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Catalog Portfolio 2018

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Lipases

Lipases (EC 3.1.1.3) catalyze the hydrolysis of water-insoluble esters such as triglycerides like triolein to diolein. In addition, lipases also convert a broad range of natural and unnatural esters, while retaining high enantio- or regioselectivity. They require no cofactors and are stable and active when organic solvents are added to the reaction mixture in high concentrations.
This combination of broad substrate range and high selectivity makes lipases an ideal catalyst for organic synthesis.

Chemists use lipase-catalyzed biotransformations to prepare enantiomerically-pure pharmaceuticals and synthetic intermediates, to protect and deprotect synthetic intermediates as well as for more specialized uses. Besides high selectivity and broad substrate range, another major advantage of lipases for synthetic reactions is that they act efficiently on water-insoluble substrates. Water, biphasic and pure organic solvent systems are possible for desired reactions.

Examples for very well described lipase catalyzed reactions are hydrolysis, esterification, aminolysis in which the natural nucleophile – water – is replaced by an alcohol, hydroperoxide or amine. The lipase-catalyzed esterification reactions are among the most significant chemical and biochemical processes of industrial relevance due to an increased use of organic esters in biotechnology and the chemical industry.

The diagram shows the general reaction schemes for the lipases catalyzed reactions: (a) hydrolysis or esterification, (b) transesterification, (c) aminolysis

Reactions catalyzed by lipases: (a) Hydrolysis or esterification, (b) Transesterification, (c) Aminolysis