Enzyme-assisted extraction and properties of collagen from Basa fish (Pangasius bocourti) skin

Abstract

Abstract Type I collagen is a fibrillar structure collagen, which plays an important role as the essential structural composition and mechanical scaffold of several tissues. The aim of the study was to determine the properties of type I collagen extracted from Basa fish skin using acetic acid as the extraction solvent with the assistance of pepsin. The collagen extraction yield was 520.5 mg/g of fresh fish skin on the basis of lyophilized dry weight. The denaturation temperature (Td) of collagen was 34.8 °C by measuring its viscosity. The identity and purity of collagen protein were examined by ultraviolet-visible spectroscopy (UV-Vis) at 230 nm. Based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), the molecular weight (Mw) of collagen α1, α2, and β subunits were approximately 130, 118, and above 200 kDa, respectively. By high performance liquid chromatography (HPLC), 17 proteinogenic amino acids were found in the collagen sample, in which the hydroxyproline content was 68.3 mg/g. The scanning electron microscope (SEM) images confirmed the fibril structure of collagen. Fourier transform infrared spectroscopy (FTIR) spectrum indicated characteristic bands according to the presence of amide A, B, I, II, and III bonds in collagen chemical structure. Therefore, purified collagen obtained from this study can be further used in various fields of application.