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A New Lipase Isolated from Oleaginous Seeds from Pachira aquatica (Bombacaceae)

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Abstract

A new lipase from seeds of Pachira aquatica was purified to homogeneity by SDS-PAGE obtaining an enzyme with a molecular weight of approximately 55 kDa. The purified lipase exhibited maximum activity at 40°C and pH 8.0, for an incubation time of 90 min. Concerning temperature stability, at the range from 4 to 50°C, it retained approximately 47% of its original activity for 3 h. The enzyme activity increased in the presence of Ca++ and Mg++, but was inhibited by Hg++, Mn++, Zn++, Al+++ and various oxidizing and reducing agents. The lipase was highly stable in the presence of organic solvents, and its activity was stimulated by methanol. The values of K m and V max were 1.65 mM and 37.3 μmol mL−1 min−1, respectively, using p-nitrophenylacetate as substrate. The enzyme showed preference for esters of long-chain fatty acids, but demonstrated significant activity against a wide range of substrates.

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Authors and Affiliations

  1. Department of Physics, State University of São Paulo, Rua Cristovão Colombo, 2265, São José do Rio Preto, SP, CEP 15054-000, Brazil

    Patricia Peres Polizelli

  2. Department of Chemistry and Environmental Sciences, IBILCE-UNESP, State University of São Paulo, Rua Cristovão Colombo, 2265, São José do Rio Preto, SP, CEP 15054-000, Brazil

    Fernanda Dell Antonio Facchini, Hamilton Cabral & Gustavo Orlando Bonilla-Rodriguez

Authors
  1. Patricia Peres Polizelli
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  2. Fernanda Dell Antonio Facchini
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  3. Hamilton Cabral
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  4. Gustavo Orlando Bonilla-Rodriguez
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Correspondence to Gustavo Orlando Bonilla-Rodriguez.

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Polizelli, P.P., Facchini, F.D.A., Cabral, H. et al. A New Lipase Isolated from Oleaginous Seeds from Pachira aquatica (Bombacaceae). Appl Biochem Biotechnol 150, 233–242 (2008). https://doi.org/10.1007/s12010-008-8145-z

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  • DOI: https://doi.org/10.1007/s12010-008-8145-z

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