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Production of laccases in submerged process by Pleurotus sajor-caju PS-2001 in relation to carbon and organic nitrogen sources, antifoams and Tween80

Some conditions in media composition for laccases production, such as different sources of carbon and organic nitrogen, antifoams and a surfactant, were studied in liquid cultures of Pleurotus sajor-caju strain PS-2001. Cultivation with fructose or glucose as carbon sources produced maximum enzyme a...

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Bibliographic Details
Published in:Journal of industrial microbiology & biotechnology 2009-01, Vol.36 (1), p.1-9
Main Authors: Bettin, Fernanda, Montanari, Queli, Calloni, Raquel, Gaio, Tamara A, Silveira, Mauricio M, Dillon, Aldo JP
Format: Article
Language:English
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Summary:Some conditions in media composition for laccases production, such as different sources of carbon and organic nitrogen, antifoams and a surfactant, were studied in liquid cultures of Pleurotus sajor-caju strain PS-2001. Cultivation with fructose or glucose as carbon sources produced maximum enzyme activities of 37 and 36UmL super(-1), respectively. When sucrose was present in the medium, the best results were obtained using 5gL super(-1) of this carbohydrate, on the 11th day of the process, attaining laccase titres of 13UmL super(-1). In a medium without casein, practically no enzyme was produced during the experiments; among the sources of nitrogen studied, pure casein led to the highest titres of laccase activity. Different concentrations of pure casein and sucrose were also tested. As to the different concentrations of casein, the addition of 1.5gL super(-1) resulted in the highest titres of laccase activity. Negligible levels of manganese peroxidase activity were also detected in the culture medium. In low concentrations, polypropylene glycol or silicon-based antifoams and the surfactant Tween80 have no significant influence on the formation of laccases by P.sajor-caju. However, enhanced concentration of polypropylene glycol negatively affected the production of laccases but favored the titres in total peroxidases, lignin peroxidase and veratryl alcohol oxidase.
ISSN:1367-5435
1476-5535
DOI:10.1007/s10295-008-0463-1