CLONING, EXPRESSION OF GENE AND CHARACTERIZATION OF RECOMBINANT MANNANASE FROM Paenibacillus curdlanolyticus B-6
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Title CLONING, EXPRESSION OF GENE AND CHARACTERIZATION OF RECOMBINANT MANNANASE FROM Paenibacillus curdlanolyticus B-6
Creator MISTER AKE-KAVITCH SIRIATCHARANON
Publisher School of Bioresources, KMUTT, Bangkok, Thailand, 10150
Publication Year 2560
Keyword Endo-mannanase / Glycoside hydrolase family 26 (GH26) / beta-mannosidase/ Multi-functional activity / Paenibacillus curdlanolyticus
Description A novel -mannanase gene (PcMan26A) of Paenibacilluscurdlanolyticus B-6 was cloned and expressed in E. coli BL21 (DE3). It consisted of 1,383 base pairs that encoded a single catalytic domain with 461 amino acids and absented a signal peptide (GenBank accession no. KU052529). The recombinant PcMan26A molecular weight was 56.4 kiloDalton. It had a similarity with -endo-Mannanase from Rhodothermusmarinus DSM4252 (P49425), Cellvibriojaponicus Ueda107 (P49424), and Bacillus subtillis NM-39 (P55278) at 33, 32 and 30%, respectively, when compared with NCBI databases. The recombinant PcMan26A showed the highest activity toward mannan, xylan, cellulose, chitin, and -1,3-1,4-glucan, with 2.71, 1.38, 1.20, 1.07, and 0.71 unit per mg protein, respectively. However, it demonstrated no activity on the starch. The results indicated that the recombinant PcMan26A was poly-specificity to -1,4-linkage substances. Interestingly, the recombinant enzyme can efficiently convert -mannan to series of manno-oligosaccharide and to mannose. In addition, the mannobiose (M2) was cleaved to mannose (M1) by the recombinant PcMan26A. The results clearly indicated that PcMan26A had a bifunctional property of endo-mannanase and -mannosidase. This is the first report of the multi-functional activities from one catalytic domain in GH family 26, especially mannanolytic enzymes.
Format PICTURE
URL Website https://explore.nrct.go.th/search_detail/result/3427
Date and time 2560
Website title ห้องสมุดงานวิจัยสำหรับสาธารณะ (Extraordinary SimplPublic Library of Research Result : EXPLORE)
National Research Council of Thailand

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