超高压处理对羊骨胶原蛋白三级结构的影响  

Effect of Ultra-high Pressure Treatment on Tertiary Structure of Sheep Bone Collagen

作　　者：刘彦秋 都日玛 白杨 娜荷芽 乔丹丹 王月宏 格日勒图[1] 莎日娜[1] Liu Yanqiu;Du Rima;Bai Yang;Na Heya;Qiao Dandan;Wang Yuehong;Ge Riletu;Sha Rina(College of Food Science and Engineering,Inner Mongolia Agricultural University,Huhhot 010018;Zhuozi County Bureau of Agriculture,Animal Husbandry and Science and Technology,Ulanqab 012300,Inner Mongolia)

机构地区：[1]内蒙古农业大学食品科学与工程学院,呼和浩特市010018 [2]卓资县农牧和科技局,内蒙古乌兰察布012300

出　　处：《中国食品学报》2022年第8期207-213,共7页Journal of Chinese Institute Of Food Science and Technology

基　　金：国家肉羊产业技术体系项目(CARS38)。

摘　　要：以羊骨胶原蛋白为研究对象,研究不同超高压压力对胶原蛋白微观形态、热变性温度、吡啶交联物以及空间结构的影响。试验结果表明:超高压处理的胶原蛋白的微观形态在压力100~300 MPa时出现短暂的聚合现象;当压力超过400 MPa时胶原蛋白结构又重新展开。差式扫描量热仪(DSC)结果显示:经超高压处理的胶原蛋白的变性温度由44.9℃(对照组)降为31.7℃;胶原蛋白吡啶交联物羟赖氨酸吡啶啉(HP)和赖氨酸吡啶啉(LP)的含量随超高压压力的增加、保压时间的延长而显著下降(P<0.05);HP和LP与超高压压力和保压时间呈极显著负相关(P<0.01)。Sheep bone collagen was used as the research object to explore the effects of different ultra-high pressure on the microstructure,thermal denaturation temperature,pyridine cross linkers of collagen and the changes of collagen spatial structure.The results showed that the micromorphology of ultra-high treated collagen polymerizes temporarily at a pressure of 100-300 MPa.When the pressure exceeded 400 MPa,the collagen structure expands again.DSC results showed that the denaturation temperature of collagen after ultra-high pressure treatment decreased from 44.9℃(control group)to 31.7℃.The contents of hydroxyl sine pyridine(HP)and lysine pyridine(LP),the cross-linkers of collagen pyridine,were significantly decreased with the increasing of ultra-high pressure pressure and the prolonging of pressure holding time(P<0.05).HP and LP were negatively correlated with ultra-high pressure and holding time(P<0.01).

关 键 词：超高压处理 胶原蛋白 热变性温度 吡啶交联 

分 类 号：TS251.94[轻工技术与工程—农产品加工及贮藏工程]