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Appl Environ Microbiol. 1969 April; 17(4): 606-610
Copyright © 1969 American Society for Microbiology. All Rights Reserved.

Lipase of Mucor pusillus1

G. A. Somkuti2, F. J. Babel and A. C. Somkuti3

a Department of Animal Sciences, Purdue University, Lafayette, Indiana 47907

ABSTRACT

Lipase of Mucor pusillus NRRL 2543 was recovered with ammonium sulfate precipitation, gel filtration on Sephadex G-75, and anion-exchange chromatography on diethylaminoethyl-Sephadex A-50. Maximal glycerol ester hydrolase (lipase) activity was observed at pH 5.0 to 5.5 and 50 C when trioctanoin and olive oil were used as substrates. The enzyme also showed esterase activity; it hydrolyzed, with the exception of methyl butyrate, all methyl esters tested. A minimum chain length of six carbons appeared to be a requirement for esterase activity, which was maximal at about pH 5.5 with methyl dodecanoate (C12) as the substrate. Neither the glycerol ester hydrolase (lipase) nor the esterase activity of the enzyme appeared to be affected by thiol group inhibitors, chelating agents, and reducing compounds. On the other hand, hydrolysis of triolein and methyl dodecanoate was arrested to the same extent in the presence of diisopropyl fluorophosphate, which suggested the involvement of serine in the active center of the enzyme. The enzyme remained stable during a 30-day storage at - 10 C.

FOOTNOTES

2 Present address: Department of Biological Sciences, Duquesne University, Pittsburgh, Pa. 15219.

3 Present address: Department of Microbiology, School of Medicine, University of Pittsburgh, Pittsburgh, Pa. 15213.

1 Published with the approval of the Director of the Purdue University Agricultural Experiment Station as Journal Series Paper No. 3564.

Appl Environ Microbiol. 1969 April; 17(4): 606-610
Copyright © 1969 American Society for Microbiology. All Rights Reserved.





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Copyright © 1969 by the American Society for Microbiology. All rights reserved.