Amylase enhances production of low molecular weight collagen peptides from the skin of spent hen, bovine, porcine, and tilapia

Hui Hong, Hongbing Fan, Bimol C. Roy, Jianping Wu

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

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.

Original languageEnglish
Article number129355
JournalFood Chemistry
Volume352
DOIs
StatePublished - Aug 1 2021

Bibliographical note

Publisher Copyright:
© 2021 Elsevier Ltd

Keywords

  • Amylase
  • Bovine
  • Collagen
  • Low molecular weight peptides
  • Porcine
  • Spent hen
  • Tilapia

ASJC Scopus subject areas

  • Analytical Chemistry
  • Food Science

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