Linked Life Data

16233516

Source:http://linkedlifedata.com/resource/pubmed/id/16233516

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2005-10-19
pubmed:abstractText
The extracellular lipase gene (lipA) from Pseudomonas fluorescens HU380 was cloned from a genomic library constructed in pBluescript SK+. Nucleotide sequence analysis revealed an open reading frame of 1854 by encoding the lipase. Its deduced amino acid sequence included internal amino acid sequences of the lipase from this strain: The lipase showed significant sequence similarity to lipases of Serratia marcescens strains and P. fluorescens strains. In Escherichia coli, lipA was expressed in the form of inclusion bodies, which were subsequently solubilized by urea followed by dialysis. The refolded protein was soluble and biologically active. The lipase purified from the E. coli transformant by this denaturation-renaturation procedure followed by only two steps of column chromatographs exhibited the same electrophoretic mobility as did the enzyme purified from P. fluorescens HU380, and both enzymes were quite similar in physicochemical properties such as specific activity, suggesting that the recombinant lipase protein has an intrinsic folding capability in vitro. The function of its C-terminal region is also discussed.
pubmed:language
eng
pubmed:journal
pubmed:status
PubMed-not-MEDLINE
pubmed:issn
1389-1723
pubmed:author
pubmed:issnType
Print
pubmed:volume
96
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
242-9
pubmed:year
2003
pubmed:articleTitle
A novel lipase from Pseudomonas fluorescens HU380: gene cloning, overproduction, renaturation-activation, two-step purification, and characterization.
pubmed:affiliation
Medical Enzyme Division, Amano Enzyme Co., Ltd., Kakamigahara, Gifu 509-0108, Japan.
pubmed:publicationType
Journal Article