Influences of Ionic Liquids on Catalytic Performances of Papain

doi:10.3969/j.issn.0251-0790.2012.06.021

Abstract

Abstract: A series of ionic liquids(ILs) based on 1-butyl-3-methylimidazolium([BMIm]), N-ethylpyridi-nium(EPy) and tetraethylammonium([NEt₄]) cations with various kinds of anions(H₂PO₄^-, ClO₄^-, HSO₄^-, CH₃COO^-, Cl^-, Br^-, NO₃^-, SCN^-, BF₄^-, PF₆^-) was examined for their influences on papain-mediated hydrolysis of N-benzoyl-L-arginine ethyl ester. By assaying the hydrolysis activity and thermodynamics deactivation parameters of papain in all these IL-containing systems, it was found that there was no correlation between the enzymatic activity or thermostability and the ILs kosmotropicity. Thus, the Hofmeister effect was not regarded as a good explanation for remarkable effects of ILs on catalytic performance of papain. In the case of BF₄^--based ILs combined with various cations, only [BMIm][BF₄] enhanced the hydrolysis activity of papain, and other ILs lowered the enzymatic activity. However, most of all the tested ILs improved the enzymatic thermostability apart from the strong acidic one -[HOOCMMIm][BF₄]. Among all the examined ILs, the BF₄^-- or PF₆^--based ILs markedly enhanced the activity or thermostability of papain. The enzyme exhibited the highest hydrolysis activity with [BMIm][PF₆], and the best thermostability with [HOEtMIm][BF₄].

Key words: Papain, Ionic liquid, Hofmeister effect, Enzyme activity, Thermostability of enzyme

CLC Number:

O621
O643

TrendMD:

HOU Xue-Dan, LOU Wen-Yong, YAN Li-Qiang, ZONG Min-Hua. Influences of Ionic Liquids on Catalytic Performances of Papain[J]. Chem. J. Chinese Universities, 2012, 33(06): 1245.

References

[1] Sheldon R. A., Lau R. M., Sorgedrager M. J., Rantwijk F., Seddon K. R.. Green Chem.[J], 2002, 4(2): 147—151 [2] Welton T.. Chem. Rev.[J], 1999, 99(8): 2071—2083 [3] Nguyen T. D., Kim K. R., Han S. J., Cho H. Y., Kim J. W., Park S. M., Park J. C., Sim S. J.. Bioresour. Technol.[J], 2010, 101(19): 7432—7438 [4] Prasad V., Kale R., Kumar V., Tiwari V.. Curr. Org. Synth.[J], 2010, 7(5): 506—531 [5] Swatloski R. P., Spear S. K., Holbrey J. D., Rogers R. D.. J. Am. Chem. Soc.[J], 2002, 124: 4974—4975 [6] Moniruzzaman M., Nakashima K., Kamiya N., Goto M.. Biochem. Eng. J.[J], 2010, 48(3): 295—314 [7] CAO Yan(曹妍), WANG Xue-Jing(王学静), LI Hui-Quan(李会泉). Chem. J. Chinese Universities(高等学校化学学报)[J], 2011, 32(11): 2663—2666 [8] Gorke J., Srienc F., Kazlauskas R.. Encycl. Indus. Biotechnol.[J], 2010, 3: 2110—2123 [9] Zhao H.. J. Chem. Technol. Biotechnol.[J], 2010, 85(7): 891—907 [10] Yang Z.. J. Biotechnol.[J], 2009, 144(1): 12—22 [11] Zhao H., Campbell S., Solomon J., Song Z. Y., Olubajo O.. Chin. J. Chem.[J] 2006, 24(4): 580—584 [12] Zhao H., Campbell S., Jackson M. L., Song Z. Y., Olubajo O.. Tetrahedron-Asymmetry[J], 2006, 17(3): 377—383 [13] Zhao H., Olubajo O., Song Z. Y., Sims A. L., Person T. E., Lawal R. A., Holley L. A.. Bioorg. Chem.[J], 2006, 34(1): 15—25 [14] Zhao H., Song Z. Y.. J. Chem. Technol. Biotechnol.[J], 2007, 82(3): 304—312 [15] Yang Z., Yue Y. J., Huang W. C., Zhuang X. M., Chen Z. T., Xing M.. J. Biochem.[J], 2009, 145(3): 355—364 [16] Davis C. N., Smith E.. Methods Biochem. Anal.[J], 1955, 2: 215—218 [17] Saleem M., Rashid M. H., Jabbar A., Perveen R., Khalid A., Rajoka M.. Process Biochem.[J], 2005, 40(2): 849—855 [18] Naidu G. S. N., Panda T.. Biochem. Eng. J.[J], 2003, 16(1): 57—67 [19] Eggers D. K., Valentine J. S.. J. Mol. Biol.[J], 2001, 314(4): 911—922 [20] Foster R. L.. The Nature of Enzymology[M], New York: Wiley, 1980 [21] Zhao H.. J. Mol. Catal. B: Enzym.[J], 2005, 37(1—6): 16—25 [22] Zhao H., Song Z., Olubajo O., Cowins J. V.. Appl. Biochem. Biotechnol.[J], 2009, 162(1): 13—23