Bacterial lipases
Many different bacterial species produce lipases which hydrolyze esters of glycerol with
preferably long-chain fatty acids. They act at the interface generated by a hydrophobic lipid …
preferably long-chain fatty acids. They act at the interface generated by a hydrophobic lipid …
Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases
▪ Abstract Bacteria produce and secrete lipases, which can catalyze both the hydrolysis and
the synthesis of long-chain acylglycerols. These reactions usually proceed with high …
the synthesis of long-chain acylglycerols. These reactions usually proceed with high …
Lipase protein engineering
A Svendsen - Biochimica et Biophysica Acta (BBA)-Protein Structure …, 2000 - Elsevier
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Advances in recombinant lipases: Production, engineering, immobilization and application in the pharmaceutical industry
Lipases are one of the most used enzymes in the pharmaceutical industry due to their
efficiency in organic syntheses, mainly in the production of enantiopure drugs. From an …
efficiency in organic syntheses, mainly in the production of enantiopure drugs. From an …
Purification and preliminary characterization of the extracellular lipase of Bacillus subtilis 168, an extremely basic pH‐tolerant enzyme
E Lesuisse, K Schanck, C Colson - European Journal of …, 1993 - Wiley Online Library
The extracellular lipase of Bacillus subtilis 168 was purified from the growth medium of an
overproducing strain by ammonium sulfate precipitation followed by phenyl‐Sepharose and …
overproducing strain by ammonium sulfate precipitation followed by phenyl‐Sepharose and …
Compilation and analysus of Bacillus Subtilis σ A -dependent promoter sequences: evidence for extended contact between RNA …
JD Helmann - Nucleic acids research, 1995 - academic.oup.com
Sequence analysis of 236 promoters recognized by the Bacillus subtilis σARNA polymerase
reveals an extended promoter structure. The most highly conserved bases include the− 35 …
reveals an extended promoter structure. The most highly conserved bases include the− 35 …
The crystal structure of Bacillus subtili lipase: a minimal α/β hydrolase fold enzyme
G Van Pouderoyen, T Eggert, KE Jaeger… - Journal of molecular …, 2001 - Elsevier
The X-ray structure of the lipase LipA from Bacillus subtilis has been determined at 1.5 Å
resolution. It is the first structure of a member of homology family I. 4 of bacterial lipases. The …
resolution. It is the first structure of a member of homology family I. 4 of bacterial lipases. The …
Thermoalkalophilic lipase of Bacillus thermocatenulatus. I. Molecular cloning, nucleotide sequence, purification and some properties
An expression library was generated by partial Sau3A digestion of genomic DNA from the
thermophile Bacillus thermocatenulatus and cloning of DNA fragments in pUC18 in …
thermophile Bacillus thermocatenulatus and cloning of DNA fragments in pUC18 in …
Screening, purification and properties of a thermophilic lipase from Bacillus thermocatenulatus
C Schmidt-Dannert, H Sztajer, W Stöcklein… - … et Biophysica Acta (BBA …, 1994 - Elsevier
By screening of 15 thermophilic Bacillus strains, five strains exhibiting lipase activity were
found. Among these the strain Bacillus thermocatenulatus (DSM 730) produced the highest …
found. Among these the strain Bacillus thermocatenulatus (DSM 730) produced the highest …
Gene Cloning and Characterization of Thermostable Lipase from Bacillus stearothermophilus L1
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 …
Escherichia coli. Sequence analysis showed an open reading frame of 1254 bp, which …