Low molecular weight (LMW) collagen peptides show skin and bone health benefits for human. However, the production of LMW collagen peptides from land vertebrate sources remains challenging due to the presence of advanced glycation end products (AGEs) cross-links. In this study, the effect of α-amylase pre-treatment on proteolytic production of LMW collagen peptides by papain was investigated; spent hen, bovine, porcine, and tilapia skin collagens (HSC, BSC, PSC, and TSC, respectively) were chosen. Results showed that pre-treatment with α-amylase considerably improved the production of LMW peptides (<2 kDa) from HSC (33.79–67.66%), PSC (86.03–90.85%), BSC (6.60–28.78%), and TSC (89.92–90.27%). The HSC presented the highest carbohydrate content and was increased the most in LMW peptides after amylase pretreatment. These results suggested that α-amylase could cleave glycosidic bonds of AGEs between collagen and thus enhance the production of LMW collagen peptides.
|State||Published - Aug 1 2021|
Bibliographical noteFunding Information:
This work was supported by grants from the Egg Farmers of Canada (EFC) and the Natural Sciences and Engineering Research Council of Canada (NSERC).
© 2021 Elsevier Ltd
- Low molecular weight peptides
- Spent hen
ASJC Scopus subject areas
- Analytical Chemistry
- Food Science