Purification of an organic solvent-tolerant lipase from Aspergillus niger MYA 135 and its application in ester synthesis.

CINTIA ROMERO; LICIA PERA; FLAVIA LOTO; CECILIA VALLEJOS; GUILLERMO CASTRO

Biocatalysis and Agricultural Biotechnology

ELSEVIER SCIENCE BV

Año: 2011 vol. 1 p. 25 - 31

1878-8181

An organic solvent-tolerant lipase from olive oil-induced Aspergillus niger MYA supernatant was purified using two methods: electroelution and ion-exchangechromatography. With electroelution purification was 8.4-fold and recovery 47% and  with ion-exchange 16.6-fold and 53.4%, respectively. The purified enzyme showed a prominent single band with SDS?PAGE and was a monomeric protein of 68 kDa. The isoelectric point (pI) of the lipase was 5.1 and optimum pH and temperature for activity were 7.0 and 37 °C, respectively. The lipase showed affinity for esters with long acyl chains, with a Km of 0.99 mM for C18. Substrate specificity of the immobilized lipase was highest for C18 among the various α- and β-naphthyl esters assayed. Substrate specificity agreed with kinetics parameters of long-chain fatty acids (C18). Transesterification activity of the A. niger MYA 135 lipase indicates that it could be a potential biocatalyst for biodiesel production.