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

Hong, H., H. Fan, B. C. Roy, and J. Wu. 2021. Amylase enhances production of low molecular weight collagen peptides from the skin of spent hen, bovine, porcine, and tilapia. Food Chemistry 352:129355. doi https://doi.org/10.1016/j.foodchem.2021.129355

PIP Author(s)

Categories

Applied Poultry Science Webinar 2020 maintenance Pathogens & Protection sexual maturity water purification egg ACP webinars laying hen gut microbiota feed restriction Prairie Poultry Meeting 2020 antioxidants Publication faba bean flock talk Research Showcase 2021 Precision Feeding egg white energy partitioning model Gompertz model bone Research Showcase 2023 broiler feather egg yolk chicken Keratin biopolymers growth model growth performance broiler breeder Spent hen Event Proceedings peer-reviewed Presentation News Inflammation PIP Newsletter phytase Collagen People of Poultry Uncategorized Small Flock Poultry Course Research Showcase 2022 Innovation Showcase carcass

About

Publication Metrics

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. The objective of this study was to investigate the effect of alpha-amylase pre-treatment on proteolytic production of LMW collagen peptides by papain using spent hen, bovine, porcine, and tilapia skin collagens (HSC, BSC, PSC, and TSC, respectively).

Approach

Frozen spent hen (about 17 months) (n = 10), fresh tilapia skin (about 6 months old), porcine skin (about 6 months old) fresh bovine hides were obtained and taken to laboratory where histological analysis of skin was carried out. The standard AOAC methods were used to determine the proximate composition (including carbohydrate content) of the skin collagen samples. Total nitrogen, protein, fat, ash and moisture content were also measured. Skin samples were sliced and grounded. Fifty grams of skin sample were then incubated with α-amylase (2% enzyme/substrate [E/S], w/w protein basis) in 500 mL 50 mM sodium phosphate buffer (pH 5.4) at 20 °C for 6 h under continual stirring for extraction of collagen. After α-amylase pre-treatment, the skin collagens were further hydrolyzed by papain to produce LMW peptides.

Analysis of Results

There were significant differences of glycoprotein (collagen) morphology among HSC, BSC, PSC, and TSC. The carbohydrate content of HSC, BSC, PSC, and TSC and was found to be 18.88 ± 0.66%, 4.48 ± 2.73%, 3.55 ± 2.00%, and 2.69 ± 0.48%, respectively. HSC showed comparatively lower MW polypeptides than BSC, PSC, and TSC. This might be due to the breakdown of collagen polypeptides during the extraction process of HSC. Glycopeptides were only observed in HSC and HP (horseradish peroxidase, positive control). Glycopeptides noticed in HSC were less than 10 kDa. However, no glycopeptides were observed in amylase pretreated HSC (HSC-Amylase-Papain). This indicates that amylase cleaved the AGE cross-links of collagen molecules, suggesting its efficiency in producing low MW peptides by papain hydrolysis. Glycopeptides were not detected in BSC, PSC, and TSC. In the current investigation, α-amylase pre-treatment considerably enhanced the production of LMW peptides.

Application

The current study, for the first time, reported the production of LMW peptides from skins of spent hen, bovine, porcine, and tilapia by employing α-amylase pre-treatment before papain hydrolysis. The results indicated that pre-treatment with α-amylase significantly enhanced the production of LMW peptides from spent hen, bovine, porcine, and tilapia skin collagens. It is suggested that α-amylase cleaved the glycosidic bonds of AGEs cross-links and thereby enhanced the production of LMW collagen peptides. The LMW peptides obtained in this study could be developed as functional ingredients in food and pharmaceutical products. Prior to that, however, bioactivities of these LMW peptides are warranted to be investigated in animal models.

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.