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Lipase from the thermotolerant fungus Rhizopus homothallicus is more thermostable when produced using solid state fermentation than liquid fermentation procedures by J.C. Mateos Diaz; J.A. Rodríguez; S. Roussos; J. Cordova; A. Abousalham; F. Carriere; J. Baratti is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Extracellular lipases were obtained from solid (SSF) and submerged (SmF) thermotolerant Rhizopus homothallicus fungus cell cultures and purified to homogeneity. The two enzymes are monomers having a molecular mass of 29.5 kDa and an identical protein structure, since the Nterminal sequences and peptide maps were identical. However, some of their properties are different, namely the specific activity on trioctanoin (8600 U/mg with SmF and 10,700 U/mg with SSF), the temperature at which maximum activity occurs (30 • C with SmF and 40 • C with SSF) and the thermal stability (half-lives at 50 • C of 0.44 h with SmF and 0.72 h with SSF). These differences between the kinetic properties suggest that when they were tested, one or both fungal lipases might still have been associated with non-proteic compounds originating from the culture medium.

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Author

J.C. Mateos Diaz; J.A. Rodríguez; S. Roussos; J. Cordova; A. Abousalham; F. Carriere; J. Baratti

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 0141-0229)

Published

2006

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)