Tailoring chain length selectivity of a solvent-tolerant lipase activity from Aspergillus niger MYA 135 by submerged fermentation

CINTIA M. ROMERO, LICIA M. PERA, CRISTINA OLIVARO, ALVARO VAZQUEZ, MARIO D. BAIGORI

FUEL PROCESSING TECHNOLOGY

ELSEVIER SCIENCE BV

Año: 2012 vol. 98 p. 23 - 29

0378-3820

The use of biocatalysts in fuel industry is an interesting and greener alternative. In this connection, it was found 22 that the chain-length selectivity profile of a solvent-tolerant lipase activity fromAspergillus nigerMYA 135 deter- 23 mined in both hydrolytic and synthetic reactions depended on theway that the enzymewas prepared. Indeed, a 24 mycelium-bound (Mb) lipase activity obtained either in presence or absence of 2% olive oil as well as a lyophi- 25 lized supernatant extract obtained in presence of 2% olive oil showed different specificity constants (1/α). 26 Thus, the highest substrate specificity in hydrolysis reaction was observed toward a long-chain fatty acid (C18; 27 1/α=1.0) with the constitutive Mb-lipase in organic medium. In addition, this lipase preparation was specific 28 toward the synthesis of methyl palmitate during esterification (1/α=1.00) and ethyl palmitate in transesterifi- 29 cation (1/α=0.93). Interestingly, the induced Mb-lipase was a highly reactive biocatalyst preparation in both 30 transesterification (58% of the reactions displayed 1/α>0.5) and esterification (88% of the reactions displayed 31 1/α>0.7) reactions. On the contrary, the induced lyophilized supernatant was the most specific enzymatic 32 system showing a clear preference for linoleic acid in esterification reactions (1/α around of 0.77 for all acyl 33 acceptors tested)