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Title 

Gene cloning and characterization of thermostable lipase from Bacillus stearothermophilus L1

Authors 

Hyung Kwoun KimSun Yang ParkJung Kee LeeTae Kwang Oh

Publisher 

Japan Society for Bioscience, Biotechnology and Agrochemistry

Issue Date 

1998

Citation 

Bioscience Biotechnology and Biochemistry, vol. 62, no. 1, pp. 66-71

Keywords 

lipaseBacillus stearothermophilusthermostable enzymetriacylglycerol lipasebacterial genegeneticsGeobacillus stearothermophilusmolecular cloningmolecular genetics

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.

ISSN 

0916-8451

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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