Distinctive activation of β-galactosidase by carboxymethylated β-glucan in vitro and mechanism study: Critical role of hydrophobic and electrostatic interactions.

Autor: Wang J; National '111' Center for Cellular Regulation and Molecular Pharmaceutics, Key Laboratory of Fermentation Engineering (Ministry of Education), Hubei University of Technology, Wuhan 430068, China; College of Bioengineering and Food, Hubei University of Technology, Wuhan 430068, China., Wu W; National '111' Center for Cellular Regulation and Molecular Pharmaceutics, Key Laboratory of Fermentation Engineering (Ministry of Education), Hubei University of Technology, Wuhan 430068, China; College of Bioengineering and Food, Hubei University of Technology, Wuhan 430068, China., Yang J; National '111' Center for Cellular Regulation and Molecular Pharmaceutics, Key Laboratory of Fermentation Engineering (Ministry of Education), Hubei University of Technology, Wuhan 430068, China; College of Bioengineering and Food, Hubei University of Technology, Wuhan 430068, China., Zhang X; National '111' Center for Cellular Regulation and Molecular Pharmaceutics, Key Laboratory of Fermentation Engineering (Ministry of Education), Hubei University of Technology, Wuhan 430068, China; College of Bioengineering and Food, Hubei University of Technology, Wuhan 430068, China., Wu Q; National '111' Center for Cellular Regulation and Molecular Pharmaceutics, Key Laboratory of Fermentation Engineering (Ministry of Education), Hubei University of Technology, Wuhan 430068, China; College of Bioengineering and Food, Hubei University of Technology, Wuhan 430068, China., Wang C; National '111' Center for Cellular Regulation and Molecular Pharmaceutics, Key Laboratory of Fermentation Engineering (Ministry of Education), Hubei University of Technology, Wuhan 430068, China; College of Bioengineering and Food, Hubei University of Technology, Wuhan 430068, China. Electronic address: Chaowhbut@foxmail.com.
Jazyk: angličtina
Zdroj: Food chemistry [Food Chem] 2024 Aug 01; Vol. 448, pp. 139082. Date of Electronic Publication: 2024 Mar 23.
DOI: 10.1016/j.foodchem.2024.139082
Abstrakt: β-galactosidase (lactase) is commercially important as a dietary supplement to alleviate the symptoms of lactose intolerance. This work investigated a unique activation of CMP (carboxymethylated (1 → 3)-β-d-glucan) on lactase and its mechanism by comparing it with carboxymethyl chitosan (CMCS), an inhibitor of lactase. The results illustrated that the secondary and tertiary structures of lactase were altered and its active sites exposed after complexation with CMP, and dissociation of lactase aggregates was also observed. These changes favored better accessibility of the substrate to the active sites of lactase, resulting in a maximum increase of 60.5 % in lactase activity. Furthermore, the hydrophobic and electrostatic interactions with lactase caused by the carboxymethyl group of CMP were shown to be crucial for its activation ability. Thus, the improvement of lactase activity and stability by CMP shown here is important for the development of new products in the food and pharmaceutical industries.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2024 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
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