Purification and characterization of a monoacylglycerol lipase from Pseudomonas sp. LP7315.

Abstract

A monoacylglycerol lipase (MGL) was purified from Pseudomonas sp. LP7315 by ammonium sulfate precipitation, anion-exchange chromatography, and preparative electrophoresis. The purified enzyme was homogeneous on SDS-PAGE with a molecular mass of 59 kDa. Its hydrolytic activity was confirmed to be specific for monoglycerides: the enzyme did not hydrolyze di… (More)

Topics

Cite this paper

@article{Sakiyama2001PurificationAC, title={Purification and characterization of a monoacylglycerol lipase from Pseudomonas sp. LP7315.}, author={Tadao Sakiyama and T. Yoshimi and Asako Miyake and M Umeoka and A. Tanaka and Shigeru Ozaki and K. Nakanishi}, journal={Journal of bioscience and bioengineering}, year={2001}, volume={91 1}, pages={27-32} }