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Intervention of transglutaminase in surimi gel under microwave irradiation.
Food Chem. 2018 Dec 01; 268:378-385.FC

Abstract

Transglutaminase (TGase) was selected as model enzyme to investigate the effects of microwave (MW) heating on its activity and structure compared to water bath (WB) heating. MW heating can enhance the activity of TGase and reach the maximum at 20 min, whereas conduction heating has little effect on the activity of TGase. The difference of dielectric properties between MW heating and WB heating were not obvious, but MW heating had higher conductivity than WB heating. The results of ultraviolet and fluorescence spectra show that MW heating can change the enzyme activity by changing the conformation of TGase. The decrease of α-helix and an increase of β-sheet and β-turn investigated by circular dichroism (CD) indicated the secondary structures of TGase were changed when treated by MW heating. Further gel properties test confirmed that TGase treated by MW could improve the functional and mechanical properties of surimi gel.

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Authors+Show Affiliations

Cao H
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.
Fan D
State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, China; Key Laboratory of Refrigeration and Conditioning Aquatie Products Processing, Ministry of Agriculture and Rural Affairs, Xiamen 361022, China; National Engineering Research Center for Functional Food, Jiangnan University, Wuxi 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi 214122, China; Collaborative Innovation Center of Food Safety and Quality Control in Jiangsu Province, Wuxi 214122, China. Electronic address: fandm@jiangnan.edu.cn.
Jiao X
National Engineering Research Center for Functional Food, Jiangnan University, Wuxi 214122, China; School of Food Science and Technology, Jiangnan University, Wuxi 214122, China.
Huang J
Key Laboratory of Refrigeration and Conditioning Aquatie Products Processing, Ministry of Agriculture and Rural Affairs, Xiamen 361022, China.
Zhao J
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; Collaborative Innovation Center of Food Safety and Quality Control in Jiangsu Province, Wuxi 214122, China.
Yan B
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.
Zhou W
Key Laboratory of Refrigeration and Conditioning Aquatie Products Processing, Ministry of Agriculture and Rural Affairs, Xiamen 361022, China.
Zhang W
Key Laboratory of Refrigeration and Conditioning Aquatie Products Processing, Ministry of Agriculture and Rural Affairs, Xiamen 361022, China.
Ye W
Key Laboratory of Refrigeration and Conditioning Aquatie Products Processing, Ministry of Agriculture and Rural Affairs, Xiamen 361022, China.
Zhang H
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; Collaborative Innovation Center of Food Safety and Quality Control in Jiangsu Province, Wuxi 214122, China.
Chen W
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; Collaborative Innovation Center of Food Safety and Quality Control in Jiangsu Province, Wuxi 214122, China.

MeSH

Circular DichroismFish ProteinsGelsMicrowavesProtein Structure, SecondarySeafoodTransglutaminases

Pub Type(s)

Journal Article

Language

eng

PubMed ID

30064772

Citation

Cao, Hongwei, et al. "Intervention of Transglutaminase in Surimi Gel Under Microwave Irradiation." Food Chemistry, vol. 268, 2018, pp. 378-385.
Cao H, Fan D, Jiao X, et al. Intervention of transglutaminase in surimi gel under microwave irradiation. Food Chem. 2018;268:378-385.
Cao, H., Fan, D., Jiao, X., Huang, J., Zhao, J., Yan, B., Zhou, W., Zhang, W., Ye, W., Zhang, H., & Chen, W. (2018). Intervention of transglutaminase in surimi gel under microwave irradiation. Food Chemistry, 268, 378-385. https://doi.org/10.1016/j.foodchem.2018.06.067
Cao H, et al. Intervention of Transglutaminase in Surimi Gel Under Microwave Irradiation. Food Chem. 2018 Dec 1;268:378-385. PubMed PMID: 30064772.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Intervention of transglutaminase in surimi gel under microwave irradiation. AU - Cao,Hongwei, AU - Fan,Daming, AU - Jiao,Xidong, AU - Huang,Jianlian, AU - Zhao,Jianxin, AU - Yan,Bowen, AU - Zhou,Wenguo, AU - Zhang,Wenhai, AU - Ye,Weijian, AU - Zhang,Hao, AU - Chen,Wei, Y1 - 2018/06/15/ PY - 2018/03/15/received PY - 2018/05/19/revised PY - 2018/06/14/accepted PY - 2018/8/2/entrez PY - 2018/8/2/pubmed PY - 2019/4/17/medline KW - Conformation KW - Microwave KW - Secondary structure KW - Surimi gelation KW - TGase activity SP - 378 EP - 385 JF - Food chemistry JO - Food Chem VL - 268 N2 - Transglutaminase (TGase) was selected as model enzyme to investigate the effects of microwave (MW) heating on its activity and structure compared to water bath (WB) heating. MW heating can enhance the activity of TGase and reach the maximum at 20 min, whereas conduction heating has little effect on the activity of TGase. The difference of dielectric properties between MW heating and WB heating were not obvious, but MW heating had higher conductivity than WB heating. The results of ultraviolet and fluorescence spectra show that MW heating can change the enzyme activity by changing the conformation of TGase. The decrease of α-helix and an increase of β-sheet and β-turn investigated by circular dichroism (CD) indicated the secondary structures of TGase were changed when treated by MW heating. Further gel properties test confirmed that TGase treated by MW could improve the functional and mechanical properties of surimi gel. SN - 1873-7072 UR - https://www.unboundmedicine.com/medline/citation/30064772/Intervention_of_transglutaminase_in_surimi_gel_under_microwave_irradiation_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0308-8146(18)31040-9 DB - PRIME DP - Unbound Medicine ER -