Conversion of Bacillus thermocatenulatus lipase into an efficient phospholipase with increased activity towards long-chain fatty acyl substrates by directed evolution and rational design.

doi:10.1093/protein/14.11.919

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Article

Conversion of Bacillus thermocatenulatus lipase into an efficient phospholipase with increased activity towards long-chain fatty acyl substrates by directed evolution and rational design.

Protein engineering - 1 Nov 2001

Kauffmann I, Schmidt-Dannert C

Abstract excerpt

The thermoalkalophilic lipase from Bacillus thermocatenulatus BTL2 exhibits a low phospholipase activity (lecithin/tributyrin ratio 0.03). A single round of random mutagenesis of the BTL2 gene followed by screening of 6000 transformants on egg-yolk plates identified three variants with 10-12-fold increased phospholipase activities, corresponding to lecithin/tributyrin ratios of 0.16-0.36. All variants were...

Topics

Amino Acid Sequence
Bacillus
Binding Sites
Escherichia coli
Gene Library
Histidine
Leucine
Lipase
Molecular Sequence Data
Mutagenesis
Mutagenesis, Site-Directed

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Phospholipases

Plasmids

Protein Binding

Protein Conformation

Recombination, Genetic

Sequence Analysis, DNA

Source

Open in PubMed

Identifiers

PMID: 11742112
DOI: 10.1093/protein/14.11.919

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-11742112-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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