The mechanism of solvent effect on the positional selectivity of Candida antarctica lipase B during 1,3-diolein synthesis by esterification

Bioresource Technology

Volumn 102, Issue 23, 2011, Pages 11048-11050

  Duan, Zhang Qun ^a,b   Du, Wei ^b   Liu, De Hua ^b  

^a Academy of State Administration of Grain   (China)

^b TSINGHUA UNIVERSITY   (China)

Author keywords

Candida antarctica lipase B; Molecular simulation; Positional selectivity; Solvent effect

Indexed keywords

CANDIDA ANTARCTICA LIPASE B; MOLECULAR SIMULATION; NOVOZYM435; POSITIONAL SELECTIVITY; SOLVENT EFFECT; SOLVENT EFFECTS; UNDERLYING MECHANISM;

BINDING ENERGY; CANDIDA; ENZYMES; ESTERIFICATION; ESTERS; GLYCEROL; ISOMERS; OLEIC ACID; YEAST;

SOLVENTS;

GLYCEROL; GLYCEROL DIOLEATE; HYDROXYL GROUP; IMMOBILIZED ENZYME; LIPASE B; OLEIC ACID; SOLVENT;

ALCOHOL; ENERGY EFFICIENCY; ENZYME ACTIVITY; ESTER; HYDROXYL RADICAL; IMMOBILIZATION; MOLECULAR ANALYSIS; NUMERICAL MODEL; SOLVENT;

ARTICLE; CANDIDA ANTARCTICA; ENERGY; ESTERIFICATION; MOLECULAR INTERACTION; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; SYNTHESIS;

BIOTECHNOLOGY; CANDIDA; CATALYSIS; DIGLYCERIDES; ESTERIFICATION; GLYCEROL; LIPASE; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR DYNAMICS SIMULATION; OLEIC ACID; ORGANIC CHEMICALS; SOLVENTS; SUBSTRATE SPECIFICITY;

CANDIDA ANTARCTICA;

EID: 82455175264     PISSN: 09608524     EISSN: 18732976     Source Type: Journal    
DOI: 10.1016/j.biortech.2011.09.003     Document Type: Article

References (21)

1. Branco R.J., Graber M., Denis V., Pleiss J. Molecular mechanism of the hydration of Candida antarctica lipase B in the gas phase: water adsorption isotherms and molecular dynamics simulations. ChemBioChem 2009, 10:2913-2919.
2. Carrea G., Ottolina G., Riva S. Role of solvents in the control of enzyme selectivity in organic media. Trends Biotechnol. 1995, 13:63-70.
3. Duan Z.Q., Du W., Liu D.H. The solvent influence on the positional selectivity of Novozym 435 during 1,3-diolein synthesis by esterification. Bioresour. Technol. 2010, 101:2568-2571.
4. Du W., Liu D.H., Li L.L., Dai L.M. Mechanism exploration during lipase-mediated methanolysis of renewable oils for biodiesel production in a tert-butanol system. Biotechnol. Prog. 2007, 23:1087-1090.
5. Hazarika S., Goswami P., Dutta N.N. Lipase catalyzed transesterification of 2-o-benzylglycerol with vinyl acetate: solvent effect. Chem. Eng. J. 2003, 94:1-10.
6. Hess B., Bekker H., Berendsen H.J.C., Fraaije J.G.E.M. LINCS: a linear constraint solver for molecular simulations. J. Comp. Chem. 1997, 18:1463-1472.
7. Humphrey W., Dalke A., Schulten K. VMD: visual molecular dynamics. J. Mol. Graph. 1996, 14:33-38.
8. Intra A., Nicotra S., Riva S., Danieli B. Significant and unexpected solvent influence on the selectivity of laccase-catalyzed coupling of tetrahydro-2-naphthol derivatives. Adv. Synth. Catal. 2005, 347:973-977.
9. Kumar S.S., Arora N., Bhatnagar R., Gupta R. Kinetic modulation of Trichosporon asahii MSR 54 lipase in presence of organic solvents: altered fatty acid specificity and reversal of enantioselectivity during hydrolytic reactions. J. Mol. Catal. B Enzym. 2009, 59:41-46.
10. Laane C., Boeren S., Vos K., Veeger C. Rules for optimization of biocatalysis in organic solvents. Biotechnol. Bioeng. 1987, 30:81-87.
11. Leonard V., Fransson L., Lamare S., Hult K., Graber M. A water molecule in the stereospecificity pocket of Candida antarctica lipase B enhances the enantioselectivity towards 2-pentanol. ChemBioChem. 2007, 8:662-667.
12. Li C., Tan T.W., Zhang H.Y., Feng W. Analysis of the conformational stability and activity of Candida antarctica lipase B in organic solvents: insight from molecular dynamics and quantum mechanics/simulations. J. Biol. Chem. 2010, 285:28434-28441.
13. Lindahl E., Hess B., van der Spoel D. GROMACS 3.0: a package for molecular simulation and trajectory analysis. J. Mol. Model 2001, 7:306-317.
14. Parks, J.M., Imhof, P., Smith, J.C., 2010. Understanding enzyme catalysis using computer simulation. Encyclopedia of Catalysis.
15. Pieraccini S., Sironi M., Colombo G. Modeling enzymatic processes: a molecular simulation analysis of the origins of regioselectivity. Chem. Phys. Lett. 2006, 418:373-376.
16. Schuttelkopf A.W., van Aalten D.M. PRODRG: a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr. D Biol. Crystallogr. 2004, 60:1355-1363.
17. Uppenberg J., Hansen M.T., Patkar S., Jones T.A. The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica. Structure 1994, 2:293-308.
18. Uppenberg J., Ohrner N., Norin M., Hult K., Kleywegt G.J., Patkar S., Waagen V., Anthonsen T., Jones T.A. Crystallographic and molecular-modeling studies of lipase B from Candida antarctica reveal a stereospecificity pocket for secondary alcohols. Biochemistry 1995, 34:16838-16851.
19. van der Spoel D., Lindahl E., Hess B., Groenhof G., Mark A.E., Berendsen H.J. GROMACS: fast, flexible, and free. J. Comput. Chem. 2005, 26:1701-1718.
20. van Gunsteren W.F., Dolenc J., Mark A.E. Molecular simulation as an aid to experimentalists. Curr. Opin. Struc. Biol. 2008, 18:149-153.
21. Wescott C.R., Klibanov A.M. The solvent dependence of enzyme specificity. Biochim. Biophys. Acta 1994, 1206:1-9.