糖基化与胰蛋白酶酶解对大豆蛋白构象和功能性质的影响  

Effects of glycosylation and trypsin enzymolysis on conformation and functional properties of soybean protein

作　　者：宋春丽[1] 任健[1] 陈佳鹏[1] 康文娜 张新 

机构地区：[1]齐齐哈尔大学食品与生物工程学院黑龙江省普通高校农产品加工重点实验室,黑龙江齐齐哈尔161006

出　　处：《中国油脂》2017年第12期22-25,共4页China Oils and Fats

基　　金：国家自然科学基金资助项目(31401639);黑龙江省本科高等学校青年创新人才支持计划(UNPYSCT-2015094)

摘　　要：利用转谷氨酰胺酶催化壳寡糖与大豆蛋白分子发生交联反应制备糖基化大豆蛋白,随后用胰蛋白酶酶解制备水解度分别为1%、5%、10%和15%的大豆蛋白酶解产物,分析糖基化及酶解对大豆蛋白的三级结构和功能性质的影响。结果表明:糖基化大豆蛋白及其酶解产物具有更加疏松的三级结构;pH 4.0、7.0的酶解产物(DH15%)经过热处理(85℃)后,其热稳定性分别为50.74%和67.66%,热稳定性较好;糖基化提高了大豆蛋白的泡沫稳定性,水解度为10%的酶解产物具有最高的起泡性;糖基化也能够提高大豆蛋白的乳化稳定性,水解度为5%的酶解产物具有较好的乳化稳定性;大豆蛋白修饰产物的体外消化性不同,糖基化大豆蛋白对胃蛋白酶的敏感性差,而其酶解产物对胰蛋白酶的敏感性差。The glycosylated soybean protein （GSPI） was first generated from soybean protein isolate （SPI） and oligochitosan catalyzed by transglutaminase and then hydrolyzed by trypsin to prepare hydrolysates with hydrolysis degrees （DH） of 1%, 5%, 10% and 15%. The effects of glysosylation and enzymolysis on the tertiary structure and functional properties of SPI were investigated. The results showed that GSPI and its hydrolysates had more loosen tertiary structure than SPI. The thermal stabilities of GSPI hydrolysates（DH 15%） after thermal treatment （85℃）were 50.74% at pH 4.0 and 67.66% at pH 7.0, respectively, indicating that thermal stabilities of GSPI hydrolysates were better. GSPI showed an increasing foam stability, and its trypsin hydrolysates with DH 10% exhibited the highest foamability. GSPI also showed an increased emulsion stability, and its trypsin hydrolysates with DH 5% exhibited better emulsion stability. The modified SPI showed different in vitro digestibilities. GSPI was less sensitive to pepsin hydrolysis, while its hydrolysates were less sensitive to trypsin hydrolysis.

关 键 词：大豆分离蛋白 糖基化 胰蛋白酶酶解 三级结构 功能性质 

分 类 号：TS201.21[轻工技术与工程—食品科学]