Authors
Michał Czelej, Katarzyna Garbacz, Tomasz Czernecki, Kamila Rachwał, Jacek Wawrzykowski, Adam Waśko
Published in
Molecules (Basel, Switzerland). Volume 30. Issue 7. Mar 25, 2025. Epub Mar 25, 2025.
Abstract
Bioactive peptides derived from milk proteins offer promising potential that can be unlocked through hydrolysis. Enzymatic hydrolysis is particularly noteworthy because of its mild conditions and its efficacy in producing peptides with various biological activities. This study focused on creating whey protein hydrolysates using three enzymes: pepsin, trypsin, and papain. The degree of hydrolysis and the antioxidant properties of the resulting peptides were evaluated, and papain demonstrated the highest degree of hydrolysis, leading to its selection for further investigation. LC-MS was employed to identify peptide sequences from the papain-derived hydrolysate, resulting in the identification of 107 distinct peptide sequences These peptides were predicted to exhibit a range of potential biological activities, including antihypertensive, antidiabetic, antioxidant, antimicrobial, and immunomodulatory effects, as well as roles in regulating glucose homeostasis, maintaining cardiovascular health, and supporting overall metabolic function. In vitro tests revealed the significant antioxidant and antibacterial properties of the hydrolysate, confirming the potential of papain-derived peptides for use in functional food and pharmaceutical applications. The novelty of this study lies in the identification of novel peptides with promising biological activities. Additional in vitro and in vivo studies are required to fully elucidate the health benefits of these peptides.
PMID:
40286053
Bibliographic data and abstract were imported from PubMed on 27 Apr 2025.
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