文献类型：期刊文献

中文题名：不同方法提取红鳍笛鲷鱼鳞胶原蛋白的结构和理化特性研究

英文题名：Characterization of collagens from scale of Lutjanus erythropterus by different extraction methods

作者：黄家宝[1,2];邓旗[1,2];薛梦凡[1,2];任雪婷[1,2];吴雨盈[1,2];孙力军[1,2];房志家[1,2];温婉宁[1,2]

机构：[1]广东海洋大学食品科技学院,广东省水产品加工与安全重点实验室,广东省海洋食品工程技术研究中心,广东省现代农业科技创新中心,广东省水产预制食品加工与品质控制工程技术研究中心,广东湛江524088;[2]海洋食品精深加工关键技术省部共建协同创新中心,大连工业大学,辽宁大连116034

年份：2024

卷号：50

期号：9

起止页码：210

中文期刊名：食品与发酵工业

外文期刊名：Food and Fermentation Industries

收录：北大核心2023、CSTPCD、、Scopus、CSCD2023_2024、北大核心、CSCD

基金：国家自然科学基金青年科学基金项目(32302186)。

语种：中文

中文关键词：红鳍笛鲷;鱼鳞;胶原蛋白;理化性质;结构表征

外文关键词：Lutjanus erythropterus;scale;collagen;physicochemical properties;structural characterization

中文摘要：为探明不同提取方法对红鳍笛鲷(Lutjanus erythropterus)鱼鳞胶原蛋白理化特性的影响,以红鳍笛鲷为原料,分别提取酸溶性胶原蛋白(acid soluble collagen,ASC)、酶溶性胶原蛋白(pepsin soluble collagen,PSC)及热水溶性胶原蛋白(hot water soluble collagen,HSC),对比分析3种胶原蛋白提取率、得率及纯度的差异,并测定其氨基酸组成、分子质量、二级结构、Zeta电位、溶解性以及微观结构等理化特性。结果表明,热水法提取率最高,为45.25%,其次为胃蛋白酶法;HSC、ASC、PSC的亚氨酸含量分别为18.28%、17.54%和18.30%。HSC、ASC和PSC均为I型胶原蛋白,包含两条α链(α1和α2),ASC比PSC的β链含量高,HSC、PSC的γ带消失;ASC、PSC具有相似的红外光谱,且保留了完整的三螺旋结构,HSC的三螺旋结构被破坏;HSC、ASC、PSC的净电荷零点为5~6;ASC、PSC在pH 5~11中溶解度较低;扫描电镜显示,ASC呈无序纤维状结构,PSC呈致密多孔网状结构,HSC则基本为薄片状。3种提取方法提取的胶原蛋白均有I型胶原蛋白特征,其结构特征及理化性质均存在差异,可根据需求选择特定的胶原蛋白提取方法用以开发特定的产品。

外文摘要：To explore the impact of various extraction techniques on the physicochemical properties of collagen in Lutjanus erythropterus scales,acid-soluble collagen(ASC),pepsin-soluble collagen(PSC),and hot water-soluble collagen(HSC)were extracted.The extraction rates,yields,and purities of the three methods were compared and analyzed.The amino acid composition,molecular weight,secondary structure,Zeta potential,solubility,and microstructure of both collagens were evaluated.The findings revealed that the highest collagen extraction rate was achieved using the hot water method(45.25%),followed by the pepsin method.The imide acid content of HSC,ASC,and PSC was 18.28%,17.54%,and 18.30%,respectively.All collagens were identified as type I collagen,consisting of twoαchains(α1 andα2).ASC exhibited a higherβchain content than PSC,while both HSC and PSC lacked theγband.ASC and PSC displayed similar IR spectra and maintained the intact triple helix structure,whereas hot water extraction resulted in triple helix degradation.Zeta potential analysis revealed a net charge of zero for HSC,ASC,and PSC within the pH range of 5-6.ASC and PSC exhibited high solubility within a neutral to alkaline pH range(5-11).Scanning electron microscope results illustrated that ASC possessed a disordered fibrous structure,PSC had a dense porous network structure,and HSC appeared primarily laminar.Although all three extraction methods yielded type I collagen,their structural and physicochemical attributes differed.Therefore,specific collagen extraction methods can be selected to develop diverse products based on specific requirements.