Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7811777 | PMC |
http://dx.doi.org/10.1002/ctm2.281 | DOI Listing |
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.
View Article and Find Full Text PDFMolecules
September 2024
Department of Medical Physiology, Faculty of Health Sciences, Jagiellonian University Medical College, 31-008 Krakow, Poland.
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.
View Article and Find Full Text PDFInt J Mol Sci
August 2024
Department of Biomedicine, Neuroscience and Advanced Diagnostics (Bi.N.D.), Biology and Genetics Section, University of Palermo, 90133 Palermo, Italy.
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.
View Article and Find Full Text PDFUltrason Sonochem
November 2024
Key Laboratory of Dairy Science, Ministry of Education, College of Food Science, Northeast Agricultural University, Harbin 150030, China. Electronic address:
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.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!