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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
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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 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
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 +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
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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 +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
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. Guisan +5 more
openaire +2 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 adsorption on different nanomaterials: a multi-scale simulation study.
Physical Chemistry, Chemical Physics - PCCP, 2015Candida antarctica lipase B (CalB) is an efficient biocatalyst for hydrolysis and esterification, which plays an important role in the production of biodiesel in the bioenergy industries.
Daohui Zhao, Chunwang Peng, Jian Zhou
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 +4 more sources