Identification and characterization of a chondroitinase ABC with a novel carbohydrate-binding module.

Autor: Liu G; College of Food Science and Engineering, Ocean University of China, 1299 Sansha Road, Qingdao 266404, China., Song L; College of Food Science and Engineering, Ocean University of China, 1299 Sansha Road, Qingdao 266404, China., Li J; College of Food Science and Engineering, Ocean University of China, 1299 Sansha Road, Qingdao 266404, China., Song X; College of Food Science and Engineering, Ocean University of China, 1299 Sansha Road, Qingdao 266404, China., Mei X; College of Food Science and Engineering, Ocean University of China, 1299 Sansha Road, Qingdao 266404, China., Zhang Y; College of Food Science and Engineering, Ocean University of China, 1299 Sansha Road, Qingdao 266404, China., Fan C; College of Food Science and Engineering, Ocean University of China, 1299 Sansha Road, Qingdao 266404, China., Chang Y; College of Food Science and Engineering, Ocean University of China, 1299 Sansha Road, Qingdao 266404, China. Electronic address: changyg@ouc.edu.cn., Xue C; College of Food Science and Engineering, Ocean University of China, 1299 Sansha Road, Qingdao 266404, China.
Jazyk: angličtina
Zdroj: International journal of biological macromolecules [Int J Biol Macromol] 2024 Jun; Vol. 271 (Pt 1), pp. 132518. Date of Electronic Publication: 2024 May 20.
DOI: 10.1016/j.ijbiomac.2024.132518
Abstrakt: Chondroitinases play important roles in structural and functional studies of chondroitin sulfates. Carbohydrate-binding module (CBM) is generally considered as an accessory module in carbohydrate-active enzymes, which promotes the association of the appended enzyme with the substrate and potentiates the catalytic activity. However, the role of natural CBM in chondroitinases has not been investigated. Herein, a novel chondroitinase ChABC29So containing an unknown domain with a predicted β-sandwich fold was discovered from Segatella oris. Recombinant ChABC29So showed enzyme activity towards chondroitin sulfates and hyaluronic acid and acted in a random endo-acting manner. The unknown domain exhibited a chondroitin sulfate-binding capacity and was identified as a CBM. Biochemical characterization of ChABC29So and the CBM-truncated enzyme revealed that the CBM enhances the catalytic activity, thermostability, and disaccharide proportion in the final enzymatic products of ChABC29So. These findings demonstrate the role of the natural CBM in a chondroitinase and will guide future modification of chondroitinases.
Competing Interests: Declaration of competing interest The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.
(Copyright © 2024 Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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