Non-Catalytic Domains of Glycoside Hydrolase Family 5 from Paenibacillus curdlanolyticus are Important for Promoting Multifunctional Enzyme Activities and Degradation of Agricultural Residues

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Author list: Fatmawati N.V.; Singkhala A.; Ketbot P.; Baramee S.; Waeonukul R.; Tachaapaikoon C.; Uke A.; Kosugi A.; Ratanakhanokchai K.; Pason P.

Publisher: The Korean Society for Applied Microbiology

Publication year: 2025

Journal: Journal of Microbiology and Biotechnology (1017-7825)

Volume number: 35

ISSN: 1017-7825

URL: https://www.scopus.com/inward/record.uri?eid=2-s2.0-105005475383&doi=10.4014%2fjmb.2501.01046&partnerID=40&md5=5bca45f54de4ce245058295325ac3b26

Languages: English-Great Britain (EN-GB)

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Abstract

PcGH5 from Paenibacillus curdlanolyticus strain B-6 is a modular protein consisting of a catalytic domain of glycoside hydrolase family 5 (GH5), and three non-catalytic domains (a family 11 carbohydrate-binding module (CBM11), a fibronectin type 3 (Fn3), and a family 3 carbohydrate-binding module (CBM3). In this study, the recombinants full-length PcGH5 and the catalytic domain (PcGH5_CD) were expressed in Escherichia coli and purified. Most GH5 members exhibit endo-cellulase activity. However, the catalytic domain enzyme of strain B-6 exhibited unique properties, showing multifunctional enzyme activities of endo-cellulase, endo-xylanase, endo-mannanase, and endo-1,3-1,4-β-glucanase. The sequence alignment of PcGH5_CD compared to other characterized GH5 enzymes suggests that the two catalytic residues and the six substrate-binding subsites of endo-cellulases were conserved with other different GH5 enzyme properties. Whereas a few conserved amino acid residues and/or short peptides located outside the active site of the GH5 endo-cellulases may be involved in broad substrate specificity of PcGH5_CD enzyme on xylan, mannan and 1,3-1,4-β-glucan. Moreover, the non-catalytic domains (CBM11-Fn3-CBM3) linked to the GH5 catalytic domain are important for promoting the multifunctional enzyme activities of PcGH5 on the β-1,4 glycosidic linkages of crystalline cellulose, highly branched polysaccharides, and β-1,4-1,6 and β-1,3-1,4 glycosidic linkages of polysaccharides, especially for the polysaccharides complex contained in agricultural residues. The full-length PcGH5 is effective in producing oligosaccharides from agricultural residues without pretreatment. Therefore, it is interesting to use it as a source of prebiotics producer for use in various food products. Copyright © 2025 by the authors.

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