Biochemical characterisation of lipase from a new strain of Bacillus sp. ITP-001

AUTOR(ES)

Barbosa, José Murillo P., Souza, Ranyere L., Melo, Cláudia Moura de, Fricks, Alini T., Soares, Cleide Mara F., Lima, Álvaro S.

FONTE

Química Nova

DATA DE PUBLICAÇÃO

2012

RESUMO

Lipases are characterised mainly by catalytic versatility and application in different industrial segments. The aim of this study was to biochemically characterise a lipase from a new strain of Bacillus sp. ITP-001. The isoelectric point and molecular mass were 3.12 and 54 kDa, respectively. The optima lipase activity was 276 U g-1 at pH 7.0 and a temperature of 80 ºC, showing greater stability at pH 5.0 and 37 ºC. Enzymatic activity was stimulated by various ions and pyridine, and inhibited by Cu+ and ethanol. The values of Km and v max were 105.26 mmol and 0.116 mmol min-1 g-1, respectively determined by the Eadie-Scatchard method.

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