Biochemical and molecular characterisation of a thermoactive, alkaline and detergent-stable lipase from a newly isolated Staphylococcus aureus strain

A newly soil-isolated Staphylococcus aureus strain secretes a non-induced lipase in the culture medium. The extracellular lipase from S. aureus (SAL3) is purified to homogeneity. The purified enzyme is a tetrameric protein (180kDa) corresponding to the association of four lipase molecules. The 15 N-...

Full description

Saved in:
Bibliographic Details
Published in:Journal of molecular catalysis. B, Enzymatic Enzymatic, 2009-04, Vol.56 (4), p.237-245
Main Authors: Horchani, Habib, Mosbah, Habib, Salem, Nadia Ben, Gargouri, Youssef, Sayari, Adel
Format: Article
Language:English
Subjects:
Bioconversions. Hemisynthesis
Biological and medical sciences
Biotechnology
Detergents
Fundamental and applied biological sciences. Psychology
Methods. Procedures. Technologies
Purification
Sequencing
Staphylococcus aureus lipase
Thermo-alkaline
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:A newly soil-isolated Staphylococcus aureus strain secretes a non-induced lipase in the culture medium. The extracellular lipase from S. aureus (SAL3) is purified to homogeneity. The purified enzyme is a tetrameric protein (180kDa) corresponding to the association of four lipase molecules. The 15 N-terminal amino acid residues showed a high degree of homology with other staphylococcal lipase sequences. The part of the gene encoding the mature SAL3 is cloned and sequenced. The deduced polypeptide sequence, corresponding to the mature SAL3, was very similar to the mature Staphylococcus simulans lipase sequence with two additional amino acid residues (LK) at the N-terminus of SAL3. The lipase activity is maximal at pH 9.5 and 55°C. The specific activity of about 4200U/mg or 3500U/mg was measured using tributyrin or olive oil emulsion as substrate, respectively, at pH 9.5 and 55°C. In contrast to other staphylococcal lipases previously characterised, SAL3 is found to be stable between pH 5 and 12 after 24h incubation. The enzyme retained 50% of its activity after 60min incubation at 60°C. This novel lipase is able to hydrolyse its substrate in presence of various oxidizing agents as well as some surfactants and some commercial detergents, then SAL3 can be considered as a good candidate for industrial and biotechnological applications.
ISSN:1381-1177
1873-3158
DOI:10.1016/j.molcatb.2008.05.011