ArticleMolecular biotechnology2010
Heterologous Expression and Purification of a Heat-Tolerant Staphylococcus xylosus Lipase.
Article in Molecular biotechnology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 13 citations in OpenAlex.
- Thermostable lipases and their dynamics of improved enzymatic properties.Applied microbiology and biotechnology · 2021Review
- Insight into the Genome of Staphylococcus xylosus, a Ubiquitous Species Well Adapted to Meat Products.Microorganisms · 2017Review
- Increase of Unsaturated Fatty Acids (Low Melting Point) of Broiler Fatty Waste Obtained Through Staphylococcus xylosus Fermentation.Current microbiology · 2015Article
- The PE-PPE domain in mycobacterium reveals a serine α/β hydrolase fold and function: an in-silico analysis.PloS one · 2011Article
- Biochemical and structural characterization of two site-directed mutants of Staphylococcus xylosus lipase.Molecular biotechnology · 2010Article
- Cloning, expression, purification, and characterization of a novel esterase from Lactobacillus plantarum.Molecular biotechnology · 2010Article
- Staphylococcus xylosus fermentation of pork fatty waste: raw material for biodiesel production.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Staphylococcus xylosus is a microorganism involved in fermentation of meat products and also a natural producer of extracellular lipases. The aim of the present work was to clone and express in E. coli a lipase from S. xylosus (AF208229). This lipase gene (1084 bp) was amplified from a S. xylosus strain isolated from naturally fermented salami and introduced in pET14b expression vector in order to express the recombinant fusion protein (histidine-tagged lipase) in E. coli. Recombinant histidine-tagged S. xylosus lipase was purified by affinity chromatography in an HPLC system. The histidine-tagged lipase is a monomer in solution, as determined by size-exclusion chromatography. It presents a high lipase activity at pH 9.0 and 42 degrees C for p-nitrophenyl acetate and p-nitrophenyl butyrate, among seven different esters assayed (pNPC(2), pNPC(4), pNPC(10), pNPC(12), pNPC(14), pNPC(16), pNPC(18)). Moreover, the enzyme presented a quite interesting thermal stability, after an incubation period of 10 min at 95 degrees C, 77% of the initial activity was retained.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.