State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China.
School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China.
J Agric Food Chem. 2022 Apr 6;70(13):4066-4075. doi: 10.1021/acs.jafc.1c05840. Epub 2022 Mar 14.
Myofibrillar protein (MP)-soluble aggregates can be made by tactics of gallic acid (GA) modification during pH shifting, and this work aimed to disclose their aggregation pattern and digestion behavior. GA modification dissociated the filamentous structure of myofibrils and caused structural reassembly to form small-sized aggregates. These aggregates were evidenced to contain GA-bridged dimers and oligomers of myosin or actin, having a molecular weight of ∼1225 kDa. Additionally, the structural rearrangement significantly decreased the surface hydrophobicity while substantially increased the surface charge. As a result, the obtained colloidal solution was translucent and heat-resistant. Intriguingly, MP-soluble aggregates exhibited a retarded digestive behavior. Further evaluation by a quartz crystal microbalance suggested that the reduced binding affinity of soluble aggregates toward gastric pepsin could be the underlying reason. This work may foster the engineering advances of modulating the MP structure-digestion for the tailor manufacturing of muscle protein-based beverages.
肌原纤维蛋白（MP）可溶性聚集体可以通过在 pH 转换过程中使用没食子酸（GA）修饰的策略来制备，本工作旨在揭示其聚集模式和消化行为。GA 修饰使肌原纤维的丝状结构解离，并导致结构重新组装形成小尺寸的聚集体。这些聚集体被证明含有通过 GA 桥接的肌球蛋白或肌动蛋白的二聚体和低聚物，分子量约为 1225 kDa。此外，结构重排显著降低了表面疏水性，同时大大增加了表面电荷。结果，得到的胶体溶液是半透明和耐热的。有趣的是，MP 可溶性聚集体表现出延迟的消化行为。通过石英晶体微天平进一步评估表明，可溶性聚集体对胃蛋白酶的结合亲和力降低可能是其原因。这项工作可能会促进调节 MP 结构-消化的工程进展，以便于定制肌肉蛋白基饮料的制造。
