摘要
本文研究了小麦面筋蛋白(WG)经胰蛋白酶限制性酶解和谷氨酰胺转氨酶(TG酶)交联后其流变特性和热特性的变化,并且对小麦面筋蛋白的结构进行了表征。结果表明,适当的胰蛋白酶限制性酶解有利于TG酶对小麦面筋蛋白的交联作用,使用80 U/g的胰蛋白酶限制性酶解和TG酶交联复合改性效果最为显著,其弹性模量G’和热变性温度Tg分别由2.26 k Pa和55.59℃提高为6.46k Pa和59.17℃。通过对小麦面筋蛋白的结构分析表明,适当的胰蛋白酶限制性酶解能够使小麦面筋蛋白分子间二硫键断裂,表面疏水性增大,从而使紧密地小麦面筋蛋白结构变得较为松散,暴露出更多谷氨酰胺残基供TG酶交联,导致水化小麦面筋蛋白形成更为多孔且致密的小麦面筋蛋白网络结构。但是过度的酶解将不利于TG酶的交联反应。
Changes in the rheological behavior and thermal properties of wheat gluten after trypsin-based enzymatic hydrolysis and the subsequent transglutaminase（TGase） catalyzed cross-linking reactions were investigated and the structure of wheat gluten was characterized.The results indicate that an appropriate degree of trypsin-based partial enzymatic hydrolysis favored TGase cross-linking.The most significant composite modification effect was observed when 80 U/g trypsin-based partial hydrolysis was combined with TGase cross-linking,where the wheat gluten storage modulus（G＇） and thermal denaturation temperature（Tg） increased from 2.26 k Pa and 55.59°C to 6.46 k Pa and 59.17°C,respectively.Structural analysis indicated that an appropriate degree of trypsin-based enzymatic hydrolysis could result in breakage of intermolecular disulfide bonds and an increase in surface hydrophobicity.Consequently,the compact wheat gluten structure became loose and more glutamine residues were exposed to allow TGase cross-linking.This resulted in the formation of a more compact and porous wheat gluten network structure from the hydrated wheat gluten.However,excessive enzymatic hydrolysis was unsuitable for TGase cross-linking.
出处
《现代食品科技》
EI
CAS
北大核心
2016年第3期177-182,280,共7页
Modern Food Science and Technology
基金
国家863计划(2013AA102201)
安徽省科技攻关重大项目(1301031031)
关键词
小麦面筋蛋白
复合改性
性质
结构
wheat gluten
composite modification
characteristics
structure
