Physicochemical properties of acid- and pepsin-soluble collagens from the cartilage of Siberian sturgeon.

Abstract

To look for the collagen alternatives of mammalian cartilages from aquatics and their by-products, acid-soluble collagen (ASC-SC) and pepsin-soluble collagen (PSC-SC) were extracted from cartilages of Siberian sturgeon (Acipenser baerii) with yields of 27.13 ± 1.15 and 14.69 ± 0.85% on dry weight basis. ASC-SC and PSC-SC had glycine as the major amino acid with the contents of 326.8 and 327.5 residues1000 residues-1, and their contents of proline and hydroxyproline were 205.9 and 208.0 residues1000 residues-1. ASC-SC and PSC-SC comprised type I collagen ([α1(I)]2α2(I)) and type II collagen ([α1(II)]3) on the literatures and results of amino acid composition, SDS-PAGE pattern, UV, and FTIR spectra. Meanwhile, FTIR spectra data indicated that there were more hydrogen bonds in ASC-SC and more intermolecular crosslinks in PSC-SC. The maximum transition temperature (Tmax) of the ASC (28.3°C) and PSC (30.5°C) was lower than those of collagens from mammalian cartilages (> 37°C). ASC-SC and PSC-SC showed high solubility in the acidic pH ranges and the solubility decreased in the presence of NaCl at concentrations above 3%. Zeta potential studies indicated that both ASC-SC and PSC-SC exhibited a net zero charge at pH6.30 and 6.32. SEM results indicated that ASC-SC and PSC-SC presented irregular dense sheet-like film linked by random-coiled filaments. Therefore, collagens from Siberian sturgeon cartilages might be the suitable alternatives of the collagens of mammal cartilages as functional ingredient to treat some diseases.