菜豆属豆类蛋白酶促凝胶性能比较研究-食品科学.PDF

菜豆属豆类蛋白酶促凝胶性能比较研究-食品科学.PDF

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菜豆属豆类蛋白酶促凝胶性能比较研究-食品科学

62 2010, Vol. 31, No. 09 食品科学 ※基础研究 陈 玲,唐传核,张业辉 (华南理工大学轻工与食品学院,广东广州 510640) :研究比较芸豆(KPI) 、红豆(RPI)和绿豆(MPI)3 种菜豆属类分离蛋白和大豆分离蛋白(SPI)在微生物转谷氨酰 胺酶(MTGase)作用下的凝胶性能,并对其凝胶形成机理加以分析。SDS电泳和哈克流变分析结果表明: 菜豆类分离蛋白是MTGase 的良好作用底物,初始成胶所需时间:KPI <MPI <SPI <RPI 。而酶反应后的凝胶 G ′值:RPI >MPI >KPI >SPI ,即KPI 形成凝胶最快,而RPI 最终成胶的强度最大;通过对不同溶剂下胶体溶 解性的比较发现,除了酶共价交联外,静电相互作用,疏水作用及氢键都是形成凝胶的主要作用力,由于菜豆属 类蛋白主要富含7S 球蛋白(不含二硫键) ,二硫键对其凝胶的稳定性作用不如SPI 明显。 微生物转谷氨酰胺酶;菜豆属;蛋白凝胶;流变学特性 Enzymatic-induced Gelation Properties of Protein Isolates from Phaseolus CHEN Ling ,TANG Chuan-he ,ZHANG Ye-hui (College of Light Industry and Food Science, South China University of Technology, Guangzhou 510640, China) Abstract:Microbial transglutaminase-induced (MTGase) gelation properties of protein isolates from red kidney bean, red bean, mung bean and soybean (designated as KPI, RPI, MPI and SPI) were investigated. SDSanalysis and dynamic oscillatory measurement indicated that the time needed to gelation onset (tgel) exhibited a following order, KPI >MPI >SPI>RPI, whereas the order of G ′ value after MTGase incubation was RPI >MPI >KPI >SPI. Protein solubility analysis of MTGase-induced gels suggested that electrostatic interaction, hydrophobic interaction and hydrogen bonds except covalent bonds were the primary forces responsible for the formation of gels. In addition, disulfide bonds were also involved in gelation. Therefore, compared to SPI, the effects of protein isolates from Phaseolus on gelation stability were less obvious due to the devoid of disulfide bonds among individual subunits in protein isolates from Phaseolus . Key words :Microbial transglutaminase-induced ;Phaseolus ;protein gel ;rheological measurement 中图分类号:TS201.7 文献标识码:A

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