Home
Resources
Publications
Purification and Characterization of an Alkaline Lipase From Pseudomonas Fluorescens AK102

Purification and Characterization of an Alkaline Lipase From Pseudomonas Fluorescens AK102

Y Kojima, M Yokoe, T Mase

Biosci Biotechnol Biochem. 1994 Sep;58(9):1564-8.

PMID: 7765474

Abstract:

An extracellular, novel alkaline lipase produced by Pseudomonas fluorescens AK102 was purified by ultrafiltration, ammonium sulfate precipitation, and DEAE-Toyopearl 650M and Phenyl-Toyopearl 650M column chromatographies. The purified enzyme was homogeneous on SDS-PAGE. The molecular weight was estimated to be about 33,000 by SDS-PAGE. The isoelectric point was pH 4.0 by isoelectric focusing. The pH stability was 4 to 10 and the optimum pH was 8 to 10. The optimum temperature was 55 degrees C and the enzyme was stable below 50 degrees C. The enzyme unspecifically liberated short chain to long chain fatty acids from p-nitrophenyl esters, methyl esters, and triglycerides. In the presence of an anionic surfactant, the enzyme was characteristically stable. These results suggested that the enzyme can be used as a home laundry product ingredient.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9001621-A	Amano Lipase from Pseudomonas fluorescens		9001-62-1	Price

As a specialist in analytical chemical Products, Alfa Chemistry offers consumers a wealth of raw materials and a full range of technologies and services.

QUICK LINKS

HEADQUARTERS

Tel:

Fax:

Email: