Department of Food Science and Technology, Shanghai Jiao Tong University, 800 Dongchuan Road, Shanghai 200240, China.
State Key Laboratory of Dairy Biotechnology, Shanghai Engineering Research Center of Dairy Biotechnology, Dairy Research Institute, Bright Dairy & Food Co., Ltd., Shanghai 200436, China.
Food Chem. 2022 Jul 30;383:132366. doi: 10.1016/j.foodchem.2022.132366. Epub 2022 Feb 7.
In present study, microbial transglutaminase (MTGase) was applied to strengthen the interaction between casein and hempseed protein (HPI) through crosslinking. The structural and functional characteristics of this heteropolymers were investigated. Both homologous and heterologous crosslinking were achieved by adding MTGase in casein-HPI system, and thus enhanced zeta potential, surface hydrophobicity, viscosity, emulsifying and gelation properties of the complex. However, HPI hindered the crosslinking due to unbalanced Lys/Gln ratios. Emulsifying and gelling properties were significantly correlated with the secondary structures. When MTGase activity was < 30 U/g or treatment time was < 2 h, the α-helix content decreased by 9% while the β-sheet content increased by 12%, respectively, with MTGase activity and treatment time increase. The structural alterations resulted in the better emulsifying activity, gel networks and water holding capacity of the complex. This work represents a novel interaction mode between casein and HPI via MTGase to elevate functional properties of complex.
在本研究中，微生物谷氨酰胺转氨酶（MTGase）通过交联作用应用于增强酪蛋白和麻蛋白（HPI）之间的相互作用。研究了这种杂聚物的结构和功能特性。通过在酪蛋白-HPI 体系中添加 MTGase，可以实现同源和异源交联，从而提高了复合物的 Zeta 电位、表面疏水性、粘度、乳化和胶凝性能。然而，由于 Lys/Gln 比例不平衡，HPI 阻碍了交联。乳化和胶凝性能与二级结构显著相关。当 MTGase 活性<30 U/g 或处理时间<2 h 时，随着 MTGase 活性和处理时间的增加，α-螺旋含量分别下降了 9%，β-折叠含量增加了 12%。结构的改变导致复合物具有更好的乳化活性、凝胶网络和持水能力。这项工作代表了一种通过 MTGase 增强复合物功能特性的酪蛋白和 HPI 之间的新型相互作用模式。
