Catalytic effect of transglutaminase mediated by myofibrillar protein crosslinking under microwave irradiation. (30th June 2019)

• Record Type: Journal Article
• Authors: Cao, Hongwei; Jiao, Xidong; Fan, Daming; Huang, Jianlian; Zhao, Jianxin; Yan, Bowen; Zhou, Wenguo; Zhang, Wenhai; Ye, Weijian; Zhang, Hao
• Is Part Of: Food chemistry. Volume 284(2019)
• Page Start: 45
• Page End: 52
• Publication Date: 2019-06-30
• Subjects: Microwave -- Myofibrillar protein -- Tranglutaminase -- Crosslinking -- Gel property -- Secondary structure; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2019.01.097
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: MW promoted aggregation as the particle tended toward larger molecular size. Gel properties of the mixed solution pre-gelled by MW were lower than WB heating. Circular dichroism indicated that WB induced the unfolding of myofibrillar proteins. MW enhanced intermolecular forces by engendering more disulfide bonds. Different behaviors of myofibrillar proteins affecting catalytic effect of TGase. Abstract: 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.