NDLI: A cel44C-man26A gene of endophytic Paenibacillus polymyxa GS01 has multi-glycosyl hydrolases in two catalytic domains

Content Provider	Springer Nature Link
Author	Cho, Kye Man Hong, Su Young Lee, Sun Mi Kim, Yong Hee Kahng, Goon Gjung Kim, Hoon Yun, Han Dae
Copyright Year	2006
Abstract	A bacterial strain Paenibacillus polymyxa GS01 was isolated from the interior of the roots of Korean cultivars of ginseng (Panax ginseng C. A. Meyer). The cel44C-man26A gene was cloned from this endophytic strain. This 4,056-bp gene encodes for a 1,352-aa protein which, based on BLAST search homologies, contains a glycosyl hydrolase family 44 (GH44) catalytic domain, a fibronectin domain type 3, a glycosyl hydrolase family 26 (GH26) catalytic domain, and a cellulose-binding module type 3. The multifunctional enzyme domain GH44 possesses cellulase, xylanase, and lichenase activities, while the enzyme domain GH26 possesses mannanase activity. The Cel44C enzyme expressed in and purified from Escherichia coli has an optimum pH of 7.0 for cellulase and lichenase activities, but is at an optimum pH of 5.0 for xylanase and mannanase activities. The optimum temperature for enzymatic activity was 50°C for all substrates. No detectable enzymatic activity was detected for the Cel44C-Man26A mutants E91A and E222A. These results suggest that the amino acid residues Glu91 and Glu222 may play an important role in the glycosyl hydrolases activity of Cel44C-Man26A.
Starting Page	618
Ending Page	630
Page Count	13
File Format	PDF
ISSN	01757598
Journal	Applied Microbiology and Biotechnology
Volume Number	73
Issue Number	3
e-ISSN	14320614
Language	English
Publisher	Springer-Verlag
Publisher Date	2006-08-16
Publisher Place	Berlin, Heidelberg
Access Restriction	Subscribed
Subject Keyword	Paenibacillus polymyxa GS01 Glycosyl hydrolases Rhizobacterium Microbial Genetics and Genomics Microbiology Biotechnology
Content Type	Text
Resource Type	Article
Subject	Medicine Applied Microbiology and Biotechnology Biotechnology

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