A lipase with broad temperature range from an alkaliphilic gamma‐proteobacterium isolated in Greenland
العنوان: | A lipase with broad temperature range from an alkaliphilic gamma‐proteobacterium isolated in Greenland |
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المؤلفون: | Mariane Schmidt, Dorte Møller Larsen, Peter Stougaard |
المصدر: | Environmental Technology. 31:1091-1100 |
بيانات النشر: | Informa UK Limited, 2010. |
سنة النشر: | 2010 |
مصطلحات موضوعية: | Protein Folding, Greenland, Triacylglycerol lipase, law.invention, Bacterial Proteins, Rhodoferax, law, RNA, Ribosomal, 16S, Alteromonadales, Escherichia coli, Environmental Chemistry, Amino Acids, Lipase, Waste Management and Disposal, Peptide sequence, Phylogeny, Water Science and Technology, biology, Pseudomonas, Temperature, General Medicine, biology.organism_classification, Recombinant Proteins, Biochemistry, Genes, Bacterial, Pseudomonadales, biology.protein, Recombinant DNA, Electrophoresis, Polyacrylamide Gel, Gammaproteobacteria |
الوصف: | A gamma-proteobacterium related to the genera Alteromonadales and Pseudomonadales, isolated from a cold and alkaline environment in Greenland, has been shown to produce a lipase active between 5 degrees C and 80 degrees C, with optimal activity at 55 degrees C and pH 8. PCR-based screening of genomic DNA from the isolated bacterium, followed by genome walking, resulted in two complete open reading frames, which were predicted to encode a lipase and its helper protein, a lipase foldase. The amino acid sequence derived for the lipase showed resemblance to lipases from Pseudomonas, Rhodoferax, Aeromonas and Vibrio. The two genes were cloned into different expression systems in E. coli with or without a putative secretion sequence, but despite the fact that both recombinant lipase and lipase foldase were observed on SDS-PAGE, no recombinant lipase activity was detected. Attempts to refold the recombinant lipase in vitro using a purified lipase foldase remained unsuccessful. |
تدمد: | 1479-487X 0959-3330 |
الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::50247a0a57e2d3211e284814b63cbea3Test https://doi.org/10.1080/09593331003770289Test |
رقم الانضمام: | edsair.doi.dedup.....50247a0a57e2d3211e284814b63cbea3 |
قاعدة البيانات: | OpenAIRE |
تدمد: | 1479487X 09593330 |
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