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Lipases for biotechnology

Current Opinion in Biotechnology, 2002
Lipases constitute the most important group of biocatalysts for biotechnological applications. The high-level production of microbial lipases requires not only the efficient overexpression of the corresponding genes but also a detailed understanding of the molecular mechanisms governing their folding and secretion.
Karl-Erich Jaeger, Thorsten Eggert
openaire   +3 more sources

Purification of lipases

Journal of Biotechnology, 1992
Interest on lipases from different sources (microorganisms, animals and plants) has markedly increased in the last decade due to the potential applications of lipases in industry and in medicine. Microbial and mammalian lipases have been purified to homogeneity, allowing the successful determination of their primary aminoacid sequence and, more ...
M. A. Taipa   +2 more
openaire   +3 more sources

Lipase–lipase interactions as a new tool to immobilize and modulate the lipase properties

Enzyme and Microbial Technology, 2005
Abstract Lipase from Burkholderia cepacia (formerly Pseudomonas fluorescens ) (BCL) was previously immobilized on glyoxyl-agarose and the active site was blocked after incubation with diethyl- p -nitrophenylphosphate, obtaining a new “glyoxyl-BCL * ” matrix to adsorbe lipases.
Jose M. Guisan   +5 more
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Staphylococcal lipases

Lipids, 1974
AbstractA lipase rich fraction was isolated from the cell free supernatant of 24 hr broth culture ofStaphylococcus aureus B‐120, grown in trypticase soy broth at 37 C. Lipase from the cell free supernatant was precipitated with equal volumes of absolute ethanol.
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Lipase‐Specific Foldases

ChemBioChem, 2004
AbstractLipases represent the most important class of enzymes used in biotechnology. Many bacteria produce and secrete lipases but the enzymes originating from Pseudomonas and Burkholderia species seem to be particularly useful for a wide variety of different biocatalytic applications.
Jan Tommassen   +2 more
openaire   +5 more sources

Lipoprotein Lipase Deficiency

The Indian Journal of Pediatrics, 2020
To analyse the clinical and molecular spectrum of Lipoprotein Lipase (LPL) deficiency and to highlight the effect of a cost-effective indigenous diet for management of this disorder.This is a single-centre retrospective study. Fifteen patients from 14 kindreds with severe hypertriglyceridemia (more than 1000 mg/dl) were evaluated for a period of 12.5 y
Shwetha Kuthiroly   +6 more
openaire   +4 more sources

Interfacial catalysis by lipases

Journal of Molecular Catalysis B: Enzymatic, 2001
Abstract We designed a convenient, specific, sensitive and continuous lipase activity assay using natural long-chain triacylglycerols (TAGs). Oil was extracted from Parinari glaberrimum seed kernels and the purified TAGs used as a substrate for detecting low levels of lipase activities. The purified TAGs are naturally fluorescent.
Beisson, Frédéric   +5 more
openaire   +4 more sources

Triacylglycerol lipase, monoacylglycerol lipase and phospholipase activities of highly purified rat hepatic lipase

Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1982
Highly purified rat hepatic lipase (NaCl-resistant, alkaline pH optimum) was studied to evaluate whether the enzyme has triacylglycerol lipase, monoacylglycerol lipase and phospholipase activities. Enzyme exhibiting a single band by SDS-polyacrylamide gel electrophoresis and having a specific activity eight times greater than that in any previous ...
Gordon L. Jensen   +2 more
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Expression of lipoprotein lipase gene in combined lipase deficiency

Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1989
The expression of the gene for lipoprotein lipase (LPL) was studied in brown adipose tissue and the liver of combined lipase deficient (cld/cld) and unaffected mice. The mRNA specific for LPL was detected in both animals. Although the size of LPL mRNA in cld mice was similar to that of unaffected mice, the mRNA concentration in affected animals was ...
K, Oka   +9 more
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