BioChem - DOS

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

Biocatalysis and agricultural biotechnology

Romero, C.M.; Pera, L.M.; Loto, F.; Vallejos, C.; Castro, G.; Baigori, M.D.

An organic solvent-tolerant lipase from olive oil-induced Aspergillus niger MYA 135 supernatant was purified using two methods: electroelution and ion-exchange chromatography. 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 68kDa. The isoelectric point (pI) of the lipase was 5.1 and optimum pH and temperature for activity were 7.0 and 37<SUP>o</SUP>C, respectively. The lipase showed affinity for esters with long acyl chains, with a K<SUB>m</SUB> of 0.99mM for C18. Substrate specificity of the immobilized lipase was highest for C18 among the various &alpha;- and &beta;-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.

2012

Elsevier

1878-8181

1

1

pp.25-31

10.1016/j.bcab.2011.08.013

http://click.ndsl.kr/servlet/OpenAPIDetailView?keyValue=05787966&target=NART&cn=NART58028481

Lipase; Aspergillus niger; Purification; Organic solvent-tolerant