Characterization of collagen from mantle of scallop Chlamys nobilis by different extraction methods
WANG Wen, FENG Chang, LIN Haisheng*, QIN Xiaoming, CAO Wenhong, ZHANG Chaohua, GAO Jialong, ZHENG Huina, CHEN Yibin
1.College of Food Science and Technology, Guangdong Ocean University, Zhanjiang 524088, China; 2.Guangdong Provincial Key Laboratory of Aquatic Products Processing and Safety, Key Laboratory of Advanced Processing of Aquatic Products of Guangdong Higher Education Institution, National Research and Development Branch Center for Shellfish Processing(Zhanjiang), South China Sea Bio-Resource Exploitation and Utilization Collaborative Innovation Center, Guangdong Ocean University, Zhanjiang 524088, China; 3.Hainan Shengmeinuo Biotechnology Company Limited, Chengmai 571925, China
Abstract: In order to compare basic properties of collagen from mantle of scallop Chlamysnobilis, collagens were extracted from the mantle of the scallop by acid-enzymatic method and hot water method, named acid-pepsin soluble collagen (A-PSC(Cn)) and hot water soluble collagen (HSC(Cn)), respectively, and then the amino acid composition, molecular weight, microstructure and thermal denature-temperature of collagen were determined. Results showed that there was higher collagen extraction rate by hot water method than that by acid-pepsic method, with the maximal content of 13.27 g/100 g prot in Gly, 10.45 g/100 g prot in Glu and 6.19 g/100 g prot in Pro in HSC(Cn), and 10.16 g/100 g prot in Glu, 7.92 g/100 g prot in Gly and 5.77 g/100 g prot in Asp in A-PSC(Cn). UV and IR spectra showed that HSC(Cn) and A-PSC(Cn) had strong absorption peak at 220 nm, and typical characteristic bands of collagen (amide A, B, Ⅰ, Ⅱ and Ⅲ). SDS-PAGE reveald that γ chain, β chain, α1 chain and α2 chain were observed in both collagens, and were identified as type Ⅰ collagen. The observation of scanning electron microscopy (SEM) found that A-PSC(Cn) was loose and porous, and that HSC(Cn) was compact and layered. It was found that HSC (Cn) possessed higher thermal denaturation temperature than A-PSC(Cn) did, indicating that both HSC(Cn) and A-PSC(Cn) were all type Ⅰ collagen, and there were differences in its structural characteristics and physical and chemical properties. A-PSC(Cn) has a complete triple helical structure, high purity, loose and porous characteristics, and HSC(Cn) has a high content of amino acid. The findings indicate that different extraction methods can be used to develop collagen products from scallop Chlamysnobilis according to research needs.