Methanol is often employed in biocatalysis with the purpose of increasing substrates solubility or as the acyl acceptor in transesterification reactions, but inhibitory effects are observed in several cases. We have studied the influence of methanol on the catalytic activity and on the conformation of the lipase from Burkholderia glumae, which is reported to be highly methanol tolerant if compared with other lipases. We detected highest activity in the presence of 50-70 % methanol. Under these conditions, however, the enzyme stability is perturbed, leading to gradual protein unfolding and finally to aggregation. These results surmise that, for this lipase, methanol-induced deactivation does not depend on inhibition of catalytic activity but rather on negative effects on the conformational stability of the catalyst. © 2013 Springer-Verlag Berlin Heidelberg.
Santambrogio, C., Sasso, F., Natalello, A., Brocca, S., Grandori, R., Doglia, S., et al. (2013). Effects of methanol on a methanol-tolerant bacterial lipase. APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 97(19), 8609-8618 [10.1007/s00253-013-4712-5].
Effects of methanol on a methanol-tolerant bacterial lipase
SANTAMBROGIO, CARLO;SASSO, FRANCESCO;NATALELLO, ANTONINO;BROCCA, STEFANIA;GRANDORI, RITA;DOGLIA, SILVIA MARIA;LOTTI, MARINA
2013
Abstract
Methanol is often employed in biocatalysis with the purpose of increasing substrates solubility or as the acyl acceptor in transesterification reactions, but inhibitory effects are observed in several cases. We have studied the influence of methanol on the catalytic activity and on the conformation of the lipase from Burkholderia glumae, which is reported to be highly methanol tolerant if compared with other lipases. We detected highest activity in the presence of 50-70 % methanol. Under these conditions, however, the enzyme stability is perturbed, leading to gradual protein unfolding and finally to aggregation. These results surmise that, for this lipase, methanol-induced deactivation does not depend on inhibition of catalytic activity but rather on negative effects on the conformational stability of the catalyst. © 2013 Springer-Verlag Berlin Heidelberg.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.