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Catalytic effect of transglutaminase mediated by myofibrillar protein crosslinking under microwave irradiation

Cao, Hongwei, Jiao, Xidong, Fan, Daming, Huang, Jianlian, Zhao, Jianxin, Yan, Bowen, Zhou, Wenguo, Zhang, Wenhai, Ye, Weijian, Zhang, Hao
Food chemistry 2019 v.284 pp. 45-52
catalytic activity, circular dichroism spectroscopy, crosslinking, disulfide bonds, enzyme activity, gels, heat, microwave radiation, molecular weight, myofibrillar proteins, myosin, polyacrylamide gel electrophoresis, protein-glutamine gamma-glutamyltransferase, solubility
Microwave (MW) heating improved the activity of transglutaminase (TGase) by inducing conformational changes due to structural modification. However, when TGase and myofibrillar protein were heated, the solubility and degree of crosslinking were similar. Further, the gel properties of the mixed solution pre-gelled by MW heating were lower than that obtained with water bath (WB) pre-gelling. We compared the effects on myofibrillar proteins at the same heating rate, our results showed that MW promoted aggregation, as the particle distribution tended toward larger molecular size. The increase of random coil as investigated by circular dichroism (CD) indicated that WB induced the unfolding of myofibrillar protein. MW enhanced intermolecular forces by engendering more disulfide bonds, which hindered the catalysis by TGase. Finally, SDS-PAGE indicated that the myosin molecules had more head crosslinking during MW treatment. MW and WB cause different response behaviors of myofibrillar protein, thereby affecting the catalytic effect of TGase.