Results 251 to 260 of about 202,412 (300)
FEMS Microbiology Reviews, 1994 Many different bacterial species produce lipases which hydrolyze esters of glycerol with preferably long-chain fatty acids. They act at the interface generated by a hydrophobic lipid substrate in a hydrophilic aqueous medium. A characteristic property of lipases is called interfacial activation, meaning a sharp increase in lipase activity observed when
Bauke W Dijkstra +2 more
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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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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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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
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Lipases at interfaces: A review
Advances in Colloid and Interface Science, 2009Lipases are acyl hydrolases that play a key role in fat digestion by cleaving long-chain triglycerides into polar lipids. Due to an opposite polarity between the enzyme (hydrophilic) and their substrates (lipophilic), lipase reaction occurs at the interface between the aqueous and the oil phases.
Reinhard Miller, M E Leser, M E Leser
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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
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Lipase–lipase interactions as a new tool to immobilize and modulate the lipase properties
Enzyme and Microbial Technology, 2005Abstract 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.
Glória Fernandez-Lorente +2 more
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2018
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 characteristics of these enzymes. This chapter reviews the main sources, structural properties, and industrial applications of these highly studied enzymes.
Casas-Godoy, Leticia +5 more
openaire +3 more sources
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 characteristics of these enzymes. This chapter reviews the main sources, structural properties, and industrial applications of these highly studied enzymes.
Casas-Godoy, Leticia +5 more
openaire +3 more sources
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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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.
openaire +2 more sources