Whole cells of recombinant CYP153A6-E. coli as biocatalyst for regioselective hydroxylation of monoterpenes

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Cannazza, Pietro ; Rabuffetti, Marco ; Donzella, Silvia ; De Vitis, Valerio ; Contente, Martina L. ; de Oliveira, Maria da Conceicao Ferreira ; de Mattos, Marcos C. ; Barbosa, Francisco G. ; de Souza Oliveira, Ricardo Pinheiro ; Pinto, Andrea ; Molinari, Francesco ; Romano, Diego

• Tipo de documento: Artigo Científico
• Fonte: AMB EXPRESS; v. 12, n. 1, p. 9-pg., 2022-04-27.

Resumo

Optimized recombinant whole cells of E. coli bearing CYP153A6 were employed for catalyzing the hydroxylation of different monoterpene derivatives. In most cases, high selectivity was observed with exclusive hydroxylation of the allylic methyl group bound to the aliphatic ring. In the case of (R)- and (S)-carvone, hydroxylation occurred also on the other allylic methyl group, although to a lesser extent. Biotransformations carried out in fed-batch mode on (S)-limonene and alpha-terpineol showed that recombinant whole cells retained activity for at least 24 h, allowing for the recovery of 3.25 mg mL(-1) of (S)-perillyl alcohol and 5.45 mg mL(-1) of 7-hydroxy-alpha-terpineol, respectively. Keypoints Different monoterpenes can be regioselectively hydroxylated by CYP153A6 monooxygenase The biotransformation with whole cells is complementary to chemical oxyfunctionalization Fed-batch biotransformations have been applied for preparative purposes (AU)

• Processo FAPESP: 19/16743-9 - Processo de internacionalização em pesquisa biotecnológica entre as Universidades de São Paulo e Milão
• Beneficiário: Ricardo Pinheiro de Souza Oliveira
• Modalidade de apoio: Auxílio à Pesquisa - Pesquisador Visitante - Internacional