PROIMI   05436
PLANTA PILOTO DE PROCESOS INDUSTRIALES MICROBIOLOGICOS
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
BIOTRANSFORMATIONS CATALYZED BY LIPASES FROM SPORE-FORMING MICROORGANISMS
Autor/es:
ABDULHAMID MB; COSTAS LUCIANA; BAIGORÍ MARIO; CASTRO G.R; PERA L.M
Lugar:
Puerto Madryn
Reunión:
Congreso; 46 Annual Meeting Argentine Society for Biochemistry and Molecular Biology (SAIB); 2010
Institución organizadora:
SAIB
Resumen:
It is generally accepted that lipase-catalyzed hydrolytic activity does
not always correlate with its esterification or transesterification
activity. Therefore, the selection of a proper lipase for a given
application is required. Thus, the aim of this study was to investigate
the reactivity of 64 lipases from spore-forming microorganisms
towards hydrolytic and transesterification reactions by using pnitrophenyl
palmitate as a chromogenic acyl donor substrate.
Specific hydrolytic activities were not highly correlated with the
corresponding specific transesterification activities using ethanol
(r=-0.113, P=0.375), starch (r=0.226, P=0.073), low-methoxyl
(LM) pectin (r=0.622, P<0.001) and high-methoxyl (HM) pectin
(r=0.533, P<0.001) as acyl acceptor. The highest specific hydrolytic
activity (52.73±1.68 U/mg) was exhibited by lipase from strain 5.
Lipases from strains 30, 47 M, 5 and Brevibacillus agri E12 gave the
highest transesterification activities in the presence of ethanol
(26.36±2.55 U/mg), starch (0.31±0.04 U/mg), LM pectin
(1.25±0.22 U/mg) and HM pectin (3.12±0.56 U/mg), respectively.
Under our assay conditions, no hydrolytic activity was detected with
lipase from strain 30.
highest transesterification activities in the presence of ethanol
(26.36±2.55 U/mg), starch (0.31±0.04 U/mg), LM pectin
(1.25±0.22 U/mg) and HM pectin (3.12±0.56 U/mg), respectively.
Under our assay conditions, no hydrolytic activity was detected with
lipase from strain 30.
Brevibacillus agri E12 gave the
highest transesterification activities in the presence of ethanol
(26.36±2.55 U/mg), starch (0.31±0.04 U/mg), LM pectin
(1.25±0.22 U/mg) and HM pectin (3.12±0.56 U/mg), respectively.
Under our assay conditions, no hydrolytic activity was detected with
lipase from strain 30.
This work was supported by grants PIP-CONICET 297 and CIUNT
26/D409