刺参体壁酶促溶性胶原蛋白的热变性  

Thermal Denaturation of Pepsin-solubilized Collagen from Sea Cucumber Body Wall

作　　者：傅宝尚 侯红漫[1] 张公亮[1] 毕景然[1] FU Baoshang;HOU Hongman;ZHANG Gongliang;BI Jingran(School of Food Science and Technology,Dalian Polytechnic University,Dalian 116034,China)

机构地区：[1]大连工业大学食品学院,辽宁大连116034

出　　处：《食品科学》2022年第10期29-35,共7页Food Science

基　　金：“十三五”国家重点研发计划重点专项(2017YFC1600403);辽宁省“兴辽英才计划”项目(XLYC1808034);辽宁省农业重大专项计划项目(2020JH1/10200001)。

摘　　要：从刺参(Stichopus japonicus)体壁中提取酶促溶性胶原蛋白(pepsin-solubilized collagen,PSC),并对其热处理过程中的降解规律及结构变化进行研究,发现PSC变性温度为35.3℃,当加热温度为40~70℃时,PSC三螺旋结构解缠绕,α-螺旋结构破坏严重,但在冷却后依靠分子间氢键和二硫键的相互作用仍可形成强凝胶体系;当加热温度超过70℃时,PSC的α-肽链开始逐渐降解成小分子多肽,冷却后分子间交联作用较差,不易形成凝胶体系。In this work,pepsin-solubilized collagen(PSC)was extracted from the body wall of sea cucumber,and its degradation and structural changes during heat treatment were studied.It was found that the denaturation temperature of PSC was 35.3℃.When PSC was heated at 40–70℃,the triple helix structure was coiled,and theα-helix structure was severely damaged;but after cooling,a strong gel system could still be formed by intermolecular hydrogen bonding and disulfide bonding interactions.When the heating temperature exceeded 70℃,theα-peptide chain of PSC began to be gradually degraded into small polypeptides,and the intermolecular cross-linking effect was too poor to form a gel system.

关 键 词：胶原蛋白 热变性 降解 凝胶 

分 类 号：TS251.92[轻工技术与工程—农产品加工及贮藏工程]