INVESTIGADORES
PERA Licia Maria
artículos
Título:
Specific enzyme-catalyzed hydrolysis and synthesis in aqueous and organic medium using biocatalysts with lipase activity from Aspergillus niger MYA 135
Autor/es:
ROMERO, CINTIA MARIANA; PERA, LICIA MARÍA; LOTO, FLAVIA; BAIGORI, MARIO DOMINGO
Revista:
CATALYSIS LETTERS
Editorial:
SPRINGER
Referencias:
Lugar: Berlin; Año: 2012 p. 25 - 31
ISSN:
1011-372X
Resumen:
In the present study, the specific hydrolytic activity of three biocatalysts such as the constitutive mycelium-bound lipase, the induced mycelium-bound lipase and the lyophilized induced supernatant from A. niger MYA 135 was evaluated in both aqueous and organic media. A direct correlation between activity in water and n-hexane was not observed for the same hydrolytic reaction. The n-hexane/water activity ratio (RO/A) was applied to characterize the activity in organic mediun. The three biocatalysts showed RO/A values higher than 1 for hydrolysis of long-chain fatty acid esters, demonstrating a higher specific hydrolytic activity in organic solvent than in water. A different behavior was observed during hydrolysis of middle-chain fatty acid esters, which was higher in aqueous medium (RO/A ˂1). Transesterifications of different alcohols with various p-nitrophenyl derivatives using all three biocatalysts preparations were also evaluated in n-hexane. For methanolysis and ethanolysis, the constitutive mycelium-bound lipase displayed an interesting preference for C16 substrate (p-nitrophenyl palmitate). The induced mycelium-bound lipase showed high specific transesterification activities in the presence of water-miscible alcohols and middle-chain fatty acid esters (p-nitrophenyl caprate and p-nitrophenyl laurate), being the highest specific transesterification activity (91.4 ± 1.7 mU/gdw) observed in a reaction mixture containing propanol and p- nitrophenyl laurate. Finally, both p-nitrophenyl caprate (C10) and p-nitrophenyl laurate (C12) were preferentially methanolized by the lyophilized induced supernatant, being this lipase activity the most specific biocatalyst preparation under transesterification conditions. A selectivity-based analysis of each lipase preparation toward transesterificaton or hydrolysis in organic medium was evaluated as well.