Document Detail


The Discoidin Domain of Bacillus circulans β-Galactosidase Plays an Essential Role in Repressing Galactooligosaccharide Production.
MedLine Citation:
PMID:  23291776     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
The recently cloned β-galactosidase from Bacillus circulans ATCC 31382, designated BgaD, contains a multiple domain architecture including a F5/8 type C domain or a discoidin (DS) domain in the C-terminal peptide region. Here we report that the DS domain plays an essential role in repressing the production of galactooligosaccharides (GOSs). We prepared deletion mutants and point-mutated forms of rBgaD-A (deletion of the BgaD signal peptide) to compare their reaction behaviors. The yields of GOS for all of the point-mutated forms as well as the deletion mutants of rBgaD-As increased as compared to rBgaD-A. In particular, W1540A mutant BgaD-A (rBgaD-A_W1540A) produced much more GOSs than rBgaD-A. Surface plasmon resonance experiments indicated that both the wild-type and the W1540A mutant DS domain showed high affinity for galactosyllactose. rBgaD-A, which has a wild-type DS domain, showed high hydrolytic activity toward galactosyllactose, while the hydrolytic activities of rBgaD-D, without a DS domain, and rBgaD-A_W1540A, with a mutant DS domain were extremely low. The findings obtained in this study indicate that the wild-type DS domain of rBgaD-A has a function that aids galactosyllactose molecules to be properly oriented within the active site, so that they can be hydrolyzed efficiently to produce galactose/glucose by inhibiting the accumulation of GOS.
Authors:
Jingyuan Song; Hiroyuki Imanaka; Koreyoshi Imamura; Masashi Minoda; Shotaro Yamaguchi; Kazuhiro Nakanishi
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-07
Journal Detail:
Title:  Bioscience, biotechnology, and biochemistry     Volume:  -     ISSN:  1347-6947     ISO Abbreviation:  Biosci. Biotechnol. Biochem.     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-1-7     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9205717     Medline TA:  Biosci Biotechnol Biochem     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
Graduate School of Natural Science and Technology, Okayama University.
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