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- Title
Immobilization and characterisation of a lipase from a new source, Bacillus sp. ITP-001.
- Authors
Cabrera-Padilla, Rebeca; Albuquerque, Matheus; Figueiredo, Renan; Fricks, Alini; Franceschi, Elton; Lima, Álvaro; A dos Santos, Onelia; Silva, Daniel; Soares, Cleide
- Abstract
A new source of lipase from Bacillus sp. ITP-001 was immobilized by physical adsorption on the polymer poly(3-hydroxybutyrate-co-hydroxyvalerate) (PHBV) in aqueous solution. The support and immobilized lipase were characterised, compared to the lyophilised lipase, with regard to the specific surface area, adsorption-desorption isotherms, pore volume ( Vp) and size (dp) by nitrogen adsorption, differential scanning calorimetry, thermogravimetric analysis, chemical composition analysis, Fourier transform infrared spectroscopy and biochemical properties. The immobilized enzyme displayed a shift in optimum pH towards the acidic side with an optimum at pH 4.0, whereas the optimum pH for the free enzyme was at pH 7.0; the optimum temperature of activity was 80 and 37 °C for the free and immobilized enzyme, respectively. The inactivation rate constant for the immobilized enzyme at 37 °C was 0.0038 h and the half-life was 182.41 h. The kinetic parameters obtained for the immobilized enzyme gave a Michaelis-Menten constant ( K) of 49.10 mM and a maximum reaction velocity ( V) of 205.03 U/g. Furthermore, the reuse of the lipase immobilized by adsorption allowed us to observe that it could be reused for 10 successive cycles, duration of each cycle (1 h), maintaining 33 % of the initial activity.
- Subjects
ENCAPSULATION (Catalysis); LIPASES; BACILLUS sphaericus; PHYSISORPTION; AQUEOUS solutions; FOURIER transform infrared spectroscopy; ATMOSPHERIC temperature
- Publication
Bioprocess & Biosystems Engineering, 2013, Vol 36, Issue 10, p1385
- ISSN
1615-7591
- Publication type
Article
- DOI
10.1007/s00449-012-0875-1