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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7811777PMC
http://dx.doi.org/10.1002/ctm2.281DOI Listing

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In Silico Hydrolysis of Lupin ( L.) Conglutins with Plant Proteases Releases Antihypertensive and Antidiabetic Peptides That Are Bioavailable, Non-Toxic, and Gastrointestinal Digestion Stable.

Int J Mol Sci

November 2024

Clinical and Research Laboratory (LACIUS, C.N., CONAHCYT National Laboratory, LANIBIOC), Deparment of Chemical, Biological, and Agricultural Sciences (DC-QB), Faculty of Biological and Health Sciences, University of Sonora, Navojoa 85880, Sonora, Mexico.

Lupin ( L.) proteins are potential sources of bioactive peptides (LBPs) that can inhibit dipeptidyl peptidase IV (DPP-IV) and angiotensin I-converting enzyme (ACE-I) activity. However, the capacity of different enzymes to release LBPs, the pharmacokinetic and bioactivities of the peptides released, and their binding affinities with the active sites of DPP-IV and ECA-I are topics scarcely addressed.

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The byproduct from wheat starch production contains approximately 70% gluten (WG) and is an inexpensive but demanding protein raw material for the food industry. This study attempted to determine the optimal hydrolysis conditions for such raw material to obtain peptides combining beneficial functional characteristics with health-promoting activity. The proteases Bromelain, Alcalase, Flavourzyme, and a protease from were used for hydrolysis.

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Article Synopsis
  • * The study explored the effects of a natural compound combination (escin-bromelain-ginkgo biloba-sage miltiorrhiza, or EBGS) on inhibiting platelet adhesion to damaged blood vessels, a crucial step in thrombus formation.
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We previously published the microbial profile of burn wounds managed with NexoBrid® in Pinderfields Regional Burns Centre, Wakefield, UK. Our results showed no significant changes in bacterial colonisation in burn wounds debrided with NexoBrid®. Previous studies described the antimicrobial properties of bromelain enzyme.

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Whey protein is an important food ingredient, but it is also considered a major food allergen. The aim of this study was to investigate the effect of ultrasound pretreatment on the structure, IgE binding capacity, functional properties and biological activity of whey protein isolate (WPI) hydrolysates (WPH), including WPI hydrolyzed by a combination of enzymes from Bromelain and ProteAXH (BA-WPI) and WPI hydrolyzed by a combination of enzymes from Papain W-40 and ProteAXH (PA-WPI). The IgE binding capacity of BA-WPI and PA-WPI was reduced to 40.

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