Publications

• Screening, gene cloning, and characterization of orsellinic acid decarboxylase from Arthrobacter sp. K8 for regio-selective carboxylation of resorcinol derivatives.

  Kino K., Hirokawa Y., Gawasawa R., Murase R., Tsuchihashi R., Hara R.

  Toward a sustainable synthesis of value-added chemicals, the method of CO₂ utilization attracts great interest in chemical process engineering. Biotechnological CO₂ fixation is a promising technology; however, efficient methods that can fix carbon dioxide are still limited. I ... >> More

  Toward a sustainable synthesis of value-added chemicals, the method of CO₂ utilization attracts great interest in chemical process engineering. Biotechnological CO₂ fixation is a promising technology; however, efficient methods that can fix carbon dioxide are still limited. Instead, some parts of microbial decarboxylases allow the introduction of carboxy group into phenolic compounds using bicarbonate ion as a C1 building block. Here, we identified a unique decarboxylase from Arthrobacter sp. K8 that acts on resorcinol derivatives. A high-throughput colorimetric decarboxylase assay facilitated gene cloning of orsellinic acid decarboxylase from genomic DNA library of strain K8. Sequence analysis revealed that the orsellinic acid decarboxylase belonged to amidohydrolase 2 family, but shared low amino acid sequence identity with those of related decarboxylases. Enzymatic characterization unveiled that the decarboxylase introduces a carboxy group in a highly regio-selective manner. We applied the decarboxylase to enzymatic carboxylation of resorcinol derivatives. Using Escherichia coli expressing the decarboxylase gene as a whole cell biocatalyst, orsellinic acid, 2,4-dihydroxybenzoic acid, and 4-methoxysalicylic acid were produced in the presence of saturated bicarbonate. These findings could provide new insights into the production of useful phenolic acids from resorcinol derivatives. << Less

  J Biotechnol 323:128-135(2020) [PubMed] [EuropePMC]

  This publication is cited by 2 other entries.

• Studies on lichen enzymes. Purification and properties of orsellinate decarboxylase obtained from Lasallia pustulata.

  Mosbach K., Schultz J.

  Eur J Biochem 22:485-488(1971) [PubMed] [EuropePMC]