• Microbiology and Biotechnology Letters
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• v.16 no.4
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• pp.259-264
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• 1988

Two forms of extracellular inulinase, designated as PI and PII were detected in the crude enzyme preparation from n species of Pseudomonas isolated from soil. PI and PII were purified to homogeneity by ammonium sulfate fractionation, DEAE Sephadex A-50 chromatography, Sephadex G-100 and Sephadex G-200 gel filteration. Both isoenzymes catalyzed specifically and endowise the cleavage of the $\beta$-2,1-fructofranoside linkage of inulin, and displayed no action upon sucrose, raffinose and levan. The optimal pH values for the PI and PII enzyme were pH 5.5 and 6.0, respectively and the highest activity of the two enzymes was observed at 55$^{\circ}C$. The Km values of PI and PII were calculated to be 2$\times$10$^{-3}$M and 5$\times$10$^{-3}$M, respectively.

• Journal of Life Science
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• v.14 no.5
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• pp.834-839
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• 2004

To improve and oil degrading activity, the lipase gene from Pseudomonase sp. was transformed into Klebsiella sp. KCL-l, an oil degrading bacterium. The selected trasformant was named as a KCL-1/pET-Lip. The surface tension of culture broth of KCL-1/pET-Lip was decreased to 33 dyne/cm from 55 dyne/cm using 4% (v/v) soybean oil as sole carbon source. The surface tension were 44 and 37.5 dyne/cm, to 2% (w/v) glucose and 4% (v/v) kerosene medium, respectively. The emulsification activity of the biosurfactant solution containing lipase of KCL-l/pET-Lip improved better than wild type KCL-l. The soybean oil was most efficient carbon source and substrate for surface activity and emulsification activity of KCL-1/pET-Lip. The expression of lipase was confirmed by SDS-PAGE.