微波辐射介导肌球蛋白交联的转谷氨酰胺酶的催化作用。
Catalytic effect of transglutaminase mediated by myofibrillar protein crosslinking under microwave irradiation.
机构信息
Key Laboratory of Refrigeration and Conditioning Aquatic Products Processing, Ministry of Agriculture and Rural Affairs, Xiamen 361022, China; State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, China; National Engineering Research Center for Functional Food, Jiangnan University, Wuxi 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi 214122, China.
State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, China; National Engineering Research Center for Functional Food, Jiangnan University, Wuxi 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi 214122, China.
出版信息
Food Chem. 2019 Jun 30;284:45-52. doi: 10.1016/j.foodchem.2019.01.097. Epub 2019 Jan 22.
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.
微波（MW）加热通过诱导结构修饰引起的构象变化来提高转谷氨酰胺酶（TGase）的活性。然而，当 TGase 和肌原纤维蛋白被加热时，溶解度和交联度相似。此外，通过 MW 加热预凝胶化的混合溶液的凝胶特性低于水浴（WB）预凝胶化的凝胶特性。我们比较了在相同加热速率下对肌原纤维蛋白的影响，结果表明 MW 促进了聚集，因为颗粒分布趋向于更大的分子尺寸。圆二色性（CD）研究表明随机卷曲的增加表明 WB 诱导了肌原纤维蛋白的展开。MW 通过生成更多的二硫键来增强分子间力，从而阻碍 TGase 的催化。最后，SDS-PAGE 表明，在 MW 处理过程中肌球蛋白分子的头部交联更多。MW 和 WB 导致肌原纤维蛋白的不同反应行为，从而影响 TGase 的催化效果。
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