The GECCO-enzymes are offered in a stable form (lyophilized). If requested by the costumer, enzymes can also be prepared as immobilized material (entrapped in hydrogels or covalently attached to polymeric resin).

Showing 1–10 of 14 results

Alcohol dehydrogenases

Alcohol dehydrogenases currently offered are listed below. For efficient cascade reactions we are offering fusions of ADHA, TbADH and ADHMi with BVMOs. Please contact us for more details.


  1. ADHA Pyrococcus furiosus
  2. TbADH Thermoanaerobacter brockii
  3. ADHMi Mesotoga infera
  4. LbADH Lactobacillus brevis
  5. EhADH Entamoeba histolytica
  6. GtADH Geobacillus thermodenitrificans
  7. PpADH Pseudonomas putida
  8. RjADH Rhodococcus jostii

Baeyer-Villiger Monooxygenases (BVMOs)

Baeyer-Villiger monooxygenases catalyze the oxidation of carbonylic substrates to ester or lactone products using NADPH as electron donor and molecular oxygen as oxidative reactant. Using protein engineering, kinetics, microspectrophotometry, crystallography, and intermediate analogs, we have captured several snapshots along the catalytic cycle which highlight key features in enzyme catalysis. After acting as electron donor, the enzyme-bound NADP(H) forms an H-bond with the flavin cofactor. This interaction is critical for stabilizing the oxygen-activating flavin-peroxide intermediate that results from the reaction of the reduced cofactor with oxygen. An essential active-site arginine acts as anchoring element for proper binding of the ketone substrate. Its positively charged guanidinium group can enhance the propensity of the substrate to undergo a nucleophilic attack by the flavin-peroxide intermediate. Furthermore, the arginine side chain, together with the NADP(+) ribose group, forms the niche that hosts the negatively charged Criegee intermediate that is generated upon reaction of the substrate with the flavin-peroxide. The fascinating ability of Baeyer-Villiger monooxygenases to catalyze a complex multistep catalytic reaction originates from concerted action of this Arg-NADP(H) pair and the flavin subsequently to promote flavin reduction, oxygen activation, tetrahedral intermediate formation, and product synthesis and release. The emerging picture is that these enzymes are mainly oxygen-activating and “Criegee-stabilizing” catalysts that act on any chemically suitable substrate that can diffuse into the active site, emphasizing their potential value as toolboxes for biocatalytic applications.

Our collection of BVMOs contains enzymes listed below. Please note that list is currently being updated as our collection has been expanded recently with new enzymes, but also with new mutants with promising characteristics. For certain enzymes we have libraries which can be screened for specific target compounds.

  1. PAMO
  2. PAMO M446G
  3. PAMO P440N
  4. PAMO P440L
  5. PAMO ΔS441ΔA442
  6. PAMO L443F
  7. PAMO A442G
  8. PAMO I67T
  9. CPDMO
  10. CRE2-PAMO-STMO chimera
  11. CRE2-PAMO-CHMO chimera
  12. CRE2-PAMO-STMO-PAMO chimera
  13. CRE2-PAMO-Met1 chimera
  14. CRE2-CPMO F156L
  15. BVMO1 Rhodococcus jostii
  16. BVMO4 Rhodococcus jostii
  17. BVMO6 Rhodococcus jostii
  18. BVMO9 Rhodococcus jostii
  19. BVMO10 Rhodococcus jostii
  20. BVMO11 Rhodococcus jostii
  21. BVMO14 Rhodococcus jostii
  22. BVMO15 Rhodococcus jostii
  23. BVMO20 Rhodococcus jostii
  24. BVMO21 Rhodococcus jostii
  25. BVMO24 Rhodococcus jostii
  26. CRE2-BVMO2 Rhodococcus jostii
  27. CRE2-BVMO3 Rhodococcus jostii
  28. CRE2-BVMO5 Rhodococcus jostii
  29. CRE2-BVMO7 Rhodococcus jostii
  30. CRE2-BVMO8 Rhodococcus jostii
  31. CRE2-BVMO12 Rhodococcus jostii
  32. CRE2-BVMO13 Rhodococcus jostii
  33. CRE2-BVMO16 Rhodococcus jostii
  34. CRE2-BVMO17 Rhodococcus jostii
  35. CRE2-BVMO18 Rhodococcus jostii
  36. CRE2-BVMO19 Rhodococcus jostii
  37. CRE2-BVMO Aspergillus fumigatus (Af2 fusion)
  38. CRE2-PAMO
  39. CRE2-CHMO Acinetobacter sp.
  40. CRE2-CPMO
  41. CRE2-HAPMO
  42. CRE2-EtaA
  43. CRE2-PAMO M446G
  44. CRE2-CPDMO
  45. CRE2-STMO
  46. CRE2-CHMO A255C-A293C (R2)
  47. CRE2-CHMO A325C-L483C (R3)
  48. CRE2-CHMO L323C-A325C (RV6)
  49. CRE2-BVMO Trichodesmium erythraeum (putative)
  50. CRE2-CHMO Rhodococcus HI-31
  51. CRE2-AcMO Gordonia sp.
  52. CRE2-AlmA Acinetobacter sp.
  53. CRE2-CHMO Brachymonas petroleovorans
  54. CRE2-MekA
  55. CRE2-CHMO Xanthobacter flavus
  56. CRE2-BVMO Haloterrigena turkmenica (putative)
  57. CRE2-TmCHMO
  58. CRE2-PockeMO
  59. CRE2-BVMO Parvi
  60. CRE2-OTEMO
  61. CRE2-BVMO Ocean


The thermostable catalase from Thermobifida fusca (TfuCat) can be used in biotechnological processes for the removal of hydrogen peroxide.

Except for catalyzing the dismutation of hydrogen peroxide, TfuCat was also found to catalyze oxidations of phenolic compounds.

more info: doi:10.1007/s00253-014-6060-5.

Cofactor-recycling enzymes

We are offering an array of cofactor-recycling enzymes for regeneration of NADH, NAPDH and deazaflavin (F0 and F420) cofactors.


Page is under construction. We are offering various thermostable and engineered dehalogenases.

Please make an inquiry.

Drug metabolism studies

We are offering various enzymes of high importance for pharmaceutical reasearch:

  1. Human monoamine oxidase (MAO)
  2. Human flavin-containing monooxygenase (FMO5)
  3. Mammalian alkyldihydroxyacetonephosphate synthase (ADPS)

Please make an inquiry.

Dye-decolorizing peroxidases (DyPs)

As alternatives for the plant and animal peroxidases, the newly discovered DyP-type peroxidases (DyPs) may offer advantages. Except for facilitating the production of peroxidases and eliminating the existence of isoforms, the ability to produce DyPs in a recombinant form also allows engineering of these biocatalysts. The first DyPs were identified less than two decades ago. DyPs are unrelated in sequence and structure to known peroxidases belonging to the plant or animal peroxidase superfamilies. DyPs are typically identified by their activity on anthraquinone dyes. While DyPs are efficient in degrading these synthetic dyes, the physiological substrates for DyPs are unclear and therefore their role in nature is enigmatic. Interestingly, recent studies suggest that bacterial DyPs may play an important role in the degradation of lignin which suggests that DyPs represent the bacterial counterparts of the fungal lignin peroxidases. Except for establishing their activity on synthetic dyes and possible role in lignin degradation, little data is available concerning their biocatalytic potential.

  1. TfuDyP Thermobifida fusca DyP
  2. SviDyP Saccharomonospora viridis DyP
  3. YfeX Escherichia coli DyP
  4. PfDyP Pseudomonas fluorescens DyP

We are also offering purified basic and acidic isoforms of horseradish peroxidase (HRP).

Epoxide hydrolases

Page is under construction. We are offering various thermostable and engineered epoxide hydrolases.

Please make an inquiry.

Flavin-containing monooxygenases (FMOs)

Flavin-containing monooxygenases are known for their broad substrate specificity and their ability to perform oxygenations of e.g. amines and sulfides. Some bacterial FMOs were shown to perform hydroxylation of indoles (MeFMO) while the human FMO5 was recently shown to be able to perform various Baeyer-Villiger oxidations. Below some of the GECCO FMOs are highlighted, while we also can offer other microbial FMOs.

  1. MeFMO – Methylophaga aminisulfidivorans flavin-containing monooxygenase, available in two formats: (1) recombinant MeFMO and (2) recombinant MeFMO fused to a cofactor recycling dehydrogenase (Org Biomol Chem. 2011 Mar 7;9(5):1337-41. doi: 10.1039/c0ob00988a)
  2. Rhodococcus jostii RHA1 flavin-containing monooxygenases: eight different FMOs belonging to class B monooxygenases (J Mol Cat B Enz 88, 2013, 20–25)
  3. Human FMO5 (ACS Chem Biol. 2016, 11(4):1039-48)


Bacterial laccases have proven advantages over fungal and plant counterparts regarding wider pH optimum, higher stability and broader biocatalytic scope. We are offering Bacillus licheniformis ATCC 9945a laccase which exhibits remarkable thermostability and resitance to inactivation by organic solvents (