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http://purl.uniprot.org/citations/8396026http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8396026http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8396026http://www.w3.org/2000/01/rdf-schema#comment"The extracellular lipase of Bacillus subtilis 168 was purified from the growth medium of an overproducing strain by ammonium sulfate precipitation followed by phenyl-Sepharose and hydroxyapatite column chromatography. The purified lipase had a strong tendency to aggregate. It exhibited a molecular mass of 19,000 Da by SDS-PAGE and a pI of 9.9 by chromatofocusing. The enzyme showed maximum stability at pH 12 and maximum activity at pH 10. The lipase was active toward p-nitrophenyl esters and triacylglycerides with a marked preference for esters with C8 acyl groups. Using trioleyl glycerol as substrate, the enzyme preferentially cleaved the 1(3)-position ester bond. No interfacial activation effect was observed with triacetyl glycerol as substrate."xsd:string
http://purl.uniprot.org/citations/8396026http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1993.tb18127.x"xsd:string
http://purl.uniprot.org/citations/8396026http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1993.tb18127.x"xsd:string
http://purl.uniprot.org/citations/8396026http://purl.uniprot.org/core/author"Lesuisse E."xsd:string
http://purl.uniprot.org/citations/8396026http://purl.uniprot.org/core/author"Lesuisse E."xsd:string
http://purl.uniprot.org/citations/8396026http://purl.uniprot.org/core/author"Colson C."xsd:string
http://purl.uniprot.org/citations/8396026http://purl.uniprot.org/core/author"Colson C."xsd:string
http://purl.uniprot.org/citations/8396026http://purl.uniprot.org/core/author"Schanck K."xsd:string
http://purl.uniprot.org/citations/8396026http://purl.uniprot.org/core/author"Schanck K."xsd:string
http://purl.uniprot.org/citations/8396026http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8396026http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8396026http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/8396026http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/8396026http://purl.uniprot.org/core/pages"155-160"xsd:string
http://purl.uniprot.org/citations/8396026http://purl.uniprot.org/core/pages"155-160"xsd:string
http://purl.uniprot.org/citations/8396026http://purl.uniprot.org/core/title"Purification and preliminary characterization of the extracellular lipase of Bacillus subtilis 168, an extremely basic pH-tolerant enzyme."xsd:string
http://purl.uniprot.org/citations/8396026http://purl.uniprot.org/core/title"Purification and preliminary characterization of the extracellular lipase of Bacillus subtilis 168, an extremely basic pH-tolerant enzyme."xsd:string
http://purl.uniprot.org/citations/8396026http://purl.uniprot.org/core/volume"216"xsd:string
http://purl.uniprot.org/citations/8396026http://purl.uniprot.org/core/volume"216"xsd:string
http://purl.uniprot.org/citations/8396026http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8396026
http://purl.uniprot.org/citations/8396026http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8396026
http://purl.uniprot.org/citations/8396026http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8396026
http://purl.uniprot.org/citations/8396026http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8396026