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Journal ArticleDOI

Lipase-catalyzed interesterification of oils and fats

A. R. Macrae
- 01 Feb 1983 - 
- Vol. 60, Iss: 2, pp 291-294
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TLDR
Extracellular microbial lipases can be used as catalysts for the interesterification of oils and fats as discussed by the authors, which gives products which are unobtainable by chemical interesterization methods.
Abstract
Extracellular microbial lipases can be used as catalysts for the interesterification of oils and fats. Use of specific lipases gives products which are unobtainable by chemical interesterification methods. Some of these products have properties of value to the oils and fats industry. The catalysts for enzymatic interesterification are prepared by coating inorganic support materials with the lipases. For batch interesterification reactions, the catalyst particles are activated by addition of a small amount of water and then stirred with a reactant mixture dissolved in petroleum ether. At the end of the reaction period, the catalyst particles are removed by filtration, and the interesterified triglycerides isolated by conventional fat fractionation techniques. The catalyst can be used in subsequent batch reactions. As an alternative to the batch reaction system, continuous enzymatic interesterification processes can be operated by pumping water containg feedstock through a packed bed of activated catalyst.

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Biodiesel fuel production by transesterification of oils.

TL;DR: Biodiesel (fatty acid methyl esters), which is derived from triglycerides by transesterification with methanol, has attracted considerable attention during the past decade as a renewable, biodegradable, and nontoxic fuel.
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Industrial applications of microbial lipases

TL;DR: Various industrial applications of microbial lipases in the detergent, food, flavour industry, biocatalytic resolution of pharmaceuticals, esters and amino acid derivatives, making of fine chemicals, agrochemicals, use as biosensor, bioremediation and cosmetics and perfumery are described.
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Enzymatic catalysis in organic media at 100 degrees C

TL;DR: Porcine pancreatic lipase catalyzes the transesterification reaction between tributyrin and various primary and secondary alcohols in a 99 percent organic medium and exhibits a high catalytic activity at that temperature.
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Enzymatic catalysis in nonaqueous solvents.

TL;DR: The rate enhancements afforded by chymotrypsin and subtilisin in the transesterification reaction in octane are of the order of 100 billion-fold; covalent modification of the active center of the enzymes by a site-specific reagent renders them catalytically inactive in organic solvents.
Journal ArticleDOI

Enzymatic catalysis in monophasic organic solvents

TL;DR: Attention is focused on the factors that influence enzymatic catalysis in monophasic solvents including the role of enzyme-associated water, the nature of the biocatalyst preparation, and the properties of the organic solvent.
References
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Journal ArticleDOI

Interesterification of fats

TL;DR: Interesterification changes the distribution of the fatty acids among the glycerides of fats or mixtures of fats from what was present originally as discussed by the authors, which affects the physical nature and behavior of fats.
Journal ArticleDOI

Hydrolysis of phosphoglycerides by purified lipase preparations I. Substrate-, positional- and stereo-specificity

TL;DR: It could be tentatively concluded that the susceptibility of the 1-acyl ester bond to lipase is influenced by the type of bond present at the 2-position, similar to that of phosphatidylcholine.
Journal ArticleDOI

Glyceride synthesis by four kinds of microbial lipase.

TL;DR: Lipases from Aspergillus niger and Rhizopus delemar synthesized glycerides from, not only fatty acid, but dibasic acids and aromatic acids, and made ester bonds at all three available positions of the glycerol molecule, while lipases from Geotricum candidum and Penicillium cyclopium synthesizedglycerides only from long chain fatty acids.
Journal ArticleDOI

On the positional and chain specificities of Candida cylindracea lipase.

TL;DR: It can be concluded that the Candida lipase is able to attack secondary ester groups of glycerol without the help of an isomerase.
Journal ArticleDOI

Characteristics of the lipase from the mold, Geotrichum candidum: a review.

TL;DR: The moldGeotrichum candidum produces an extracellular lipase, readily concentrated by removal of the culture medium in which the microorganism is grown, which has an optimum pH of 8.2, and the lyophilized powder is extremely stable, retaining activity for at least eight years when stored at-20 C.
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