Catalytic and molecular properties of alkaliphilic and thermotolerant β-etherase from Altererythrobacter sp. B11

Abstract

ABSTRACT Phenylpropanone monomers, including guaiacyl hydroxypropanone, are important precursors for the synthesis of various chemicals. The monomers are obtained in a three-step cascade reaction catalyzed by a group of enzymes in the β-etherase system that cleaves the β-O-4 bond, the major bond in lignin. In this study, one of the β-etherase of the glutathione-S-transferase superfamily, AbLigF2, was discovered in genus Altererythrobacter, and the recombinant etherase was characterized. The enzyme showed maximal activity at 45 °C, maintained 30% of its activity after 2 h at 50 °C, and was the most thermostable among the previously reported enzymes. Moreover, N13, S14, and S115, located near the thiol group of glutathione, had a significant effect on the maximum reaction rate of enzyme activity. This study suggests that AbLigF2 has the potential to serve as a thermostable enzyme for lignin utilization and provides insights into its catalytic mechanism.