Mucor griseocyanus Lipase: Production, Characterization and Study of Some Catalytic Properties of the Immobilised Enzyme

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dc.contributor.authorJanny Coca Armas
dc.contributor.authorJulio C. Dustet Mendoza
dc.contributor.authorJose L. Martinez Hernandez
dc.date.accessioned2014-05-12T10:59:14Z
dc.date.available2014-05-12T10:59:14Z
dc.date.issued2008
dc.description.abstractThe 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 lipase exhibited 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.en_US
dc.identifier.citationFood Technol. Biotechnol. 46 (2) 195–201 (2008)en_US
dc.identifier.urihttp://hdl.handle.net/123456789/1148
dc.language.isoenen_US
dc.subjectMucor griseocyanusen_US
dc.subjectlipaseen_US
dc.subjectsubmerged culturesen_US
dc.subjectselective hydrolysisen_US
dc.titleMucor griseocyanus Lipase: Production, Characterization and Study of Some Catalytic Properties of the Immobilised Enzymeen_US
dc.typeArticleen_US

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