Biochemical characterisation of lipase from a new strain of Bacillus sp. ITP-001
Autor: | José Murillo P. Barbosa, Ranyere L. Souza, Cláudia Moura de Melo, Alini T. Fricks, Cleide Mara F. Soares, Álvaro S. Lima |
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Jazyk: | English<br />Spanish; Castilian<br />Portuguese |
Rok vydání: | 2012 |
Předmět: | |
Zdroj: | Química Nova, Vol 35, Iss 6, Pp 1173-1178 (2012) |
Druh dokumentu: | article |
ISSN: | 1678-7064 0100-4042 |
DOI: | 10.1590/S0100-40422012000600020 |
Popis: | 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. |
Databáze: | Directory of Open Access Journals |
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