作 者：
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机构地区：
华南理工大学轻工与食品学院
出 处：
《食品科学》
2010年第9期62-66,共5页
摘 要：
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-PAGE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:KPIMPI>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。
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.SDS-PAGE analysis and dynamic oscillatory measurement indicated that the time needed to gelation onset（tgel） exhibited a following order,KPIMPISPIRPI,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.
关 键 词：
微生物转谷氨酰胺酶
菜豆属
蛋白凝胶
流变学特性
领 域：
[轻工技术与工程]
[轻工技术与工程]
