Properties and Characteristics of Acid-Soluble Collagen from Salmon Skin Defatted with the Aid of Ultrasonication

Abstract

Salmon skin, a byproduct from the deskinning process, can be used as an alternative source of collagen. Due to the high fat content in skin, the defatting process is required prior to extraction. The properties and characteristics of acid-soluble collagen (ASC) from salmon skin (Oncorhynchus nerka), defatted using isopropanol without and with ultrasonication (70% amplitude for 10 min), were investigated. The ASC from the skin that was defatted with aid of ultrasonication (U-ASC) exhibited lower (p w/w, dry weight basis). U-ASC had a higher hydroxyproline content (49.15 mg/g dry sample) and maximum transition temperature (Tmax) (11.6 °C) than C-ASC (collagen extracted from skin defatted without ultrasonication). Both of the ASCs were classified as type I collagen. C-ASC and U-ASC had isoelectric points of 7.17 and 7.40, respectively. Fourier transform infrared (FTIR) and circular dichroism spectra reconfirmed the triple-helix structure of both ASCs. The major amino acid of both collagens was glycine (297–308 residues/1000 residues). A high amount of imino acid (191–193 residues/1000 residues) was also found. After gastrointestinal digestion, the degree of hydrolysis of the digested U-ASC (23.19%) was slightly higher than that of the digested C-ASC (22.31%). However, both digests had no differences in antioxidant activities. Both of the ASCs could be therefore used as functional ingredient.

Keywords

• salmon skin
• collagen
• defatting process
• ultrasonication
• digestion