Cascade catalysis in membranes with enzyme immobilization for multi-enzymatic conversion of CO2 to methanol

New Biotechnology

Volumn 32, Issue 3, 2015, Pages 319-327

  Luo, Jianquan ^a   Meyer, Anne S ^a   Mateiu, R V ^a   Pinelo, Manuel ^a  

^a TECHNICAL UNIVERSITY OF DENMARK   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

CARBON DIOXIDE; CATALYSIS; ECONOMIC AND SOCIAL EFFECTS; ENZYME ACTIVITY; ENZYME INHIBITION; FORMALDEHYDE; MASS TRANSFER; MEMBRANE FOULING; METHANOL; MICROFILTRATION;

ALCOHOL DEHYDROGENASE; CATALYTIC EFFICIENCIES; FLAT SHEET POLYMERIC MEMBRANES; FORMALDEHYDE DEHYDROGENASE; FORMATE DEHYDROGENASE; NON-COVALENT IMMOBILIZATION; OPERATIONAL CONDITIONS; SUBSTRATE CONCENTRATIONS;

ENZYME IMMOBILIZATION;

ALCOHOL DEHYDROGENASE; CARBON DIOXIDE; FORMALDEHYDE; FORMALDEHYDE DEHYDROGENASE; FORMATE DEHYDROGENASE; FORMIC ACID; METHANOL; ORGANIC SOLVENT; POLYMER; ALDEHYDE DEHYDROGENASE; FORMALDEHYDE DEHYDROGENASE, GLUTATHIONE-INDEPENDENT; IMMOBILIZED ENZYME; NICOTINAMIDE ADENINE DINUCLEOTIDE; SOLVENT;

ARTICLE; BIOTRANSFORMATION; CATALYSIS; CONTROLLED STUDY; DIFFUSION; ENZYME ACTIVITY; ENZYME IMMOBILIZATION; ENZYME MECHANISM; FILTRATION; FLOW; MEMBRANE; NEGATIVE FEEDBACK; NONHUMAN; PRESSURE; PRIORITY JOURNAL; SEPARATION TECHNIQUE; ANIMAL; BOVINE; CANDIDA; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; LIVER; METABOLISM; SACCHAROMYCES CEREVISIAE;

ALCOHOL DEHYDROGENASE; ALDEHYDE OXIDOREDUCTASES; ANIMALS; CANDIDA; CARBON DIOXIDE; CATALYSIS; CATTLE; ENZYMES, IMMOBILIZED; FORMATE DEHYDROGENASES; LIVER; METHANOL; NAD; POLYMERS; PRESSURE; SACCHAROMYCES CEREVISIAE; SOLVENTS; SUBSTRATE SPECIFICITY;

EID: 84924249754     PISSN: 18716784     EISSN: 18764347     Source Type: Journal    
DOI: 10.1016/j.nbt.2015.02.006     Document Type: Article

References (33)

1. Qiao J., Liu Y., Hong F., Zhang J. A review of catalysts for the electroreduction of carbon dioxide to produce low-carbon fuels. Chem Soc Rev 2014, 43:631-675.
2. 2 conversion into fuels and chemicals by catalytic, photocatalytic and electrocatalytic processes. Energy Environ Sci 2013, 6:3112-3135.
3. Ruschig U., Müller U., Willnow P., Höpner T. CO2 reduction to formate by NADH catalysed by formate dehydrogenase from Pseudomonas oxalaticus. Eur J Biochem 1976, 70:325-330.
4. Kuwabata S., Tsuda R., Yoneyama H. Electrochemical conversion of carbon dioxide to methanol with the assistance of formate dehydrogenase and methanol dehydrogenase as biocatalysts. J Am Chem Soc 1994, 116:5437-5443.
5. Obert R., Dave B.C. Enzymatic conversion of carbon dioxide to methanol: enhanced methanol production in silica sol-gel matrices. J Am Chem Soc 1999, 121:12192-12193.
6. 2 to formate by a bacterial carbon dioxide reductase. Science 2013, 342:1382-1385.
7. Baskaya F.S., Zhao X., Flickinger M., Wang P. Thermodynamic feasibility of enzymatic reduction of carbon dioxide to methanol. Appl Biochem Biotechnol 2010, 162:391-398.
8. 2 to methanol by biomimetic coimmobilization of three dehydrogenases in protamine-templated titania. Ind Eng Chem Res 2009, 48:4210-4215.
9. Shi J., Wang X., Jiang Z., Liang Y., Zhu Y., Zhang C. Constructing spatially separated multienzyme system through bioadhesion-assisted bio-inspired mineralization for efficient carbon dioxide conversion. Bioresour Technol 2012, 118:359-366.
10. Wang X., Li Z., Shi J., Wu H., Jiang Z., Zhang W., et al. Bioinspired approach to multienzyme cascade system construction for efficient carbon dioxide reduction. ACS Catal 2014, 4:962-972.
11. 2 catalyzed by coimmobilized enzymes. Biotechnol Bioeng 2008, 99:508-514.
12. 2 to methanol by a polyenzymatic system encapsulated in phospholipids-silica nanocapsules. New J Chem 2013, 37:3721-3730.
13. Zhao F., Li H., Jiang Y., Wang X., Mu X. Co-immobilization of multi-enzyme on control-reduced graphene oxide by non-covalent bonds: an artificial biocatalytic system for the one-pot production of gluconic acid from starch. Green Chem 2014, 16:2558-2565.
14. Liu F., Banta S., Chen W. Functional assembly of a multi-enzyme methanol oxidation cascade on a surface-displayed trifunctional scaffold for enhanced NADH production. Chem Commun 2013, 49:3766-3768.
15. Sassolas A., Blum L.J., Leca-Bouvier B.D. Immobilization strategies to develop enzymatic biosensors. Biotechnol Adv 2012, 30:489-511.
16. Jochems P., Satyawali Y., Diels L., Dejonghe W. Enzyme immobilization on/in polymeric membranes: status, challenges and perspectives in biocatalytic membrane reactors (BMRs). Green Chem 2011, 13:1609-1623.
17. Giorno L., Drioli E. Biocatalytic membrane reactors: applications and perspectives. Trends Biotechnol 2000, 18:339-349.
18. Luo J., Meyer A.S., Jonsson G., Pinelo M. Fouling-induced enzyme immobilization for membrane reactors. Bioresour Technol 2013, 147:260-268.
19. Luo J., Marpani F., Brites R., Frederiksen L., Meyer A.S., Jonsson G., et al. Directing filtration to optimize enzyme immobilization in reactive membranes. J Membr Sci 2014, 459:1-11.
20. Giorno L., Drioli E., Carvoli G., Cassano A., Donato L. Study of an enzyme membrane reactor with immobilized fumarase for production of L-malic acid. Biotechnol Bioeng 2001, 72:77-84.
21. Hadidi M., Zydney A.L. Fouling behavior of zwitterionic membranes: impact of electrostatic and hydrophobic interactions. J Membr Sci 2014, 452:97-103.
22. Kozlovskaya V., Ok S., Sousa A., Libera M., Sukhishvili S.A. Hydrogen-bonded polymer capsules formed by layer-by-layer self-assembly. Macromolecules 2003, 36:8590-8592.
23. SchÜTte H., Flossdorf J., Sahm H., Kula M.-R. Purification and properties of formaldehyde dehydrogenase and formate dehydrogenase from Candida boidinii. Eur J Biochem 1976, 62:151-160.
24. Ando M., Yoshtmoto T., Ogushl S., Rikitake K., Shibata S., Tsuru D. Formaldehyde dehydrogenase from pseudomonas putida: purification and some properties. J Biochem 1979, 85:1165-1172.
25. Reisler E., Pouyet J., Eisenberg H. Molecular weights, association, and frictional resistance of bovine liver glutamate dehydrogenase at low concentrations. Equilibrium and velocity sedmintation, light-scattering studies, and settling experiments with macroscopic models of the enzyme oligomer. Biochemistry 1970, 9:3095-3102.
26. Hermia J. Constant pressure blocking filtration laws-application to power-law non-newtonian fluids. Trans Inst Chem Eng 1982, 60:183-187.
27. Luo J., Meyer A.S., Jonsson G., Pinelo M. Enzyme immobilization by fouling in ultrafiltration membranes: impact of membrane configuration and type on flux behavior and biocatalytic conversion efficacy. Biochem Eng J 2014, 83:79-89.
28. Affandy A., Keshavarz-Moore E., Versteeg H.K. Application of filtration blocking models to describe fouling and transmission of large plasmids DNA in sterile filtration. J Membr Sci 2013, 437:150-159.
29. Palacio L., Ho C.-C., Zydney A.L. Application of a pore-blockage-cake-filtration model to protein fouling during microfiltration. Biotechnol Bioeng 2002, 79:260-270.
30. Mazzuca S., Giorno L., Spadafora A., Mazzei R., Drioli E. Immunolocalization of β-glucosidase immobilized within polysulphone capillary membrane and evaluation of its activity in situ. J Membr Sci 2006, 285:152-158.
31. Jim K.J., Fane A.G., Fell C.J.D., Joy D.C. Fouling mechanisms of membranes during protein ultrafiltration. J Membr Sci 1992, 68:79-91.
32. Jia F., Narasimhan B., Mallapragada S. Materials-based strategies for multi-enzyme immobilization and co-localization: a review. Biotechnol Bioeng 2014, 111:209-222.
33. Wen N., Liu W., Hou Y., Zhao Z. The kinetics behavior of the reduction of formaldehyde catalyzed by alcohol dehydrogenase (ADH) and partial uncompetitive substrate inhibition by NADH. Appl Biochem Biotechnol 2013, 170:370-380.