Lipases are endowed with a substrate specificity that surpasses that of any other known enzyme. This confers on these enzymes an application potential that is literally boundless. Lipases can be employed in the production of pharmaceuticals, cosmetics, leather, detergents, foods, perfumery, medical diagnostics, and other organic synthetic materials. This review attempts to present a comprehensive discussion on the present status of this unique group of enzymes in industry, as well as the actual potential. It represents an endeavor to provide a sincere answer to the question, "What can be done with this enzyme?" as well as, "Can lipase be utilized for this purpose?" It is intended that the manuscript will cover or at least mention all known applications, based on the exploitation of a particular type of reaction catalyzed by lipases. An attempt will be made to cover as large a number of references as possible, so as to further underline the importance and significance of lipase action for industry. JAOCS 74, 621-634 (1997).

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Ester synthesis by the Mucor miehei lipase has been studied for various alcohol substrates: n‐propanol, n‐butanol, isoamyl alcohol, n‐hexanol, n‐octanol, 2‐ethylhex‐anol, n‐decanol, and lauryl alcohol. The effects of temperature, the nature of the acid, and immobilization of the lipase on its substrate specficity have been elucidated by carrying out esterifications at 29 and 50 °C with lauric and oleic acids and by using both the soluble and immobilized (resin‐adsorbed) forms of the lipase as catalysts. Higher synthesis rates were obtained with oleic acid than with lauric acid. A bimodal distribution pattern was observed for the reaction rate as a function of alcohol chain length. Two superimposed “bells” were obtained with maxima at C4 (butanol) and C10 (decanol) at 29 °C. Whereas immobilization of the lipase did not influence this substrate specificity, an increase in temperature to 50 °C caused a shift in the first peak from C4 to C6 (hexanol), while the second peak position was not affected. The minimum, in all cases, was found to be at C8 (octanol).

The effects of temperature, speed of agitation, enzyme concentration, etc., on butyl laurate synthessis using Mucor miehei lipase (Lipozymetrade mark) have been studied. Although the soluble enzyme was quite thermcstable in aqeous solution, it deactivated rapidly at and above 40 degrees C in the presence of butanol. This enzyme immobilized on an anion-exchange resin (Lipozymetrade mark) showed enhanced stability (as compared to the soluble form) to denaturation by butanol under the same conditions. The denaturation of M. miehei lipase was found to be a function of the butanol concentration in the aqueous phase, and rapid denaturation takes place at the concentration corresponding to its saturation at that temperature. (c) 1995 John Wiley & Sons, Inc.

Esterification, catalyzed by papaya (Carica papaya) lipase (CPL), was studied with various alcohols and carboxylic acids under competitive conditions. Acids studied were straight-chain saturates of different chain lengths, with octanoic acid as the reference. Alcohols chosen were aliphatic straight-chain, branched, secondary, tertiary, terpene, and aromatic alcohols of different chain lengths, using 1-hexanol as the reference. The initial reaction rate increased with increasing chain length of the acid from C4:0 to C18:0, followed by a slight decrease with C20:0. In the case of alcohols, an optimum chain length of 8 carbon atoms was obtained for the straight-chain aliphatic group (C2 to C16). Ethanol, 1-propanol, and secondary and tertiary alcohols showed rather low reactivity. Branching of the alcohols was found not to affect the reactivity in esterification; among the terpenes, beta-citronellol [(2E)-3, 7-dimethyl-6-octenol] and geraniol [(2E)-3,7-dimethylocta-2, 6-dien-1-ol] were found to be more reactive than nerol [(2Z)-3, 7-dimethylocta-2,6-dien-1-ol]. The highest reaction rate was found for the aromatic benzyl alcohol (phenylmethanol).