INVESTIGADORES
ROMERO Cintia Mariana
congresos y reuniones científicas
Título:
Transesterification activity of a mycelium-bound lipase from Aspergillus niger MYA 135.
Autor/es:
ROMERO C.M., PERA L.M., BAIGORÍ M.D
Lugar:
Rosario. Santa Fe
Reunión:
Congreso; SAIB. 42 Annual Meeting. Argentina; 2006
Institución organizadora:
SAIB
Resumen:
EN-C02
TRANSESTERIFICATION ACTIVITY OF A MYCELIUMBOUND
LIPASE FROM Aspergillus niger MYA 135
Romero CM; Pera LM; Baigorí M
PROIMI-CONICET Av. Belgrano y Pje. Caseros, 4000 Tucumán.
Tel: 0381-4344888
E-mail: Baigori@hotmail.com
Introduction: Lipases (EC 3.1.1.3) can be used for the synthesis
of esters by transesterification with acyl donors in organic
solvents. These enzymes have moved far from their original
application to the biotechnological processing of fat and other
lipids. Transesterification is especially useful for the preparation
of optically active compounds, which are formed by resolution or
asymmetrization of racemic or prochiral suitable substrate. The
aim of this work was to determine the transesterification activity
of a mycelium-bound lipase from Aspergillus niger MYA 135.
Methods: Enzymatic transesterifications were performed in nhexano
using p-nitrophenyl palmitate and the assayed alcohol as
substrates. Mycelium-bound lipase was directly used as a source
of lipase. The released p-nitrophenol was extracted with Na2CO3
before measurement at 405 nm. Reaction mixtures without the
assayed alcohol were used as a hydrolysis control. Qualitative
analyses of alkylpalmitates were done by thin layer
chromatography using chloroform as developing solvent. Result
and Conclusion: Under our experimental conditions methyl, ethyl,
propyl, buthyl, hexyl and hepthyl palmitate were synthesized. The
higher specific transesterification activity (mU per g of dry weight)
was observed in presence of hexanol (60.8 ± 1.2 mU/g). This
work was supported by grants PICTO 761 and PIP 6062.
