Skip to main content
SpringerLink
Log in

Different strategies for multi-enzyme cascade reaction for chiral vic-1,2-diol production

  • Research Paper
  • Published:
Bioprocess and Biosystems Engineering Aims and scope Submit manuscript

Abstract

The stereoselective three-enzyme cascade for the one-pot synthesis of (1S,2S)-1-phenylpropane-1,2-diol ((1S,2S)-1-PPD) from inexpensive starting substrates, benzaldehyde and acetaldehyde, was explored. By coupling stereoselective carboligation catalyzed by benzoylformate decarboxylase (BFD), L-selective reduction of a carbonyl group with alcohol dehydrogenase from Lactobacillus brevis (ADHLb) as well as the coenzyme regeneration by formate dehydrogenase (FDH), enantiomerically pure diastereoselective 1,2-diol was produced. Two different multi-enzyme system approaches were applied: the sequential two-step one-pot and the simultaneous one-pot cascade. All enzymes were kinetically characterized. The impact of acetaldehyde on the BFD and ADHLb stability was investigated. To overcome the kinetic limitation of acetaldehyde in the carboligation reaction and to reduce its influence on the enzyme stability, experiments were performed in two different excesses of acetaldehyde (100 and 300%). Due to the ADHLb deactivation by acetaldehyde, the simultaneous one-pot cascade proved not to be the first choice for the investigated three-enzyme system. In the sequential cascade with 300% acetaldehyde excess a 100% yield of vic 1,2-diol was reached.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5
Fig. 6
Fig. 7

Similar content being viewed by others

References

  1. Ricca E, Brucher B, Schrittwieser JH (2011) Multi-enzymatic cascade reactions: overview and perspectives. Adv Synth Catal 353:2239–2262

    Article  CAS  Google Scholar 

  2. Enoki J, Meisborn J, Müller AC, Kourist R (2016) A multi-enzymatic cascade reaction for the stereoselective production of γ-oxyfunctionalyzed amino acids. Front Microbiol 7:425

    Article  PubMed  PubMed Central  Google Scholar 

  3. Monti D, Ferrandi EE, Zanellato I, Hua L, Polentini F, Carrea G, Riva S (2009) One-pot multienzymatic synthesis of 12-ketoursodeoxycholic acid: subtle cofactor specificities rule the reaction equilibria of five biocatalysts working in a row. Adv Synth Catal 351:1303–1311

    Article  CAS  Google Scholar 

  4. Burton SG, le Roes-Hill M (2008) In: Garcia-Junceda E (ed) Multi-step enzyme catalysis—biotransformations and chemoenzymatic synthesis. Wiley, Weinheim

    Google Scholar 

  5. Fischer T, Pietruszka J (2010) Key building blocks via enzyme-mediated synthesis. Top Curr Chem 297:1–43

    Article  CAS  PubMed  Google Scholar 

  6. Hailes HC, Dalby PA, Woodley JM (2007) Integration of biocatalytic conversions into chemical syntheses. J Chem Technol Biotechnol 82:1063–1066

    Article  CAS  Google Scholar 

  7. Xue R, Woodley JM (2012) Process technology for multi-enzymatic reaction systems. Bioresour Technol 115:183–195

    Article  CAS  PubMed  Google Scholar 

  8. Rios-Solisa L, Morrisa P, Granta C, Odeleyea AO, Hailesb HC, Warda JM, Dalbya PA, Baganza F, Lyea GJ (2015) Modelling and optimisation of the one-pot, multi-enzymatic synthesis of chiral amino-alcohols based on microscale kinetic parameter determination. Chem Eng Sci 122:360–372

    Article  CAS  Google Scholar 

  9. Hall M, Bommarius AS (2011) Enantioenriched compounds via enzyme-catalyzed redox reactions. Chem Rev 111:4088–4110

    Article  CAS  PubMed  Google Scholar 

  10. Lavandera I, Kern A, Ferreira-Silva B, Glieder A, de Wildeman S, Kroutil W (2008) Stereoselective bioreduction of bulky-bulky ketones by a novel ADH from Ralstonia sp. J Org Chem 73:6003–6005

    Article  CAS  PubMed  Google Scholar 

  11. Patel RN (2008) Synthesis of chiral pharmaceutical intermediates by biocatalysis. Coord Chem Rev 252:659–701

    Article  CAS  Google Scholar 

  12. Choudary BM, Chowdari NS, Madhi S, Kantam ML (2003) A trifunctional catalyst for one-pot synthesis of chiral diols via heck coupling—n-oxidation—asymmetric dihydroxylation: application for the synthesis of diltiazem and taxol side chain. J Org Chem 68:1736–1746

    Article  CAS  PubMed  Google Scholar 

  13. Goldberg K, Schroer K, Lütz S (2007) Biocatalytic ketone reduction–a powerful tool for the production of chiral alcohols-part II: whole-cell reductions. Appl Microbiol Biotechnol 76:237–255

    Article  CAS  PubMed  Google Scholar 

  14. Kulig J, Simon R, Rose C, Husain S, Häckh M, Lüdke S, Zeitler K, Kroutil W, Pohl M, Rother D (2012) Stereoselective synthesis of bulky 1,2-diols with alcohol dehydrogenases. Catal Sci Technol 2:1580–1589

    Article  CAS  Google Scholar 

  15. Kihumbu D, Stillger T, Hummel W, Liese A (2002) Enzymatic synthesis of all stereoisomers of 1-phenylpropane-1,2-diol. Tetrahedron: Asymmetry 13:1069–1072

    Article  CAS  Google Scholar 

  16. Shanmuganathan S, Natalia D, Greiner L, Dominguez de Maria P (2012) Oxidation-hydroxymethylation-reduction: a one-pot three-step biocatalytic synthesis of optically active a-aryl vicinal diols. Green Chem 14:94–97

    Article  CAS  Google Scholar 

  17. Švarc A, Valinger D, Vasić-Rački Đ, Presečki AV (2015) Stereoselective synthesis of phenylpropane 1,2-diols from (S)-2-hydroxypropiophenone by NADH-dependent oxidoreductases. Biochem Eng J 103:250–255

    Article  CAS  Google Scholar 

  18. Jakoblinnert A, Rother D (2014) A two-step biocatalytic cascade in micro-aqueous medium: using whole cells to obtain high concentrations of a vicinal diol. Green Chem 16:3472–3482

    Article  CAS  Google Scholar 

  19. Bencze LC, Paizs C, Tosa ML, Dan Irimie F, Retey J (2011) Chemoenzymatic one-pot synthesis of both (R)-and (S)-aryl-1,2-ethanediols. ChemCatChem 3:343–346

    Article  CAS  Google Scholar 

  20. Kamal A, Sandbhor M, Ahmed K, Adil SF, Ali Shaik A (2013) Chemoenzymatic synthesis of enantiomerically pure terminal 1,2-diols. Tetrahedron: Asymmetry 14:3861–3866

    Article  CAS  Google Scholar 

  21. Iding H, Dünnwald T, Greiner L, Liese A, Müller M (2000) Benzoylformate decarboxylase from Pseudomonas putida as stable catalyst for the synthesis of chiral 2-hydroxy ketones. Chem Eur J 6:1483–1495

    Article  CAS  PubMed  Google Scholar 

  22. Peper S, Kara S, Long WS, Liese A, Niemeyer B (2011) Immobilization and characterization of benzoylformate decarboxylase from Pseudomonas putida on spherical silica carrier. Bioprocess Biosyst Eng 34:671–680

    Article  CAS  PubMed  Google Scholar 

  23. Aymard C, Belarbi A (2000) Kinetics of thermal deactivation of enzymes: a simple three parameters phenomenological model can describe the decay of enzyme activity, irrespectively of the mechanism. Enzym Microb Technol 27:612–618

    Article  CAS  Google Scholar 

  24. Polakovič M, Bryjak J (2002) Modelling of the kinetics of thermal inactivation of glucoamylase from Aspergillus niger. J Mol Catal B: Enzym 19–20:443–450

    Article  Google Scholar 

  25. Kara S, Long WS, Berheide M, Peper S, Niemeyer B, Liese A (2011) Influence of reaction conditions on the enantioselectivity of biocatalyzed C–C bond formations under high pressure conditions. J Biotechnol 152:87–92

    Article  CAS  PubMed  Google Scholar 

  26. Kuznetsova IM, Turoverov KK, Uversky VN (2014) What macromolecular crowding can do to a protein. Int J Mol Sci 15:23090–23140

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  27. Hollmann F, Arends IW, Holtmann D (2011) Enzymatic reductions for the chemist. Green Chem 13:2285–2314

    Article  CAS  Google Scholar 

  28. Dominguez de Maria P, Stillger T, Pohl M, Kiesel M, Liese A, Groger H, Trauthwein H (2008) Enantioselective C–C bond ligation using recombinant Escherichia coli-whole-cell biocatalysts. Adv Synth Catal 350:165–173

    Article  CAS  Google Scholar 

  29. Jakoblinnert A, Mladenov R, Paul A, Sibilla F, Schwaneberg U, Ansorge-Schumacher MB, Dominguez de Maria P (2011) Asymmetric reduction of ketones with recombinant E. coli whole cells in neat substrates. Chem Commun 47:12230–12232

    Article  CAS  Google Scholar 

Download references

Acknowledgements

This work was supported by University of Zagreb short-term financial scientific research support under the title “Mathematical modeling of the biocatalytic synthesis of industrially interesting products”. The authors would like to thank Prof. Martina Pohl from the Institute of Bio- and Geosciences, IBG-1: Biotechnology, Research center Jülich, Germany for the gift of alcohol dehydrogenase from Lactobacillus brevis and Davor Valinger from Faculty of Food Technology and Biotechnology, University of Zagreb for the isolation of enzyme benzoylformate decarboxylase.

Author information

Authors and Affiliations

  1. Faculty of Chemical Engineering and Technology, University of Zagreb, Savska cesta 16, 10000, Zagreb, Croatia

    Ana Vrsalović Presečki, Anera Švarc & Đurđa Vasić-Rački

  2. Faculty of Textile Technology, University of Zagreb, Prilaz baruna Filipovića 28, 10000, Zagreb, Croatia

    Lela Pintarić

Authors
  1. Ana Vrsalović Presečki
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Lela Pintarić
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Anera Švarc
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Đurđa Vasić-Rački
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Ana Vrsalović Presečki.

Ethics declarations

Conflict of interest

The authors declare that they have no conflict of interest.

Electronic supplementary material

Below is the link to the electronic supplementary material.

Supplementary material 1 (DOCX 197 KB)

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Presečki, A.V., Pintarić, L., Švarc, A. et al. Different strategies for multi-enzyme cascade reaction for chiral vic-1,2-diol production. Bioprocess Biosyst Eng 41, 793–802 (2018). https://doi.org/10.1007/s00449-018-1912-5

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s00449-018-1912-5

Keywords

Search

Navigation