Okumura_1980_J.Biochem_87_205

Reference

Title : Purification and properties of partial glyceride hydrolase of Penicillium cyclopium M1 - Okumura_1980_J.Biochem_87_205
Author(s) : Okumura S , Iwai M , Tsujisaka Y
Ref : J Biochem , 87 :205 , 1980
Abstract :

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.

PubMedSearch : Okumura_1980_J.Biochem_87_205
PubMedID: 7358629
Gene_locus related to this paper: penca-mdgli

Related information

Gene_locus penca-mdgli

Citations formats

Okumura S, Iwai M, Tsujisaka Y (1980)
Purification and properties of partial glyceride hydrolase of Penicillium cyclopium M1
J Biochem 87 :205

Okumura S, Iwai M, Tsujisaka Y (1980)
J Biochem 87 :205