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
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