Cloning, purification and characterisation of Staphylococcus warneri lipase 2

A gene encoding an extracellular lipase was identified in Staphylococcus wa rneri 863. The deduced lipase is organised as a prepro-protein and has sign ificant similarity to other staphylococcal lipases. The mature part of the lipase was expressed with an N-terminal histidine tag in Escherichia coli, purified and biochemically characterised. The results show that the purifie d lipase (named SWL2) combines the properties of the staphylococcal lipases characterised so far. It has both a high preference for short chain substr ates and surprisingly, it also displays phospholipase activity. Homology al ignment was used to analyse sequence-function relationships of the staphylo coccal lipase family with the aim to identify the structural basis underlyi ng the different properties of the staphylococcal lipases. (C) 2001 Elsevie r Science B.V. All rights reserved.