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    Soluble Aggregates of Myofibrillar Proteins Engineered by Gallic Acid: Colloidal Structure and Resistance to In Vitro Gastric Digestion

    Year: 2022

    Journal: J. Agric. Food Chem., Volume 70, APR 6, page 4066–4075

    Authors: Chen, Xing; Chen, Kaiwen; Cheng, Hao; Liang, Li

    Organizations: Natural Science Foundation of Jiangsu Province, China [BK20190589]; National Natural Science Foundation of China [31901611]; Fundamental Research Funds for the Central Universities, China [JUSRP11970]; Youth Talent Support Project of Jiangsu Association for Science and Technology

    Keywords: myofibrillar protein; soluble aggregate; structure; in vitro digestion; colloidal engineering

    Myofibrillar protein (MP)-soluble aggregates can be made by tactics of gallic acid (GA) modification during pHshifting, and this work aimed to disclose their aggregation pattern andin vitrodigestion behavior. GA modification dissociated thefilamentous structure of myofibrils and caused structural reassembly to form small-sized aggregates. These aggregates were evidencedto contain GA-bridged dimers and oligomers of myosin or actin, having a molecular weight of similar to 1225 kDa. Additionally, thestructural rearrangement significantly decreased the surface hydrophobicity while substantially increased the surface charge. As aresult, the obtained colloidal solution was translucent and heat-resistant. Intriguingly, MP-soluble aggregates exhibited a retardeddigestive behavior. Further evaluation by a quartz crystal microbalance suggested that the reduced binding affinity of solubleaggregates toward gastric pepsin could be the underlying reason. This work may foster the engineering advances of modulating theMP structure-digestion for the tailor manufacturing of muscle protein-based beverages.
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