Insight into the solubilization mechanism of wheat gluten by protease modification from conformational change and molecular interaction perspective.

Autor: Li W; Key Laboratory of Jianghuai Agricultural Product Fine Processing and Resource Utilization of Ministry of Agriculture and Rural Affairs, State Key Laboratory of Tea Plant Biology and Utilization, School of Tea and Food Science & Technology, Anhui Agricultural University, Hefei 230036, China., Zhou Q; Key Laboratory of Jianghuai Agricultural Product Fine Processing and Resource Utilization of Ministry of Agriculture and Rural Affairs, State Key Laboratory of Tea Plant Biology and Utilization, School of Tea and Food Science & Technology, Anhui Agricultural University, Hefei 230036, China., Xu J; Key Laboratory of Jianghuai Agricultural Product Fine Processing and Resource Utilization of Ministry of Agriculture and Rural Affairs, State Key Laboratory of Tea Plant Biology and Utilization, School of Tea and Food Science & Technology, Anhui Agricultural University, Hefei 230036, China., Zhu S; Key Laboratory of Jianghuai Agricultural Product Fine Processing and Resource Utilization of Ministry of Agriculture and Rural Affairs, State Key Laboratory of Tea Plant Biology and Utilization, School of Tea and Food Science & Technology, Anhui Agricultural University, Hefei 230036, China., Lv S; Key Laboratory of Jianghuai Agricultural Product Fine Processing and Resource Utilization of Ministry of Agriculture and Rural Affairs, State Key Laboratory of Tea Plant Biology and Utilization, School of Tea and Food Science & Technology, Anhui Agricultural University, Hefei 230036, China., Yu Z; Key Laboratory of Jianghuai Agricultural Product Fine Processing and Resource Utilization of Ministry of Agriculture and Rural Affairs, State Key Laboratory of Tea Plant Biology and Utilization, School of Tea and Food Science & Technology, Anhui Agricultural University, Hefei 230036, China., Yang Y; Anhui Bi Lv Chun Biotechnology Co., Ltd., Chuzhou 239200, China., Liu Y; Key Laboratory of Jianghuai Agricultural Product Fine Processing and Resource Utilization of Ministry of Agriculture and Rural Affairs, State Key Laboratory of Tea Plant Biology and Utilization, School of Tea and Food Science & Technology, Anhui Agricultural University, Hefei 230036, China., Zhou Y; Key Laboratory of Jianghuai Agricultural Product Fine Processing and Resource Utilization of Ministry of Agriculture and Rural Affairs, State Key Laboratory of Tea Plant Biology and Utilization, School of Tea and Food Science & Technology, Anhui Agricultural University, Hefei 230036, China., Sui X; College of Food Science, Northeast Agricultural University, Harbin 150030, China. Electronic address: xiaonan.sui@neau.edu.cn., Zhang Q; Key Laboratory of Jianghuai Agricultural Product Fine Processing and Resource Utilization of Ministry of Agriculture and Rural Affairs, State Key Laboratory of Tea Plant Biology and Utilization, School of Tea and Food Science & Technology, Anhui Agricultural University, Hefei 230036, China. Electronic address: 850326065@qq.com., Xiao Y; Key Laboratory of Jianghuai Agricultural Product Fine Processing and Resource Utilization of Ministry of Agriculture and Rural Affairs, State Key Laboratory of Tea Plant Biology and Utilization, School of Tea and Food Science & Technology, Anhui Agricultural University, Hefei 230036, China. Electronic address: xiaoyaqing92@163.com.
Jazyk: angličtina
Zdroj: Food chemistry [Food Chem] 2024 Jul 30; Vol. 447, pp. 138992. Date of Electronic Publication: 2024 Mar 16.
DOI: 10.1016/j.foodchem.2024.138992
Abstrakt: The low solubility limits the utilization of other functional characteristics of wheat gluten (WG). This study effectively improved the solubility of WG through protease modification and explored the potential mechanism of protease modification to enhance the solubility of WG, further stimulating the potential application of WG in the food industry. Solubility of WG modified with alkaline protease, complex protease, and neutral protease was enhanced by 98.99%, 54.59%, and 51.68%, respectively. Notably, the content of β-sheet was reduced while the combined effect of hydrogen bond and ionic bond were increased after protease modification. Meanwhile, the reduced molecular size and viscoelasticity as well as the elevated surface hydrophobicity, thermostability, water absorption capacity, and crystallinity were observed in modified WG. Moreover, molecular docking indicated that protease was specifically bound to the amino acid residues of WG through hydrogen bonding, hydrophobic interaction, and salt bridge.
Competing Interests: Declaration of competing interest The authors declare no conflict of interest.
(Copyright © 2024 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
Externí odkaz: