 35.5% for A-LPH and PP-LPH, respectively. Antioxidant capacities ranged for ABTS•+ IC50 from 0.3 to 0.9 Trolox equivalents (TE) mg/mL, DPPH• IC50 from 0.7 to 13.5 TE mg/mL and nitric oxide (NO) inhibition IC50 from 0.3 to 1.3 mg/mL. LPH from PP–green pea, A–green pea and A–black bean inhibited pancreatic lipase (PL) (IC50 = 0.9 mg/mL, 2.2 mg/mL and 1.2 mg/mL, respectively) (p < 0.05). For HMG-CoA reductase (HMGR) inhibition, the LPH from A–chickpea (0.15 mg/mL), PP–lentil (1.2 mg/mL), A–green pea (1.4 mg/mL) and PP–green pea (1.5 mg/mL) were potent inhibitors. Combinations of PP–green pea + A–black bean (IC50 = 0.4 mg/mL), A–green pea + PP–green pea (IC50 = 0.9 mg/mL) and A–black bean + A–green pea (IC50 = 0.6 mg/mL) presented synergistic effects to inhibit PL. A–chickpea + PP–lentil (IC50 = 0.8 mg/mL) and PP–lentil + A–green pea (IC50 = 1.3 mg/mL) interacted additively to inhibit HMGR and synergistically in the combination of A–chickpea + PP–black bean (IC50 = 1.3 mg/mL) to block HMGR. Peptides FEDGLV and PYGVPVGVR inhibited PL and HMGR in silico, showing predicted binding energy interactions of −7.6 and −8.8 kcal/mol, respectively. Combinations of LPH from different legume protein sources could increase synergistically their anti-adipogenic potential.
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Sanchez-Reinoso, Zain, Sarah Todeschini, Jacinthe Thibodeau, Laila Ben Said, Ismail Fliss, Laurent Bazinet, and Sergey Mikhaylin. "Impact of Pulsed Electric Fields and pH on Enzyme Inactivation and Bioactivities of Peptic Hydrolysates Produced from Bovine and Porcine Hemoglobin." Foods 11, no. 21 (October 22, 2022): 3313. http://dx.doi.org/10.3390/foods11213313.

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The production of bioactive peptides from hemoglobin via peptic hydrolysis is a promising alternative to valorizing slaughterhouse blood proteins. Nevertheless, it has some limitations such as low yield, high cost of enzymes, and the use of chemical reagents. The latter is aggravated by the pH increase to inactivate the enzyme, which can affect the bioactivity of the peptides. Thus, this study aimed to evaluate the effect of pulsed electric fields (PEF) on the pepsin inactivation and biological activities (antimicrobial and antioxidant) of hemoglobin hydrolysates. Bovine (Hb-B) and porcine (Hb-P) hemoglobin were hydrolyzed with pepsin for 3 h and treated with PEFs to inactivate the enzyme. The degree of hydrolysis (DH) did not show significant changes after PEF inactivation, whereas peptide population analysis showed some changes in PEF-treated hydrolysates over time, suggesting residual pepsin activity. PEF treatments showed no significant positive or negative impact on antimicrobial and antioxidant activities. Additionally, the impact of pH (3, 7, and 10) on bioactivity was studied. Higher pH fostered stronger anti-yeast activity and DPPH-scavenging capacity, whereas pH 7 fostered antifungal activity. Thus, the use of hemoglobin from the meat industry combined with PEF treatments could fit the circular economy concept since bioactive peptides can be produced more eco-efficiently and recycled to reduce the spoilage of meat products. Nevertheless, further studies on PEF conditions must be carried out to achieve complete inactivation of pepsin and the potential enhancement of peptides’ bioactivity.
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Krasnoshtanova, Alla Al'bertovna, and Leonid Viktorovich Shul'ts. "PREPARATION AND EVALUATION OF THE FUNCTIONAL PROPERTIES OF PROTEIN ISOLATES AND HY-DROLYSATES FROM PLANT RAW MATERIALS." chemistry of plant raw material, no. 4 (December 15, 2022): 299–309. http://dx.doi.org/10.14258/jcprm.20220410952.

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Animal protein plays a key role in the human diet as the most balanced amino acid composition; however, its consumption often causes allergic reactions. Plant protein serves as a substitute for animal protein. The most promising sources of plant protein are the seeds of cereals, pulses, oilseeds and cereals. Research aim: selection of conditions for obtaining protein isolates and enzymatic hydrolysates having the desired functional properties from different types of vegetable raw materials.Pea, corn and oat flour LLC "FavoritT"; linseed flour LLC NGO "Compass Health". Enzyme preparations: chymotrypsin LLC "Samson-Med"; Protex 40E Genencor; protosubtilin G3x produced by PO "Sibbiofarm" LLC; pancreatin PJSC "Biosintez"; trypsin LLC "Diaem"; beef pepsin OJSC "MHSF". Crude protein content was determined by Kjeldahl method, protein substances - by modified Lowry method. Fat-holding, water-holding, emulsifying and foaming capacities, as well as allergenicity of protein isolates and hydrolysates were determined. Conditions for protein substances extraction from flax, corn, oat and pea flour with the yield of high-molecular protein fraction not less than 70 % of raw protein content were selected. The conditions of protein isolates precipitation to produce preparations containing not less than 85% of protein have been selected. The type of enzyme preparation for hydrolysis - pancreatin - was selected. It was found that in order to increase water- and fat-holding capacity of pea isolate, hydrolysis is possible with duration not exceeding 15 min, for all other isolates hydrolysis is undesirable. The best emulsifying and foam-forming capacities are possessed by linseed hydrolysates after 60 and 90 min of hydrolysis, respectively. Enzymatic hydrolysis was shown to reduce the allergenicity of plant proteins. The obtained hydrolysates of vegetable proteins can be used as ingredients for functional products, as well as for obtaining products with reduced allergenicity.
39

Humiski, L. M., and R. E. Aluko. "Physicochemical and Bitterness Properties of Enzymatic Pea Protein Hydrolysates." Journal of Food Science 72, no. 8 (October 2007): S605—S611. http://dx.doi.org/10.1111/j.1750-3841.2007.00475.x.

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40

Dhankhar, Rajesh, Anil Dhaka, and Sakshi. "Bioconversion of Water Hyacinth to Ethanol by Using Cellulase from Trichoderma atroviride AD-130." Advanced Materials Research 918 (April 2014): 145–48. http://dx.doi.org/10.4028/www.scientific.net/amr.918.145.

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The Present study showed that water hyacinth could be used as a suitable alternative cheaper carbohydrate source for bioethanol production. Crude cellulase and β-glucosidase were produced by using fungi Trichoderma atroviride AD-130. Highest yield of reducing sugars (451.13 g/L) was obtained from acid pretreated water hyacinth supplemented with 0.1% PEG-6000. The highest ethanol concentration (16.43 g/L) from enzymatic hydrolysate of substrate was achieved with a corresponding ethanol yield of 0.28 g/g sugar.
41

BROWN, ANN, TIIU KAURI, D. J. KUSHNER, and S. P. MATHUR. "MEASUREMENT AND SIGNIFICANCE OF CELLULOSE IN PEAT SOILS." Canadian Journal of Soil Science 68, no. 4 (November 1, 1988): 681–85. http://dx.doi.org/10.4141/cjss88-065.

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The degree of decomposition of 30 organic soils from southern Superior Province of the Precambrian Shield was investigated by comparing the cellulose component, measured as glucose in the acid hydrolysate, with the aerobic respiration rate and with the rubbed fiber content of the soils. Bivarient analyses of these parameters show reasonable correlation. It is suggested, therefore, that cellulose determination is suitable for assessing the biodegradation potential of organic soils. The method is quantitative and less subject to operator error and variability than the fiber determinations, and more rapid and reproducible than measurement of carbon dioxide produced by respiration. Key words: Cellulose, peatlands, organic soils, respiration rate, degree of decomposition
42

Li, Huan, and Rotimi E. Aluko. "Identification and Inhibitory Properties of Multifunctional Peptides from Pea Protein Hydrolysate." Journal of Agricultural and Food Chemistry 58, no. 21 (November 10, 2010): 11471–76. http://dx.doi.org/10.1021/jf102538g.

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43

Soral-Smietana, Maria, Ryszard Amarowicz, Alicja Swigon, and Lolke Sijtsma. "Comparison of solubility of pea protein hydrolysate by three analytical methods." International Journal of Food Sciences and Nutrition 50, no. 6 (January 1999): 407–11. http://dx.doi.org/10.1080/096374899100978.

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44

Sarigiannidou, Krystalia, Davide Odelli, Flemming Jessen, Mohammad Amin Mohammadifar, Fatemeh Ajalloueian, Mar Vall-llosera, Antonio Fernandes de Carvalho, and Federico Casanova. "Interfacial Properties of Pea Protein Hydrolysate: The Effect of Ionic Strength." Colloids and Interfaces 6, no. 4 (December 7, 2022): 76. http://dx.doi.org/10.3390/colloids6040076.

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The effect of a tryptic hydrolysis as well as the effect of ionic strength (0–0.4 M NaCl) was investigated on the oil/water interfacial properties of soluble pea protein hydrolysate (SPPH) at neutral pH and room temperature (20 ± 0.01 °C). SEC-MALS and SDS-Page analysis showed that tryptic hydrolysis created a lower molecular weight polypeptide mixture, whereas FTIR analysis and DSC thermograms demonstrated a more disordered and flexible structure. The bulk properties of SPPH were studied in terms of hydrodynamic diameter and turbidity, where higher particle size (+ ~13 nm) and turbidity were observed at 0.4 M NaCl. Regarding the interfacial properties, the surface activity of SPPH improved by increasing ionic strength, with maximum interfacial pressure (14.28 mN/m) at 0.4 M NaCl. Nevertheless, the addition of NaCl negatively affected the elasticity and strength of the interfacial film, where the sample without salt exhibited the highest dilatational and shear storage modulus in all the frequencies considered.
45

Folador, J. F., L. K. Karr-Lilienthal, C. M. Parsons, L. L. Bauer, P. L. Utterback, C. S. Schasteen, P. J. Bechtel, and G. C. Fahey. "Fish meals, fish components, and fish protein hydrolysates as potential ingredients in pet foods." Journal of Animal Science 84, no. 10 (October 1, 2006): 2752–65. http://dx.doi.org/10.2527/jas.2005-560.

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46

Xie, M. S., and G. R. Dubyak. "Guanine-nucleotide- and adenine-nucleotide-dependent regulation of phospholipase D in electropermeabilized HL-60 granulocytes." Biochemical Journal 278, no. 1 (August 15, 1991): 81–89. http://dx.doi.org/10.1042/bj2780081.

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We have characterized the regulation of phospholipase D (PLD) in electropermeabilized HL-60 granulocytes in which endogenous phospholipids were pre-labelled with [3H]oleic acid. Treatment of these permeabilized cells with the non-hydrolysable GTP analogues guanosine 5′-[gamma-thio]triphosphate (GTP[S]) and guanosine 5′-[beta gamma-imido]triphosphate induced a sustained (near-linear for up to 60 min) accumulation of phosphatidic acid (PA). In the presence of ethanol a sustained production of phosphatidylethanol (PEt) was also observed. With increasing concentrations of ethanol, PEt formation increased, whereas PA formation declined; this indicated involvement of a PLD-type effector enzyme. The ability of GTP[S] to stimulate this PLD activity was Mg(2+)-dependent and was inhibited by GDP and its non-hydrolysable beta-thio analogue. Ca2+, at concentrations less than or equal to nM, had no effect on the GTP[S]-dependent PLD activity. However, higher concentrations of Ca2+ produced a significant potentiation of this activity. Inclusion of MgATP (greater than or equal to 0.1 mM), but not other nucleoside triphosphates, also induced a large potentiation of GTP[S]-dependent PLD activation. In the absence of guanine nucleotides, MgATP elicited no significant activation of PLD. Significantly, this effect of ATP was not mimicked by adenosine 5′-[beta gamma-methylene]triphosphate, a non-hydrolysable ATP analogue. Rather, this analogue inhibited both basal and ATP-potentiated GTP[S]-dependent PLD activity. This suggests that the ability of ATP to potentiate GTP[S]-dependent PLD activity involves phosphotransferase action rather than simple allosteric effects induced by adenine nucleotide binding. The absolute magnitude of the GTP[S]-dependent PLD activity which could be potentiated by MgATP was decreased by 90% when the permeabilized cells were preincubated for various times before addition of these stimulatory agents. This time-dependent loss of MgATP-induced potentiation was prevented when the permeabilized cells were preincubated in the presence of GTP[S]. These results demonstrate that electropermeabilized HL-60 granulocytes can be used to discriminate synergistic roles for a GTP-binding protein(s) and an ATP-dependent process (kinase?) in the regulation of phospholipase D activity.
47

Frączek, R., E. Kostyra, H. Kostyra, and S. Krawczuk. "Immunoreactive properties of pea protein extract and its trypsin hydrolysates." Journal of Animal and Feed Sciences 16, no. 3 (September 6, 2007): 472–84. http://dx.doi.org/10.22358/jafs/66803/2007.

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48

Vázquez, Manuel, and Antonio M. Martin. "Mathematical model forPhaffia rhodozyma growth using peat hydrolysates as substrate." Journal of the Science of Food and Agriculture 76, no. 4 (April 1998): 481–87. http://dx.doi.org/10.1002/(sici)1097-0010(199804)76:4<481::aid-jsfa973>3.0.co;2-z.

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49

Häberer, Doreen, Maria Tasker, Martin Foltz, Nori Geary, Margriet Westerterp, and Wolfgang Langhans. "Intragastric infusion of pea-protein hydrolysate reduces test-meal size in rats more than pea protein." Physiology & Behavior 104, no. 5 (October 2011): 1041–47. http://dx.doi.org/10.1016/j.physbeh.2011.07.003.

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50

Barac, Miroljub, Slavica Cabrilo, Sladjana Stanojevic, Mirjana Pesic, Milica Pavlicevic, Branislav Zlatkovic, and Miodrag Jankovic. "Functional properties of protein hydrolysates from pea (Pisum sativum,L) seeds." International Journal of Food Science & Technology 47, no. 7 (May 3, 2012): 1457–67. http://dx.doi.org/10.1111/j.1365-2621.2012.02993.x.

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