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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
exaly +4 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
openaire +4 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 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
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.
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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.
Jose M. Palomo +5 more
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Assay of lipoprotein lipase and hepatic lipase
1992Abstract Lipoprotein lipase (LPL) and hepatic lipase (HL) are two key enzymes in the metabolism and interconversion of lipoproteins (1-3; Table 1). The reactions occur at endothelial surfaces of blood vessels, where the enzymes are attached by interaction with polyanions, probably heparan sulphate proteo glycans anchored in the ...
Gunilla Bengtsson-Olivecrona +1 more
openaire +1 more source
2010
Lipases are highly active in the polymerization of a range of monomers. Both ring-opening polymerization of cyclic monomers such as lactones and carbonates as well as polycondensation reactions have been investigated in great detail. Moreover, in combination with other (chemical) polymerization techniques, lipase-catalyzed polymerization has been ...
Yeniad, B., Naik, H., Heise, A.
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Lipases are highly active in the polymerization of a range of monomers. Both ring-opening polymerization of cyclic monomers such as lactones and carbonates as well as polycondensation reactions have been investigated in great detail. Moreover, in combination with other (chemical) polymerization techniques, lipase-catalyzed polymerization has been ...
Yeniad, B., Naik, H., Heise, A.
openaire +3 more sources
5 Lipoprotein Lipase and Hepatic Lipase
1983Publisher Summary This chapter reviews information on the two major lipolytic enzymes in postheparin plasma, lipoprotein lipase (LpL), and hepatic triglyceride lipase (H-TGL), particularly focusing on their structure, mechanism of action, and role in lipoprotein metabolism.
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Immobilized Lipases for Biodiesel Production: Current and Future Greening Opportunities
Renewable and Sustainable Energy Reviews, 2020Chiaki Ogino +2 more
exaly