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

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 ?-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 ?-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 ?-amylase could cleave glycosidic bonds of AGEs between collagen and thus enhance the production of LMW collagen peptides.

Automated summary

The use of ?-amylase pre-treatment significantly improves the production of low molecular weight collagen peptides from spent hen, porcine, bovine, and tilapia skin sources. Among these sources, spent hen skin has the highest carbohydrate content and shows the greatest increase in LMW peptides after amylase pretreatment. This suggests that ?-amylase can cleave the glycosidic bonds of AGEs in collagen and enhance the production of LMW collagen peptides.