Issue 7, 2015

Saturation mutagenesis in selected amino acids to shift Pseudomonas sp. acidic lipase Lip I.3 substrate specificity and activity

Abstract

Several Pseudomonas sp. CR611 Lip I.3 mutants with overall increased activity and a shift towards longer chain substrates were constructed. Substitution of residues Y29 and W310 by smaller amino acids provided increased activity on C18-substrates. Residues G152 and S154, modified to study their influence on interfacial activation, displayed a five and eleven fold increased activity.

Graphical abstract: Saturation mutagenesis in selected amino acids to shift Pseudomonas sp. acidic lipase Lip I.3 substrate specificity and activity

Supplementary files

Article information

Article type
Communication
Submitted
28 Oct 2014
Accepted
28 Nov 2014
First published
28 Nov 2014

Chem. Commun., 2015,51, 1330-1333

Author version available

Saturation mutagenesis in selected amino acids to shift Pseudomonas sp. acidic lipase Lip I.3 substrate specificity and activity

P. Panizza, S. Cesarini, P. Diaz and S. Rodríguez Giordano, Chem. Commun., 2015, 51, 1330 DOI: 10.1039/C4CC08477B

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