TY - JOUR
T1 - Amylase enhances production of low molecular weight collagen peptides from the skin of spent hen, bovine, porcine, and tilapia
AU - Hong, Hui
AU - Fan, Hongbing
AU - Roy, Bimol C.
AU - Wu, Jianping
N1 - Publisher Copyright:
© 2021 Elsevier Ltd
PY - 2021/8/1
Y1 - 2021/8/1
N2 - 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.
AB - 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.
KW - Amylase
KW - Bovine
KW - Collagen
KW - Low molecular weight peptides
KW - Porcine
KW - Spent hen
KW - Tilapia
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U2 - 10.1016/j.foodchem.2021.129355
DO - 10.1016/j.foodchem.2021.129355
M3 - Article
C2 - 33667924
AN - SCOPUS:85101757447
SN - 0308-8146
VL - 352
JO - Food Chemistry
JF - Food Chemistry
M1 - 129355
ER -