Results 341 to 350 of about 406,174 (392)
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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.
Roberto Fernandez-Lafuente +5 more
openaire +2 more sources
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
openaire +2 more sources
ACS Applied Materials and Interfaces, 2016
Enhancing the activity and stability of enzymes and improving their reusability are critical challenges in the field of enzyme immobilization. Here we report a facile and efficient biomimetic mineralization to embed thermophilic lipase QLM in zeolite ...
Hongming He +7 more
semanticscholar +1 more source
Enhancing the activity and stability of enzymes and improving their reusability are critical challenges in the field of enzyme immobilization. Here we report a facile and efficient biomimetic mineralization to embed thermophilic lipase QLM in zeolite ...
Hongming He +7 more
semanticscholar +1 more source
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 +5 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 +5 more sources
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
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
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
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
Relevant pH and lipase for in vitro models of gastric digestion.
Food & Function, 2016The development of in vitro digestion models relies on the availability of in vivo data such as digestive enzyme levels and pH values recorded in the course of meal digestion.
L. Sams +3 more
semanticscholar +1 more source
Opening Lids: Modulation of Lipase Immobilization by Graphene Oxides
, 2016Lipases, which can be immobilized and reused for many reaction cycles, are important enzymes with many industrial applications. A key challenge in lipase immobilization for catalysis is to open the lipase lid and maintain it in an open conformation in ...
M. Mathesh +7 more
semanticscholar +1 more source
Interfacial catalysis by lipases
Journal of Molecular Catalysis B: Enzymatic, 2001Abstract 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 +5 more sources