LAUSR

Abstract In this study, the mechanism of rapid gelatinization of rabbit skin collagen was examined. Yield and gel strength of gelatin extracted from rabbit skin reached (60.02 ± 2.50)% and (439 ± 17)g, respectively, via pretreatment for 5 min with 1% (w/v) HCl. The results of gelatin extracted from purified rabbit skin collagen demonstrated that a short-term acid pretreatment will cause obvious cleaning loss. SDS-PAGE analysis revealed that the covalent bonds in rabbit skin collagen are easily destroyed by acid, initially destroying the covalent cross-linking between collagen molecules and covalent bonds in a non-helix crystallization. Only when the subunits are exposed will the peptide bonds be destroyed. Analysis of FTIR and SEM suggested that acid pretreatment destroyed the original spatial structure of collagen in a short period of time. Meanwhile, the collagen took on the appearance of orderly wavy folds. As the acid pretreatment continues, the gelatinized collagen will form a new conformation through new hydrogen bonding, and its surface folds became smaller.