Abstract
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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
