Physicochemical and Functional Properties of Type I Collagens in Red Stingray (Dasyatis akajei) Skin.

Junde Chen,Kunyuan Wu,Yushuang Li,Zhongbao Li,Ruizao Yi,Shenjia Shi,Jianying Li,Sijia Wu

doi:10.3390/md17100558

Junde Chen, Kunyuan Wu + Show 6 more

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https://doi.org/10.3390/md17100558

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Abstract

Collagen is widely used in the pharmaceutical, tissue engineering, nutraceutical, and cosmetic industries. In this study, acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) were extracted from the skin of red stingray, and its physicochemical and functional properties were investigated. The yields of ASC and PSC were 33.95 ± 0.7% and 37.18 ± 0.71% (on a dry weight basis), respectively. ASC and PSC were identified as type I collagen by Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis (SDS-PAGE) analysis, possessing a complete triple helix structure as determined by UV absorption, Fourier transform infrared, circular dichroism, and X-ray diffraction spectroscopy. Contact angle experiments indicated that PSC was more hydrophobic than ASC. Thermal stability tests revealed that the melting temperature of PSC from red stingray skin was higher than that of PSC from duck skin, and the difference in the melting temperature between these two PSCs was 9.24 °C. Additionally, both ASC and PSC were functionally superior to some other proteins from terrestrial sources, such as scallop gonad protein, whey protein, and goose liver protein. These results suggest that PSC from red stingray skin could be used instead of terrestrial animal collagen in drugs, foods, cosmetics, and biological functional materials, and as scaffolds for bone regeneration.

Highlights

Collagen, the most abundant protein in vertebrates, is a major structural protein in the connective tissue of animal skin and bone, and constitutes about 30% of the total proteins [1]
The yield of pepsin-soluble collagen (PSC) from red stingray skin was higher than acid-soluble collagen (ASC), indicating that the breakdown of covalent cross-links by pepsin digestion of the terminal peptides of collagen results in the dissolution of more collagen triple helix structures by acetic acid, providing a higher collagen yield [18]
The SDS-PAGE protein patterns of red stingray collagens were compared using the profile of commercial rat rail type I collagen, which was used as a reference for the collagen type I protein pattern

Summary

Introduction

The most abundant protein in vertebrates, is a major structural protein in the connective tissue of animal skin and bone, and constitutes about 30% of the total proteins [1]. Twenty-eight types of collagens have been identified, each possessing a unique amino acid sequence, structure, and function [2]. Type I is the most promising in terms of its marketable prospects [3]. It possesses a stable triple helix structure, which is formed by three α subunits and a right-handed helix. The hydrogen bond between glycine and an amide group in the adjacent α chains is the key to a stable collagen triple helix. In type I collagens, a very short terminal region (telopeptide) is present, but it does not participate in the triple helix structure [4]. Pepsin is used to digest peptide chains in the telopeptide region of collagen

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