Journal
FOOD CHEMISTRY
Volume 284, Issue -, Pages 45-52Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2019.01.097
Keywords
Microwave; Myofibrillar protein; Tranglutaminase; Crosslinking; Gel property; Secondary structure
Funding
- National Natural Science Foundation of China [31822038]
- National Thirteenth Five-Year Plan for Science Technology [2018YFD0400600]
- Open Project Program of Key Laboratory of Refrigeration and Conditioning Aquatic Products Processing, Ministry of Agriculture and Rural Affairs [KLRCAPP2018-01]
- National First-class Discipline Program of Food Science and Technology [JUFSTR20180102]
- program of Collaborative innovation center of food safety and quality control in Jiangsu Province
- six talent peak high-level talent project of Jiangsu Province [2015-NY-008]
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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.
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