Linked Life Data

15837431

Source:http://linkedlifedata.com/resource/pubmed/id/15837431

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-3
pubmed:dateCreated
2005-5-30
pubmed:abstractText
The Staphylococcus xylosus strain secretes a non-induced lipase in culture medium: S. xylosus lipase (SXL). Pure SXL is a monomeric protein (43 kDa). The 23 N-terminal amino acid residues were sequenced. This sequence is identical to that of Staphylococcus simulans lipase (SSL); in addition, it exhibits a high degree of homology with Staphylococcus aureus lipase (SAL NCTC 8530) sequences. The cloning and sequencing of gene part encoding the mature lipase shows one nucleotide difference with SSL, which corresponds to the change of one residue at a position 311. The lipase activity is maximal at pH 8.2 and 45 degrees C. SXL is able to hydrolyse triacylglycerols without chain length specificity. The specific activity of about 1900 U/mg was measured using tributyrin or triolein as substrate at pH 8.2 and at 45 degrees C in the presence of 2 mM CaCl2. In contrast to some previously characterized staphylococcal lipases, Ca2+ is not required to trigger the activity of SXL. SXL was found to be stable between pH 5 and pH 8.5. The enzyme maintains 50% of its activity after a 15-min incubation at 60 degrees C. Using tripropionin or vinyl esters as substrates, SXL does not present the interfacial activation phenomenon. Unlike many lipases, SXL is able to hydrolyse its substrate in the presence of bile salts or amphiphilic proteins. SXL is a serine enzyme, which is inhibited by THL.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
1723
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
282-91
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Biochemical and molecular characterization of Staphylococcus xylosus lipase.
pubmed:affiliation
Laboratoire de biochimie et de génie enzymatique des lipases, ENIS, BPW 3038 Sfax, Tunisia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't