Cloning, sequencing and expression in Escherichia coli of a thermophilic lipase from Bacillus thermoleovorans ID-1.
A thermophilic lipase of Bacillus thermoleovorans ID-1 was cloned and sequenced. The lipase gene codes 416 amino acid residues and contains the conserved pentapeptide Ala-X-Ser-X-Gly as other Bacillus lipase genes. The optimum temperature of the lipase is 75 degrees C, which is higher than other known Bacillus lipases. For expression in Escherichia coli, the lipase gene was subcloned in pET-22b(+) vector with a strong T7 promoter. Lipase activity was approximately 1.4-fold greater than under the native promoter.
Cho
A R
AR
Department of Biotechnology, College of Engineering and Bioproducts Research Center, Yonsei University, 134 Shinchon-Dong, Sudaemun-Ku, Seoul, South Korea.
Yoo
S K
SK
Kim
E J
EJ
D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology* / Q000235:genetics; D001483:Base Sequence; D003001:Cloning, Molecular / Q000379:methods; D017124:Conserved Sequence; D004795:Enzyme Stability; D004926:Escherichia coli; D015698:Genomic Library; D006358:Hot Temperature; D007700:Kinetics; D008049:Lipase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013816:Thermodynamics
D011994:Recombinant Proteins; D008049:Lipase