Predicting enzyme behavior in nonconventional media: correlating nitrilase function with solvent properties.

作者: Praveen Kaul , U. C. Banerjee

DOI: 10.1007/S10295-008-0332-Y

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摘要: The insolubility of nitrile substrates in aqueous reaction mixture decreases the enzymatic rate. We studied interaction fourteen water miscible organic solvents with immobilized hydrolyzing biocatalyst. Correlation nitrilase function physico–chemical properties has allowed us to predict enzyme behavior such non-conventional media. Addition solvent up a critical concentration leads an enhancement rate, however, any further increase beyond latter decrease catalytic efficiency enzyme, probably due protein denaturation. dielectric constant (e) showed linear correlation used and extent hydrolysis. Unlike alcohols, rate case aprotic could be linearly correlated log P. Further, kinetic analysis confirmed that affinity for its substrate (Km) was highly dependent upon used. Finally, prospect engineering also permitted control enantioselectivity by regulating enantiomer traffic at active site.

参考文章(23)
Norman Layh, Andrew Willetts, Enzymatic nitrile hydrolysis in low water systems Biotechnology Letters. ,vol. 20, pp. 329- 331 ,(1998) , 10.1023/A:1005358809561
Alexander M. Klibanov, Improving enzymes by using them in organic solvents Nature. ,vol. 409, pp. 241- 246 ,(2001) , 10.1038/35051719
Anirban Banerjee, Praveen Kaul, U. C. Banerjee, Purification and characterization of an enantioselective arylacetonitrilase from Pseudomonas putida. Archives of Microbiology. ,vol. 184, pp. 407- 418 ,(2006) , 10.1007/S00203-005-0061-9
Paul A. Fitzpatrick, Alexander M. Klibanov, How can the solvent affect enzyme enantioselectivity Journal of the American Chemical Society. ,vol. 113, pp. 3166- 3171 ,(1991) , 10.1021/JA00008A054
Praveen Kaul, Anirban Banerjee, Uttam Chand Banerjee, Stereoselective nitrile hydrolysis by immobilized whole-cell biocatalyst. Biomacromolecules. ,vol. 7, pp. 1536- 1541 ,(2006) , 10.1021/BM0507913
Praveen Kaul, Anirban Banerjee, S. Mayilraj, Uttam C. Banerjee, Screening for enantioselective nitrilases : Kinetic resolution of racemic mandelonitrile to (R)-(-)-mandelic acid by new bacterial isolates Tetrahedron-asymmetry. ,vol. 15, pp. 207- 211 ,(2004) , 10.1016/J.TETASY.2003.10.041
Marco Terreni, Giuseppe Pagani, Daniela Ubiali, Roberto Fernández-Lafuente, Cesar Mateo, José M Guisán, None, Modulation of penicillin acylase properties via immobilization techniques: one-pot chemoenzymatic synthesis of Cephamandole from Cephalosporin C. Bioorganic & Medicinal Chemistry Letters. ,vol. 11, pp. 2429- 2432 ,(2001) , 10.1016/S0960-894X(01)00463-2
Kazushi Kinbara, Kenichi Sakai, Yukihiko Hashimoto, Hiroyuki Nohira, Kazuhiko Saigo, Design of resolving reagents: p-substituted mandelic acids as resolving reagents for 1-arylalkylamines Tetrahedron-asymmetry. ,vol. 7, pp. 1539- 1542 ,(1996) , 10.1016/0957-4166(96)00175-9
Shinichirou Tawaki, Alexander M. Klibanov, Inversion of enzyme enantioselectivity mediated by the solvent Journal of the American Chemical Society. ,vol. 114, pp. 1882- 1884 ,(1992) , 10.1021/JA00031A054
Charles R. Wescott, Alexander M. Klibanov, Solvent variation inverts substrate specificity of an enzyme Journal of the American Chemical Society. ,vol. 115, pp. 1629- 1631 ,(1993) , 10.1021/JA00058A002