Combined cross-linked enzyme aggregates (combi-CLEAs) for efficient integration of a ketoreductase and a cofactor regeneration system

Journal of Biotechnology

Volumn 184, Issue , 2014, Pages 7-10

  Ning, Chenxi ^a   Su, Erzheng ^b   Tian, Yanjun ^a   Wei, Dongzhi ^a  

^a EAST CHINA UNIVERSITY OF SCIENCE AND TECHNOLOGY   (China)

^b NANJING FORESTRY UNIVERSITY   (China)

Author keywords

Asymmetric catalysis; Cofactor regeneration; Combi CLEAs; Ketoreductase

Indexed keywords

BIOTECHNOLOGY;

ASYMMETRIC CATALYSIS; CHIRAL ALCOHOLS; COFACTOR REGENERATION; COMBI-CLEAS; CROSS-LINKED ENZYME AGGREGATES; KETOREDUCTASE; KETOREDUCTASES; LOW COSTS;

CATALYSIS;

ALCOHOL DERIVATIVE; BUTYRIC ACID; CROSS LINKED ENZYME AGGREGATE; GLUCOSE DEHYDROGENASE; OXIDOREDUCTASE; UNCLASSIFIED DRUG; ACETOACETIC ACID DERIVATIVE; CROSS LINKING REAGENT; ETHYL 4-CHLORO-3-OXOBUTANOATE; GLUCOSE;

ARTICLE; BIOTRANSFORMATION; CHIRALITY; CONTROLLED STUDY; COST; CROSS LINKING; ENZYME SUBSTRATE; PRIORITY JOURNAL; SYNTHESIS; CATALYSIS; CHEMISTRY; TEMPERATURE;

ACETOACETATES; ALCOHOLS; CATALYSIS; CROSS-LINKING REAGENTS; GLUCOSE; OXIDOREDUCTASES; TEMPERATURE;

EID: 84901452145     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2014.05.004     Document Type: Article

References (21)

1. Betancor L., Berne C., Luckarift H.R., Spain J.C. Coimmobilization of a redox enzyme and a cofactor regeneration system. Chem. Commun. 2006, 34:3640-3642.
2. Cao L.Q., Rantwijk F., Van Sheldon R.A. Cross-linked enzyme aggregates: a simple and effective method for the immobilization of penicillin acylase. Org. Lett. 2000, 2:1361-1364.
3. Fagain C.O. Enzyme stabilization-recent experimental progress. Enzyme Microb. Technol. 2003, 33:137-149.
4. Honda T., Miyazaki M., Nakamura H., Maeda H. Facile preparation of an enzyme-immobilized microreactor using a cross-linking enzyme membrane on a microchannel surface. Adv. Synth. Catal. 2006, 348:2163-2171.
5. Iyer P.V., Ananthanarayan L. Enzyme stability and stabilization-aqueous and non-aqueous environment. Process Biochem. 2008, 43:1019-1032.
6. Kataoka M., Yamamoto K., Kawabata H., Wada M., Kita K., Yanase H., Shimizu S. Stereoselective reduction of ethyl 4-chloro-3-oxobutanoate by Escherichia coli transformant cells coexpressing the aldehyde reductase and glucose dehydrogenase genes. Appl. Microbiol. Biotechnol. 1999, 51:486-490.
7. Kizaki N., Yasohara Y., Hasegawa J., Wada M., Kataoka M., Shimizu S. Synthesis of optically pure ethyl (S)-4-chloro-3-hydroxybutanoate by Escherichia coli transformant cells coexpressing the carbonyl reductase and glucose dehydrogenase genes. Appl. Microbiol. Biotechnol. 2001, 55:590-595.
8. Ladero M., Santos A., Garcia-Ochoa F. Kinetic modelling of the thermal inactivation of an industrial β-galactosidase from Kluyveromyces fragilis. Enzyme Microb. Technol. 2006, 38:1-9.
9. Leipold F., Hussain S., Ghislieri D., Turner N.J. Asymmetric reduction of cyclic imines catalyzed by a whole-cell biocatalyst containing an (S)-imine reductase. ChemCatChem 2013, 5:3505-3508.
10. Patel R.N. Synthesis of chiral pharmaceutical intermediates by biocatalysis. Coord. Chem. Rev. 2008, 252:659-701.
11. Pollard D.J., Woodley J.M. Biocatalysis for pharmaceutical intermediates: the future is now. Trends Biotechnol. 2007, 25:66-73.
12. Poltorak O.M., Chukhrai E.S., Kozlenkov A.A., Chaplin M.F., Trevan M.D. The putative common mechanism for inactivation of alkaline phosphatase isoenzymes. J. Mol. Catal. B: Enzym. 1999, 7:157-163.
13. Schoevaart R., Wolbers M.W., Golubovic M., Ottens M., Kieboom A.P.G., Rantwijk F., Van Wielen L.A.M., van der Sheldon R.A. Preparation, optimization, and structures of cross-linked enzyme aggregates (CLEAs). Biotechnol. Bioeng. 2004, 87:754-762.
14. Shah S., Sharma A., Gupta M.N. Preparation of cross-linked enzyme aggregates by using bovine serum albumin as a proteic feeder. Anal. Biochem. 2006, 351:207-213.
15. Sheldon R.A. Cross-linked enzyme aggregates (CLEAs): stable and recyclable biocatalysts. Biochem. Soc. Trans. 2007, 35:1583-1587.
16. Shimizu S., Kataoka M., Katoh M., Morikawa T., Miyoshi T., Yamada H. Stereoselective reduction of ethyl 4-chloro-3-oxobutanoate by a microbial aldehyde reductase in an organic solvent-water diphasic system. Appl. Environ. Microbiol. 1990, 56:2374-2377.
17. Vrtis J.M., White A.K., Metcalf W.W., van der Donk W.A. Phosphite dehydrogenase: a versatile cofactor-regeneration enzyme. Angew. Chem. Int. Ed. 2002, 41:3257-3259.
18. Wandrey C., Flaschel E., Schuegerl K. Problems in extrapolation of enzyme kinetics measurements to reactor design using hog kidney acylase as an example. Biotechnol. Bioeng. 1979, 21:1649-1670.
19. Wang M.F., Jia C.X., Qi W., Yu Q.X., Peng X., Su R.X., He Z.M. Porous-CLEAs of papain: application to enzymatic hydrolysis of macromolecules. Biores. Technol. 2011, 102:3541-3545.
20. Wilson L., Betancor L., Fernandez-Lorente G., Fuentes M., Hidalgo A., Guisan J.M., Pessela B.C.C., Fernandez-Lafuente R. Cross-linked aggregates of multimeric enzymes: a simple and efficient methodology to stabilize their quaternary structure. Biomacromolecules 2004, 5:814-817.
21. Zhang Z.J., Pan J., Liu J.F., Xu J.H., He Y.C., Liu Y.Y. Significant enhancement of (R)-mandelic acid production by relieving substrate inhibition of recombinant nitrilase in toluene-water biphasic system. J. Biotechnol. 2011, 152:24-29.