Structural characteristics, component interactions and functional properties of gelatins from three fish skins extracted by five methods
文献类型: 外文期刊
作者: Yu, Ermeng 1 ; Pan, Chuanyan 2 ; Luo, Xu 2 ; Ruan, Qiufeng 2 ; Chen, Weijie 2 ; Fang, Yikun 2 ; Wang, Kang 4 ; Qin, Yanyang 2 ; Lv, Min 2 ; Ma, Huawei 2 ;
作者机构: 1.CAFS, Guangdong Prov Key Lab Aquat Anim Immunol & Sustai, Pearl River Fisheries Res Inst, Guangzhou 510380, Peoples R China
2.Guangxi Acad Fishery Sci, Guangxi Key Lab Aquat Genet Breeding & Hlth Aquacu, Nanning 530021, Peoples R China
3.Chinese Acad Agr Sci, Lab Aquaculture & Nutr, Beijing 100081, Peoples R China
4.Guangxi Univ, Coll Anim Sci & Technol, Nanning 530005, Peoples R China
关键词: Fish skin gelatin; Structural characteristics; Component interactions; Functional properties; High performance liquid chromatography-mass; spectrometry (HPLC-MS); Dry salting and wet salting methods
期刊名称:INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES ( 影响因子:8.2; 五年影响因子:7.8 )
ISSN: 0141-8130
年卷期: 2023 年 248 卷
页码:
收录情况: SCI
摘要: Fish skin gelatin is an important functional product used in food, medicine and other industries. However, the structure and function of gelatins extracted with different methods differ significantly, thus limiting its production and application. This study used dry-salting, wet-salting, pepsin, acid and heat methods to extract gelatins from the skins of tilapia, grass carp and sea perch. Then, their structural characteristics (micro- and ultrastructure, amyloid-like fibril, etc.) and functional properties (viscosity, emulsifying performance, antioxidant abilities, etc.) were analyzed, and interaction between gelatin components were also explored. According to the results, the gelatins extracted with dry-salting and wet-salting methods had better reticular structure, larger fiber length/height, and higher viscosity properties, emulsifying and antioxidant capacity. The gelatin extracted by applying heat has the highest gel strength, and the gelatin extracted using pepsin had better thermal stability, water absorption capacity, and fat absorption capacity. Further analysis of component interaction showed that 11 types of collagens detected in the gelatins might promote the conversion of collagen to gelatin through selfassembly ability. The co-assembly of different types of collagens enhanced the properties of gelatin. Decorin had a positive effect on gelatin network structure, but Metallopeptidase inhibited the formation of network structure. Different methods can produce personalized gelatin products according to specific needs. The mining of component interaction would reveal the mechanism of gelatin formation and promote the development of gelatin synthetic biology.
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