Journal
CRITICAL REVIEWS IN FOOD SCIENCE AND NUTRITION
Volume -, Issue -, Pages -Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/10408398.2022.2145262
Keywords
Microorganisms; enzyme; biocatalysis; bioactivities; bioactive peptides
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Funding
- Universidade Federal da Fronteira Sul (UFFS) [PES-2020-0264, 270/GR/UFFS/2020]
- Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq) [308880/2021-8]
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Enzymatic hydrolysis is an important strategy to release bioactive peptides from food proteins. Unconventional microbial proteases (UMPs) have gained attention in recent years for their potential to produce bioactive protein hydrolysates. This review discusses the production of UMPs and their use in obtaining bioactive protein hydrolysates, with a focus on antioxidant and anti-hypertensive properties. The review also highlights the in vivo bioactivities of these hydrolysates and peptides. Further research is needed to explore the commercial utility of UMPs and the obtained hydrolysates.
Enzymatic hydrolysis is the most prominent strategy to release bioactive peptides from different food proteins and protein-rich by-products. Unconventional microbial proteases (UMPs) have gaining increased attention for such purposes, particularly from the 2010s. In this review, we present and discuss aspects related to UMPs production, and their use to obtain bioactive protein hydrolysates. Antioxidant and anti-hypertensive potentials, commonly evaluated through in vitro testing, are mainly reported. The in vivo bioactivities of protein hydrolysates and peptides produced through UMPs action are highlighted. In addition to bioactivities, enzymatic hydrolysis acts by modulating the functional properties of proteins for potential food uses. The compiled literature indicates that UMPs are promising biocatalysts to generate bioactive protein hydrolysates, adding up to commercially available enzymes. From the recent interest on this topic, continuous and in-depth research is needed to advance toward the applicability and commercial utility of both UMPs and obtained hydrolysates.
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