Biotransformations catalyzed by lipases from spore-forming microorganisms

ABDULHAMID MB, COSTAS L, BAIGORI M, CASTRO GR, PERA LM

Puerto Madryn - Chubut

Congreso; XLVI Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; 2010

SAIB

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