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Lipases

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The following article is from The Great Soviet Encyclopedia (1979). It might be outdated or ideologically biased.

Lipases

 

enzymes of the hydrolase class that catalyze the hydrolysis of ester linkages in triglycerides, with the formation of a fatty acid and glycerol. Lipases have been discovered in animals, plants (for example, in sunflower seeds), and microorganisms.

In mammals, lipases digest (decompose) fat. They are contained predominantly in pancreatic juice, from which a pure preparation of pancreatic lipase was first isolated in 1956. They are also found in the intestinal walls and in milk. Lipoprotein lipase, which catalyzes the hydrolysis of triglycerides bonded to proteins, is found in the blood plasma. The length of the chains and the degree to which the fatty acids are unsaturated have almost no influence on the activity of a lipase. Pancreatic and lipoprotein lipases hydrolyze only emulsified fats. The hydrolysis of triglycerides catalyzed by lipases is reversible. The reverse reaction is possible by means of biosynthesis.

REFERENCE

Lipid Metabolism. New York-London, 1970.

N. V. PROKAZOVA

The Great Soviet Encyclopedia, 3rd Edition (1970-1979). © 2010 The Gale Group, Inc. All rights reserved.
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References in periodicals archive
Freire, "Production and use of lipases in bioenergy: a review from the feedstocks to biodiesel production," Enzyme Research, vol.
Table 1: Characteristics of TA lipases. TA lipases MW T pH ([degrees]C) Pseudomonas sp.
Except for lipase immobilized on chitosan using acetone adsorption, all lipases demonstrated the highest activity at 45[degrees]C (Figures 4 and 5), suggesting that immobilized enzymes were significantly more active at higher temperatures than the free enzyme.
rugosa lipases seem more efficient in catalyzing the incorporation of long-chain unsaturated fatty acids such as oleic acid than medium-chain saturated fatty acids such as caprylic acid.
After the culture, and when a maximum lipase activity is detected according to the results of a first culture, stabilization of the whole-cell biocatalysts was developed according to the method of Ban et al.
Commercial Lipase and Whole-Cell-Catalyzed Transesterification.
Lipases as sustainable biocatalysts for the sustainable industrial production of fine chemicals and cosmetics.
Solid-state fermentation of coconut kernel-cake as substrate for the production of lipases by the coconut kernel-associated fungus Lasiodiplodia theobromae VBE-1.
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