Mucor griseocyanus Lipase: Production, Characterization and Study of Some Catalytic Properties of the Immobilised Enzyme
Janny Coca Armas1, Julio C. Dustet Mendoza2 and José L. Martínez Hernández3*
1Grupo de Biotecnología Aplicada, Centro de Ingeniería de Procesos, Facultad de Ingeniería Química, Instituto Superior Politécnico 'José Antonio Echeverría', Calle 114 #11901 entre 119 y 127, Marianao, Ciudad Habana, CP 19390 Cuba
2Laboratorio de Hidroquímica, División de Inocuidad de los Alimentos y Sanidad, Centro de Investigaciones Pesqueras, Avenida 5a y 246, Barlovento, Playa, Ciudad Habana, CP 16500 Cuba
3Departamento de Biotecnología, Facultad de Ciencias Químicas, Universidad Autónoma de Coahuila, Blvd. V. Carranza e Ing. J. C. Valdés, Col. Republica, Saltillo, Coahuila, CP 25000 México
Article history:
Received August 9, 2006
Accepted June 11, 2007
Key words:
Mucor griseocyanus, lipase, submerged cultures, selective hydrolysis
Summary:
The aim of this work is to study the production of extracellular lipase by Mucor griseocyanus 55.1.1 strain on different substrates in order to select the ideal one for lipase synthesis. The carbon sources used were: olive oil, glycerol, coconut oil, sunflower oil, glucose, starch and sucrose. The obtained results indicate that the synthesis of the enzyme was possible in the presence of all substrates. Lipase activities in the range of 0.04 to 0.1 IU/mL were obtained. It was found that the most suitable carbon source for the production of the enzyme was a combination of coconut oil and sucrose at 0.5 and 1.5 % (m/V), respectively, and the level of activity reached under this condition was 0.113 IU/mL. The optimum pH and temperature for enzymatic extract activities were identified in a pH range of 4 to 6 and at a temperature of 60 °C. Enzymatic extract was stable for a period of 5 h in neutral and weakly acidic media (pH=6) at moderate temperatures between 20 and 40 °C. Studies on the catalytic properties (stereoselectivity and enantioselectivity) of the immobilized lipase using the esters of methyl phenyl glycinic and (R,S)-methyl mandelic acid showed excellent properties of the enzyme compared to commercial lipases tested. M. griseocyanus lipaseexhibited a greater stereoselectivity towards the R-isomer of methyl phenyl glycinic acid ester. However, with the esters of methyl mandelic acid, the enzyme showed a certain preference toward the S-isomer and it was hydrolysed 20 times faster than the R-isomer.
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