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

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A direct approach for finding functional lipolytic enzymes from the Paenibacillus polymyxa genome
Yeo Jin Jung; H K Kim; Jihyun Kim; Seung Hwan Park; Tae Kwang Oh; Jung-Kee Lee
Bibliographic Citation
Journal of Microbiology and Biotechnology, vol. 15, no. 1, pp. 155-160
Publication Year
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.
genome databaselipasepaenibacillus polymyxa
Korea Soc-Assoc-Inst
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Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
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