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Title 

A direct approach for finding functional lipolytic enzymes from the Paenibacillus polymyxa genome

Authors 

Yeo Jin JungH K KimJihyun KimSeung Hwan ParkTae Kwang OhJung-Kee Lee

Publisher 

The Korean Society for Applied Microbiology

Issue Date 

2005

Citation 

Journal of Microbiology and Biotechnology, vol. 15, no. 1, pp. 155-160

Keywords 

genome databaselipasepaenibacillus polymyxa4 nitrophenyl hexanoateester derivativeesterasehexanoic acidtriacylglycerol lipaseunclassified drugxylan endo 1,3 beta xylosidase

Abstract 

A direct approach was used to retrieve active lipases from Paenibacillus polymyxa genome databases. Twelve putative lipase genes were tested using a typical lipase sequence rule built on the basis of a consensus sequence of a catalytic triad and oxyanion hole. Among them, six genes satisfied the sequence rule and had similarity (about 25%) with known bacterial lipases. To obtain the six lipase proteins, lipase genes were expressed in E. coli cells and lipolytic activities were measured by using tributyrin plate and p-nitrophenyl caproate. One of them, contig 160-26, was expressed as a soluble and active form in E. coli cell. After purifying on Ni-NTA column, its detailed biochemical properties were characterized. It had a maximum hydrolytic activity at 30°C and pH 7-8, and was stable up to 40°C and in the range of pH 5-8. It most rapidly hydrolyzed pNPC6 among various PNP-esters. The other contigs were expressed more or less as soluble forms, although no lipolytic activities were detected. As they have many conserved regions with lipase 160-26 as well as other bacterial lipases throughout their sequence, they are suggested as true lipase genes.

ISSN 

1017-7825

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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