Gene cloning and characterization of thermostable lipase from Bacillus stearothermophilus L1

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Title
Gene cloning and characterization of thermostable lipase from Bacillus stearothermophilus L1
Author(s)
Hyung Kwoun Kim; Sun Yang Park; Jung Kee Lee; Tae Kwang Oh
Bibliographic Citation
Bioscience Biotechnology and Biochemistry, vol. 62, no. 1, pp. 66-71
Publication Year
1998
Abstract
The gene coding for an extracellular lipase of Bacillus stearothermophilus L1 was cloned in Escherichia coli. Sequence analysis showed an open reading frame of 1254 bp, which encodes a polypeptide of 417 amino acid residues. The polypeptide was composed of a signal sequence (29 amino acids) and a mature protein of 388 amino acids. An alanine replaces the first glycine in the conserved pentapeptide (Gly-X-Ser-X-Gly) around the active site serine. The expressed lipase was purified by hydrophobic interaction and ion exchange chromatography using buffers containing 0.02% (v/v) Triton X-100. The lipase was most active at 60-65°C and in alkaline conditions around pH 9-10. The lipase had highest activity toward p-nitrophenyl caprylate among the synthetic substrates and tripropionin among the triglycerides. It hydrolyzed beef tallow and palm oil more rapidly than olive oil at 50°C.
Keyword
lipaseBacillus stearothermophilusthermostable enzyme
ISSN
0916-8451
Publisher
T&F (Taylor & Francis)
DOI
http://dx.doi.org/10.1271/bbb.62.66
Type
Article
Appears in Collections:
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
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