INVESTIGADORES
PERA Licia Maria
artículos
Título:
Tailoring chain length selectivity of a solvent-tolerant lipase activity from Aspergillus niger MYA 135 by submerged fermentation
Autor/es:
ROMERO, CINTIA MARIANA; PERA, LICIA MARÍA; OLIVARO, CRISTINA; VAZQUEZ, ALVARO; BAIGORI, MARIO DOMINGO
Revista:
FUEL PROCESSING TECHNOLOGY
Editorial:
ELSEVIER SCIENCE BV
Referencias:
Año: 2012 vol. 98 p. 23 - 29
ISSN:
0378-3820
Resumen:
The use of biocatalysts in fuel industry is an interesting and greener alternative. In this connection, it was found that the chain-length selectivity profile of a solvent-tolerant lipase activity fromAspergillus nigerMYA 135 deter- mined in both hydrolytic and synthetic reactions depended on theway that the enzymewas prepared. Indeed, a mycelium-bound (Mb) lipase activity obtained either in presence or absence of 2% olive oil as well as a lyophi-lized supernatant extract obtained in presence of 2% olive oil showed different specificity constants (1/á). Thus, the highest substrate specificity in hydrolysis reaction was observed toward a long-chain fatty acid (C18; 1/á=1.0) with the constitutive Mb-lipase in organic medium. In addition, this lipase preparation was specific toward the synthesis of methyl palmitate during esterification (1/á=1.00) and ethyl palmitate in transesterifi-cation (1/á=0.93). Interestingly, the induced Mb-lipase was a highly reactive biocatalyst preparation in both transesterification (58% of the reactions displayed 1/á>0.5) and esterification (88% of the reactions displayed 1/á>0.7) reactions. On the contrary, the induced lyophilized supernatant was the most specific enzymatic system showing a clear preference for linoleic acid in esterification reactions (1/á around of 0.77 for all acyl acceptors tested)