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Please use this identifier to cite or link to this item: http://hdl.handle.net/10204/445

Title: Cloning and characterization of a carboxylesterase from Bacillus coagulans 81-11
Authors: Mnisi, SM
Louw, M
Theron, J
Keywords: Bacillus coagulans
Lipolytic activity
Issue Date: Apr-2005
Publisher: Springer Science and Business Media Inc
Citation: Mnisi, SM, Louw, M and Theron, J. 2005. Cloning and characterization of a carboxylesterase from Bacillus coagulans 81-11. Current Microbiology, vol. 50(4), pp 196-201
Abstract: A genomic library of Bacillus coagulans strain 81 -11 was screened in Escherichia coli JM83 for lipolytic activity by using tributyrin agar plates. A 2.4 kb DNA fragment was subcloned from a lipolytic-positive clone and completely sequenced. Nucleotide sequence analysis predicted a 723 bp open reading frame (ORF), designated estC1, encoding a protein of 240 amino acids with an estimated molecular mass of 27 528 Da and a pI of 9.15. The deduced amino acid sequence of the estC1 gene exhibited significant amino acid sequence identity with carboxylesterases from thermophilic Geobacillus spp. and sequence analysis showed that the protein contains the signature G-X-S-XG included in most esterases and lipases. Enzyme assays using p-nitrophenyl (p-NP) esters with different acyl chain lengths as the substrate confirmed the esterase activity. EstCl exhibited a marked preference for esters of short-chain fatty acids, yielding the highest activity with p-NP butyrate, Maximum activity was found at pH 8 and 50°C, although the enzyme displayed stability at temperatures up to 60°C.
Description: Copyright: 2004 Springer Science and Business Media Inc
URI: http://hdl.handle.net/10204/445
ISSN: 0343-8651
Appears in Collections:General science, engineering & technology

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