Department of Food Science, University of Guelph, 50 Stone Road E, Guelph, Ontario N1G 2W1, Canada.
Food Chem. 2021 Feb 15;338:128010. doi: 10.1016/j.foodchem.2020.128010. Epub 2020 Sep 6.
Potential improvements to the physical properties of brittle, self-assembled zein networks through microbial transglutaminase crosslinking were investigated. The formation of crosslinked heteropolymers was also explored with networks containing zein and either soy or pea protein isolates as supplemented lysine sources. The observed SDS-PAGE bands did not show any evidence of zein crosslinking. Soy and pea isolates underwent extensive crosslinking on their own, but heteropolymers were not observed in multiprotein networks with zein. Despite the lack of crosslinking observed, rheological and textural analysis revealed that the enzymatic treatment of zein produced a weaker, more brittle structure. With no significant changes in secondary structure, determined through FTIR, the observed behaviour was primarily attributed to glutamine deamidation by microbial transglutaminase in the absence of sufficient lysine through changes to the hydrophobicity of the protein such that non-covalent bonding within network was modified.
通过微生物转谷氨酰胺酶交联来改善脆性自组装玉米醇溶蛋白网络的物理性质的研究。还探索了含有玉米醇溶蛋白和大豆或豌豆分离蛋白作为补充赖氨酸源的网络中形成的交联杂聚物。观察到的 SDS-PAGE 带没有显示出玉米醇溶蛋白交联的任何证据。大豆和豌豆分离蛋白本身经历了广泛的交联，但在含有玉米醇溶蛋白的多蛋白网络中没有观察到杂聚物。尽管没有观察到交联，但流变学和质构分析表明，玉米醇溶蛋白的酶处理产生了一个较弱、较脆的结构。通过傅里叶变换红外光谱（FTIR）确定二级结构没有显著变化，观察到的行为主要归因于微生物转谷氨酰胺酶在缺乏足够赖氨酸的情况下通过改变蛋白质的疏水性使谷氨酰胺脱酰胺，从而改变了网络内的非共价键合。
