High performing immobilized Baeyer-Villiger monooxygenase and glucose dehydrogenase for the synthesis of ε-caprolactone derivative

Marie Delgove, Daniela Valencia, Jordi Solé, Katrien Bernaerts, Stefaan de Wildeman, Marina Guillén, Gregorio Álvaro

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

The industrial application of Baeyer-Villiger monooxygenases (BVMOs) is typically hindered by stability and cofactor regeneration considerations. The stability of biocatalysts can be improved by immobilization. The goal of this study was to evaluate the (co)-immobilization of a thermostable cyclohexanone monooxygenase from Thermocrispum municipale (TmCHMO) with a glucose dehydrogenase (GDH) from Thermoplasma acidophilum for NADPH cofactor regeneration.

Both enzymes were immobilized on an amino-functionalized agarose-based support (MANA-agarose). They were applied to the oxidation of 3,3,5-trimethylcyclohexanone for the synthesis of ε-caprolactone derivatives which are precursors of polyesters. The performances of the immobilized biocatalysts were evaluated in reutilization reactions with as many as 15 cycles and compared to the corresponding soluble enzymes. Co-immobilization proved to provide the most efficient biocatalyst with an average conversion of 83% over 15 reutilization cycles leading to a 50-fold increase of the biocatalyst yield compared to the use of soluble enzymes which were applied in a fed-batch strategy.

TmCHMO was immobilized for the first time in this work, with very good retention of the activity throughout reutilization cycles. This immobilized biocatalyst contributes to the application of BVMOs in up-scaled biooxidation processes.
Original languageEnglish
Pages (from-to)134-141
Number of pages8
JournalApplied Catalysis A-General
Volume572
DOIs
Publication statusPublished - 25 Feb 2019

Keywords

  • BIOCATALYST
  • Baeyer-Villiger monooxygenase
  • Biocatalyst immobilization
  • CYCLOHEXANONE MONOOXYGENASE
  • Cofactor recycling
  • DISCOVERY
  • ENTRY
  • ESCHERICHIA-COLI
  • Glucose dehydrogenase
  • Lactone monomer
  • OXIDATION
  • POLYESTERS
  • SCALE

Cite this

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title = "High performing immobilized Baeyer-Villiger monooxygenase and glucose dehydrogenase for the synthesis of ε-caprolactone derivative",
abstract = "The industrial application of Baeyer-Villiger monooxygenases (BVMOs) is typically hindered by stability and cofactor regeneration considerations. The stability of biocatalysts can be improved by immobilization. The goal of this study was to evaluate the (co)-immobilization of a thermostable cyclohexanone monooxygenase from Thermocrispum municipale (TmCHMO) with a glucose dehydrogenase (GDH) from Thermoplasma acidophilum for NADPH cofactor regeneration.Both enzymes were immobilized on an amino-functionalized agarose-based support (MANA-agarose). They were applied to the oxidation of 3,3,5-trimethylcyclohexanone for the synthesis of ε-caprolactone derivatives which are precursors of polyesters. The performances of the immobilized biocatalysts were evaluated in reutilization reactions with as many as 15 cycles and compared to the corresponding soluble enzymes. Co-immobilization proved to provide the most efficient biocatalyst with an average conversion of 83{\%} over 15 reutilization cycles leading to a 50-fold increase of the biocatalyst yield compared to the use of soluble enzymes which were applied in a fed-batch strategy.TmCHMO was immobilized for the first time in this work, with very good retention of the activity throughout reutilization cycles. This immobilized biocatalyst contributes to the application of BVMOs in up-scaled biooxidation processes.",
keywords = "BIOCATALYST, Baeyer-Villiger monooxygenase, Biocatalyst immobilization, CYCLOHEXANONE MONOOXYGENASE, Cofactor recycling, DISCOVERY, ENTRY, ESCHERICHIA-COLI, Glucose dehydrogenase, Lactone monomer, OXIDATION, POLYESTERS, SCALE",
author = "Marie Delgove and Daniela Valencia and Jordi Sol{\'e} and Katrien Bernaerts and {de Wildeman}, Stefaan and Marina Guill{\'e}n and Gregorio {\'A}lvaro",
year = "2019",
month = "2",
day = "25",
doi = "10.1016/j.apcata.2018.12.036",
language = "English",
volume = "572",
pages = "134--141",
journal = "Applied Catalysis A-General",
issn = "0926-860X",
publisher = "Elsevier",

}

High performing immobilized Baeyer-Villiger monooxygenase and glucose dehydrogenase for the synthesis of ε-caprolactone derivative. / Delgove, Marie; Valencia, Daniela; Solé, Jordi; Bernaerts, Katrien; de Wildeman, Stefaan; Guillén, Marina; Álvaro, Gregorio.

In: Applied Catalysis A-General, Vol. 572, 25.02.2019, p. 134-141.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - High performing immobilized Baeyer-Villiger monooxygenase and glucose dehydrogenase for the synthesis of ε-caprolactone derivative

AU - Delgove, Marie

AU - Valencia, Daniela

AU - Solé, Jordi

AU - Bernaerts, Katrien

AU - de Wildeman, Stefaan

AU - Guillén, Marina

AU - Álvaro, Gregorio

PY - 2019/2/25

Y1 - 2019/2/25

N2 - The industrial application of Baeyer-Villiger monooxygenases (BVMOs) is typically hindered by stability and cofactor regeneration considerations. The stability of biocatalysts can be improved by immobilization. The goal of this study was to evaluate the (co)-immobilization of a thermostable cyclohexanone monooxygenase from Thermocrispum municipale (TmCHMO) with a glucose dehydrogenase (GDH) from Thermoplasma acidophilum for NADPH cofactor regeneration.Both enzymes were immobilized on an amino-functionalized agarose-based support (MANA-agarose). They were applied to the oxidation of 3,3,5-trimethylcyclohexanone for the synthesis of ε-caprolactone derivatives which are precursors of polyesters. The performances of the immobilized biocatalysts were evaluated in reutilization reactions with as many as 15 cycles and compared to the corresponding soluble enzymes. Co-immobilization proved to provide the most efficient biocatalyst with an average conversion of 83% over 15 reutilization cycles leading to a 50-fold increase of the biocatalyst yield compared to the use of soluble enzymes which were applied in a fed-batch strategy.TmCHMO was immobilized for the first time in this work, with very good retention of the activity throughout reutilization cycles. This immobilized biocatalyst contributes to the application of BVMOs in up-scaled biooxidation processes.

AB - The industrial application of Baeyer-Villiger monooxygenases (BVMOs) is typically hindered by stability and cofactor regeneration considerations. The stability of biocatalysts can be improved by immobilization. The goal of this study was to evaluate the (co)-immobilization of a thermostable cyclohexanone monooxygenase from Thermocrispum municipale (TmCHMO) with a glucose dehydrogenase (GDH) from Thermoplasma acidophilum for NADPH cofactor regeneration.Both enzymes were immobilized on an amino-functionalized agarose-based support (MANA-agarose). They were applied to the oxidation of 3,3,5-trimethylcyclohexanone for the synthesis of ε-caprolactone derivatives which are precursors of polyesters. The performances of the immobilized biocatalysts were evaluated in reutilization reactions with as many as 15 cycles and compared to the corresponding soluble enzymes. Co-immobilization proved to provide the most efficient biocatalyst with an average conversion of 83% over 15 reutilization cycles leading to a 50-fold increase of the biocatalyst yield compared to the use of soluble enzymes which were applied in a fed-batch strategy.TmCHMO was immobilized for the first time in this work, with very good retention of the activity throughout reutilization cycles. This immobilized biocatalyst contributes to the application of BVMOs in up-scaled biooxidation processes.

KW - BIOCATALYST

KW - Baeyer-Villiger monooxygenase

KW - Biocatalyst immobilization

KW - CYCLOHEXANONE MONOOXYGENASE

KW - Cofactor recycling

KW - DISCOVERY

KW - ENTRY

KW - ESCHERICHIA-COLI

KW - Glucose dehydrogenase

KW - Lactone monomer

KW - OXIDATION

KW - POLYESTERS

KW - SCALE

U2 - 10.1016/j.apcata.2018.12.036

DO - 10.1016/j.apcata.2018.12.036

M3 - Article

VL - 572

SP - 134

EP - 141

JO - Applied Catalysis A-General

JF - Applied Catalysis A-General

SN - 0926-860X

ER -