本研究旨在研究pH3.0和7.0的十二种豆类蛋白分离物的热诱导凝胶的流变学和质地特性,包括黑豆(BKPI)。斑点菜豆(SKPI),熊猫豆(PDPI),牛仔(CPPI),绿豆(MPI),小豆(API),米豆(RPI),黑大豆(BPI),大豆(SPI),鹰嘴豆(CPI),蚕豆(BRPI)和豌豆(PPI)。SDS-PAGE显示7S球蛋白是BKPI中的突出蛋白,SKPI,PDPI,CPPI,MPI,API和RPI,CPI的主要蛋白质部分是11S球蛋白,和BPI,SPI,BRPI和PPI包含7S和11S球蛋白作为主要成分。基于凝胶的幂律常数(K')和硬度,十二种豆类蛋白质分为三类高,中等和低凝胶强度。BKPI,SKPI和PDPI(菜豆蛋白是主要蛋白质级分)显示出高的凝胶强度,而与pH无关。静电相互作用,疏水作用和氢键是豆科植物蛋白质凝胶网络形成过程中最重要的分子间力,其中在pH3.0和pH7.0时的凝胶强度受到静电相互作用和氢键的显着影响,分别。此外,凝胶强度也受到非网络蛋白的显著负面影响。SEM观察表明,pH7.0时凝胶的微观结构比pH3.0时更致密,更均匀,从而导致更好的持水性。这些发现对于理解豆类蛋白质凝胶的差异非常重要,并为扩大豆类蛋白质在凝胶食品中的应用奠定了科学支持。
This
study aimed to investigate the rheological and textural properties of heat-induced gels from twelve legume protein isolates at pH 3.0 and 7.0, including black kidney bean (BKPI), speckled kidney bean (SKPI), panda bean (PDPI), cowpea (CPPI), mung bean (MPI), adzuki bean (API), rice bean (RPI), black soybean (BPI), soybean (SPI), chickpea (CPI), broad bean (BRPI) and pea (PPI). SDS-PAGE revealed that 7S globulin was prominent protein in BKPI, SKPI, PDPI, CPPI, MPI, API and RPI, the main protein fraction of CPI was 11S globulin, and BPI, SPI, BRPI and PPI contained both 7S and 11S globulins as major components. Based on the gel\'s Power Law constant (K\') and hardness, twelve legume proteins were divided into three categories with high, medium and low gel strength. BKPI, SKPI and PDPI with Phaseolin being the major protein fraction showed high gel strength regardless of pH. Electrostatic interactions, hydrophobic interactions and hydrogen bonds were the most important intermolecular forces in the formation of legume protein gel networks, of which gel strength at pH 3.0 and pH 7.0 was significantly affected by electrostatic interactions and hydrogen bonds, respectively. Moreover, gel strength was also remarkably negatively influenced by the non-network proteins. SEM observation indicated that the microstructure of gels at pH 7.0 was denser and more homogeneous than that at pH 3.0, leading to better water holding capacity. These findings would be of great importance for understanding the differences in legume protein gels, and also laid the scientific support for expanding applications of legume proteins in gel-based foods.