Degradation of rice bran hemicellulose by Paenibacillus sp. strain HC1: Gene cloning, characterization and function of β-D-glucosidase as an enzyme involved in degradation
Archives of Microbiology, ISSN: 0302-8933, Vol: 184, Issue: 4, Page: 215-224
2005
- 19Citations
- 25Captures
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Metrics Details
- Citations19
- Citation Indexes19
- CrossRef19
- 19
- Captures25
- Readers25
- 25
Article Description
A bacterium (strain HC1) capable of assimilating rice bran hemicellulose was isolated from a soil and identified as belonging to the genus Paenibacillus through taxonomical and 16S rDNA sequence analysis. Strain HC1 cells grown on rice bran hemicellulose as a sole carbon source inducibly produced extracellular xylanase and intracellular glycosidases such as β-D-glucosidase and β-D-arabinosidase. One of them, β-D-glucosidase was further analyzed. A genomic DNA library of the bacterium was constructed in Escherichia coli and gene coding for β-D-glucosidase was cloned by screening for β-D-glucoside-degrading phenotype in E. coli cells. Nucleotide sequence determination indicated that the gene for the enzyme contained an open reading frame consisting of 1,347 bp coding for a polypeptide with a molecular mass of 51.4 kDa. The polypeptide exhibits significant homology with other bacterial β-D-glucosidases and belongs to glycoside hydrolase family 1. β-D-Glucosidase purified from E. coli cells was a monomeric enzyme with a molecular mass of 50 kDa most active at around pH 7.0 and 37°C. Strain HC1 glycosidases responsible for degradation of rice bran hemicellulose are expected to be useful for structurally determining and molecularly modifying rice bran hemicellulose and its derivatives. © Springer-Verlag 2005.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=27744473179&origin=inward; http://dx.doi.org/10.1007/s00203-005-0038-8; http://www.ncbi.nlm.nih.gov/pubmed/16205911; http://link.springer.com/10.1007/s00203-005-0038-8; http://www.springerlink.com/index/10.1007/s00203-005-0038-8; http://www.springerlink.com/index/pdf/10.1007/s00203-005-0038-8; https://dx.doi.org/10.1007/s00203-005-0038-8; https://link.springer.com/article/10.1007/s00203-005-0038-8
Springer Science and Business Media LLC
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