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Lipoprotein lipase and hepatic lipase
Current Opinion in Lipidology, 1990Lipoprotein metabolism involves two major steps (Eisenberg 1990). First, triglyceride (TG) rich lipoproteins bind transiently to lipoprotein lipase (LPL) at the vascular endothelium (Fig. 1). The enzyme rapidly hydrolyzes triglycerides, which accomplishes two things (Eckel 1989): it enables the tissues to utilize fatty acids from the lipoproteins, and ...
Thomas Olivecrona +1 more
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Use of immobilized lipases for lipase purification via specific lipase–lipase interactions
Journal of Chromatography A, 2004Lipase from Pseudomonas fluorescens (PFL), an enzyme with a great tendency to yield bimolecular aggregates, was immobilized via multipoint covalent attachment on glyoxyl-agarose in the presence of Triton X-100. This strategy permitted to obtain the enzyme with the active center oriented towards the reaction medium.
Jose M, Palomo +5 more
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Journal of Inherited Metabolic Disease, 1988
SummaryTwo enzymes, lipoprotein lipase and hepatic triglyceride lipase, are involved in the hydrolysis of triglycerides from chylomicrons and very low density lipoprotein (VLDL). Lipoprotein lipase has an absolute requirement for apolipoprotein CII for activity.
H, Greten, F U, Beil
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SummaryTwo enzymes, lipoprotein lipase and hepatic triglyceride lipase, are involved in the hydrolysis of triglycerides from chylomicrons and very low density lipoprotein (VLDL). Lipoprotein lipase has an absolute requirement for apolipoprotein CII for activity.
H, Greten, F U, Beil
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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
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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 +2 more sources
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
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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 +2 more sources
2012
Lipases are ubiquitous enzymes, widespread in nature. They were first isolated from bacteria in the early nineteenth century and the associated research continuously increased due to the particular characteristics of these enzymes. This chapter reviews the main sources, structural properties, and industrial applications of these highly studied enzymes.
Casas-Godoy, Leticia +4 more
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Lipases are ubiquitous enzymes, widespread in nature. They were first isolated from bacteria in the early nineteenth century and the associated research continuously increased due to the particular characteristics of these enzymes. This chapter reviews the main sources, structural properties, and industrial applications of these highly studied enzymes.
Casas-Godoy, Leticia +4 more
openaire +4 more sources

