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Structural Properties and Biological Activities of Collagens from Four Main Processing By-Products (Skin, Fin, Cartilage, Notochord) of Sturgeon (Acipenser gueldenstaedti)

文献类型： 外文期刊

作者： Meng, Dawei 1 ; Wei, Qiwei 2 ; Takagi, Yasuaki 3 ; Dai, Zhiyuan 1 ; Zhang, Yan 4 ;

作者机构： 1.Zhejiang Gongshang Univ, Inst Seafood, Zhejiang Prov Joint Key Lab Aquat Prod Proc, 149 JiaoGong Rd, Hangzhou 310012, Peoples R China

2.Chinese Acad Fishery Sci, Yangtze River Fisheries Res Inst, Key Lab Freshwater Biodivers Conservat, Minist Agr & Rural Affairs, Wuhan 430223, Peoples R China

3.Hokkaido Univ, Fac Fisheries Sci, 3-1-1 Minato Cho, Hakodate, Hokkaido 0418611, Japan

4.Zhejiang Univ, Liangzhu Lab, Med Ctr, Hangzhou 310058, Zhejiang, Peoples R China

关键词： Sturgeon by-products; Collagen; Structural properties; Fibril-forming characteristics; Collagen peptides; Antioxidant activity

期刊名称：WASTE AND BIOMASS VALORIZATION （ 影响因子：3.2； 五年影响因子：3.4 ）

ISSN： 1877-2641

年卷期： 2023 年

页码：

收录情况： SCI

摘要： During the processing of sturgeon, large amounts of by-products, such as skin, fin, cartilage, and notochord, are produced. These by-products have not been effectively used, resulting in a serious waste of sturgeon resources. In this study, we aimed to obtain the collagen from these by-products and evaluate the fibril-forming characteristics of the collagen molecules and the antioxidant activity of the collagen peptides. The structural properties of pepsin-soluble collagen were analyzed by SDS-PAGE and FTIR. Collagen fibril- forming characteristics were detected by turbidity assay and SEM observation. The antioxidant activities of collagen peptides were determined by Hydroxyl and ABTS radical scavenging assays. SDS-PAGE results showed that the skin and fin collagens were characterized as type I collagen, and the cartilage and notochord collagens were characterized as type II collagen. Sturgeon type II collagens could only be self-assembled into fibrils at low phosphate ion concentration, whereas sturgeon type I collagens could be self-assembled into fibrils at long range of phosphate ion concentrations. The fibril-forming ability of sturgeon type I collagen was higher than that of porcine type I collagen. The fibril diameter of type I collagen was higher than that of type II collagen. The antioxidant activity of notochord and skin collagen peptides was higher than that of the other two collagen peptides. The results of this study will provide helpful information for the application of sturgeon collagen in the functional food and biomedical material industries. Meanwhile, it will promote the effective use of collagen from different sturgeon by-products. [Graphics] .

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