Research Article
Cloning and characterization of a dextranase gene from Lipomyces starkeyi and its expression in Saccharomyces cerevisiae
Article first published online: 9 NOV 2005
DOI: 10.1002/yea.1311
Copyright © 2005 John Wiley & Sons, Ltd.
Additional Information
How to Cite
Kang, H.-K., Kim, S. H., Park, J.-Y., Jin, X.-J., Oh, D.-K., Soo Kang, S. and Kim, D. (2005), Cloning and characterization of a dextranase gene from Lipomyces starkeyi and its expression in Saccharomyces cerevisiae. Yeast, 22: 1239–1248. doi: 10.1002/yea.1311
Publication History
- Issue published online: 9 NOV 2005
- Article first published online: 9 NOV 2005
- Manuscript Accepted: 12 SEP 2005
- Manuscript Received: 29 MAR 2005
Funded by
- Ministry of Science and Technology, South Korea. Grant Number: MG05-0301-1-0
- Abstract
- Article
- References
- Cited By
Keywords:
- dextranase;
- Lipomyces starkeyi;
- Saccharomyces cerevisiae;
- expression
Abstract
A dextranase-encoding cDNA from L. starkeyi KSM22 was isolated and characterized. The 2052 bp cDNA fragment (lsd1) harbouring the dextranase gene exhibited one open reading frame (ORF) composed of 1824 bp flanked by a 41 bp 5′-UTR and a 184 bp 3′-UTR, including a 27 bp poly(A) tail. The lsd1 gene contains no introns. The open reading frame encodes a 608 amino acid polypeptide (LSD1) with a 67.6 kDa predicted molecular mass. There was a 77% deduced amino acid sequence identity between the LSD1 dextranase and the dextranase from Penicillium minioluteum. The primary structure of LSD1 dextranase exhibits distant similarity with the enzymes of the glycosyl hydrolase family 49 that comprises Penicillium dextranase. The optimum pH of LSD1 was 6.0 and the optimum temperature was 37 °C. LSD1 dextranase activity was substantially abolished by exposure to 1 mM Hg2+, Ag3+ and Mn2+. LSD1 exhibited high hydrolysing activity towards dextran (100%), soluble starch (22%) and mutan (8%). Copyright © 2005 John Wiley & Sons, Ltd.

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