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Biotechnology of Microbial Lipases
Engleski
140 b
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Lipases (triacylglycerol acylhydrolase, E.C. 3.1.1.3) are ubiquitous enzymes of considerable physiological significance and industrial importance. They catalyze the hydrolysis of triacylglycerols to diacylglycerols, monoacylglycerols, free fatty acids and glycerol. This hydrolytic reaction is reversible under low water activities or micro- aqueous conditions, resulting in the synthesis of ester bonds. Generally, their natural substrates are long chain fatty acyl esters insoluble in aqueous solutions. The interest in lipases stems primarily from their ability to preferentially hydrolyze long/short or saturated/unsaturated fatty acyl residues and their positional specificity for the 1 (3) or 1,2 (2,3) positions of a triacylglycerol molecule. They remain active in a number of organic solvents and can catalyze various synthetic as well as hydrolytic reactions, which make them excellent candidates for application in different industries/sectors like oleochemicals, detergents, pharmaceuticals, food and dairy, pulp and paper, leather processing, agrochemicals, bioremediation, biopolymer, biosensors, biodiesel and others.
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