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Open AccessJournal ArticleDOI

Immobilisation and application of lipases in organic media.

Patrick Adlercreutz
- 08 Jul 2013 - 
- Vol. 42, Iss: 15, pp 6406-6436
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TLDR
The practical applications of lipases in organic media reviewed include ester synthesis, modification of triacylglycerols and phospholipids, fatty acid enrichment, enantiomer resolution, biodiesel production and acylation of carbohydrates and bioactive compounds.
Abstract
Different methods of preparing lipases for use in organic media are critically reviewed. Solid lipase preparations can be made by typical immobilisation methods such as adsorption, entrapment, covalent coupling or cross-linking. Immobilisation is especially attractive for lipases because, in addition to the normal benefits of enzyme immobilisation, it can also lead to a considerable increase in catalytic activity, probably caused by conformational changes in the lipase molecules. Activation can be achieved, for example, using hydrophobic support materials or surfactants during the immobilisation procedure. Surfactants can also be used to solubilise lipases in organic media via the formation of hydrophobic ion pairs, surfactant-coated lipase or reversed micelles. Lipase preparation methods are discussed with regard to potential lipase inactivation and activation effects, mass transfer limitations, lipase stability and other features important for applications. The practical applications of lipases in organic media reviewed include ester synthesis, modification of triacylglycerols and phospholipids, fatty acid enrichment, enantiomer resolution, biodiesel production and acylation of carbohydrates and bioactive compounds.

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Citations
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Journal ArticleDOI

Enzyme immobilization by adsorption: a review

TL;DR: In this paper, a comparative analysis of the literature reports on the recent trends in the enzyme immobilization by adsorption is presented, where both carriers, carrier modifiers and procedures developed for effective adaption of the enzymes are discussed.
Journal ArticleDOI

Immobilization of lipases on hydrophobic supports involves the open form of the enzyme

TL;DR: The results confirm that the lipases immobilized on octyl agarose presented their open form stabilized while the covalent preparation maintains a closing/opening equilibrium that may be modulated by altering the medium.
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Lipase catalysis in organic solvents: advantages and applications

TL;DR: The present review describes the advantages of lipase-catalyzed reactions in organic Solvents and various effects of organic solvents on their activity.
Journal ArticleDOI

Microbial lipases and their industrial applications: a comprehensive review

TL;DR: Immobilization has made the use of microbial lipases accomplish its best performance and hence suitable for several reactions and need to enhance aroma to the immobilization processes and reduce logistical liability on the environment and user.
References
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Journal ArticleDOI

Analysis of membrane and surface protein sequences with the hydrophobic moment plot.

TL;DR: An algorithm has been developed which identifies alpha-helices involved in the interactions of membrane proteins with lipid bilayers and which distinguishes them from helices in soluble proteins, and suggests four transmembrane helices and a surface-seeking helix in fragment B, the moiety known to have trans Membrane function.
Journal ArticleDOI

Biodiesel production from waste cooking oil: 1. Process design and technological assessment

TL;DR: The acid-catalyzed process using waste cooking oil proved to be technically feasible with less complexity than the alkali-catalystzed process, thereby making it a competitive alternative to commercial biodiesel production by the alkaline-catalyszed process.
Journal ArticleDOI

A serine protease triad forms the catalytic centre of a triacylglycerol lipase.

TL;DR: The X-ray structure of the Mucor miehei triglyceride lipase is reported and the atomic model obtained reveals a Ser .. His .. Asp trypsin-like catalytic triad with an active serine buried under a short helical fragment of a long surface loop.
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