PURIFICATION AND PROPERTIES OF LIPASE FROM PENICILLIUM-SIMPLICISSIMUM

被引：90

作者：

SZTAJER, H

LUNSDORF, H

ERDMANN, H

MENGE, U

SCHMID, R

机构：

[1] Gesellschaft für Biotechnologische Forschung, Braunschweig

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1992年 / 1124卷 / 03期

关键词：

LIPASE; ENZYME PURIFICATION; HYDROPHOBIC INTERACTION CHROMATOGRAPHY; (P-SIMPLICISSIMUM);

D O I：

10.1016/0005-2760(92)90137-K

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A Penicillium simplicissimum strain has been found to produce an inducible extracellular lipase. Triolein was the best inducer for the enzyme production with the highest activity being achieved after 48 h of incubation. The purified lipase showed a molecular weight of 56 000 by SDS-PAGE. The enzyme exhibited a high ratio of apolar amino acids. The lipase was stable in the pH range of 5-7 and at 50-degrees-C for 15 min. The optimum assay conditions were 37-degrees-C and pH 5.0. The enzyme showed a high stability in water immiscible organic solvents. Lipase from P. simplicissimum is nonspecific and hydrolyses each of the three bonds of triacylglycerols.

引用

页码：253 / 261

页数：9

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[1] ENZYMATIC TRANSESTERIFICATIONS OF CARBONATES IN WATER-RESTRICTED ENVIRONMENTS [J].