Lipase from Aspergillus niger NRRL337 catalyzed the synthesis of esters from various dicarboxylic acids and diols. Amongthe esters synthesized, those from 1,13-tridecanedioic acid and 1,3-propanediol were separated by gel permeation chromatography. The constitution of the

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A lipolytic enzyme which hydrolyzed monoacylglycerols more easily than triacylglycerols was found in the culture broth of Penicillium cyclopium M1. The enzyme was purified to homogeneity and its properties were investigated. Among various substrates used, monoacylglycerols, especially those of medium chain fatty acids, were hydrolyzed very rapidly. Although the rate was low, the enzyme hydrolyzed methyl esters of fatty acids, Span or triacylglycerols of medium chain fatty acids. Based on its substrate specificity, the enzyme was regarded as a partial glyceride hydrolase. When the partial glyceride hydrolase was used in conjunction with lipase on triacylglycerol, the degree of hydrolysis of triacylglycerol became extremely high.

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Penicillium cyclopium Westring produced two kinds of lipases (EC 3.1.1.3) (A and B). At the begining of the cultivation, activity of B-lipase was detected more than that of A-lipase, though only A-lipase was accumulated at the last stage. The pH stability of B-lipase suggested that the eventual decrease of B-lipase activity was brought about by undesirable pH of culture fluid. Two lipases were isolated respectively in homogeneous states and characterized. The pI's of A-and B-lipases were 4.96 and 4.15 and their molecular weights were 27000 and 36000, respectively. In addition, the substrate specificities of two lipases were significantly different from each other.