Synthesis of vitamin E succinate from Candida rugosa lipase in organic medium

Abstract

A screening of commercially available lipases for the synthesis of vitamin E succinate showed that lipase from Candida rugosa presented the highest yield. The synthesis of vitamin E succinate in organic solvents with different lgP values ranging from −1.3 to 3.5 was investigated. Of particular interest was that dimethyl sulfoxide (DMSO) with the lowest lgP exhibited the highest yield among all the organic solvents used. It suggests that lgP is incapable of satisfactorily predicting the biocompatibility of organic solvents due to the complexity of enzymatic reaction with hydrophilic and hydrophobic substrates in organic solvent. Effects of different operating conditions, such as molar ratio of substrate, enzyme concentration, reaction temperature, mass transfer, and reaction time were also studied. Under the optimum conditions of 10 g/L enzyme, a stirring rate of 100 r/min, a substrate molar ratio of 5:1 at 55 °C for 18 h, a satisfactory yield(46.95%) was obtained. The developed method has a potential to be used for efficient enzymatic production of vitamin E succinate.

Keywords

Vitamin E succinate / Candida rugosa lipase / Operating condition

References

[1] Valentin H. E., Qi Q. Appl. Microbiol. Biotechnol., 2005, 68: 436.

[2] Barros L., Correia D. M., Ferreira I. C. F. R., Baptistaa P., Santos-Buelga C. Food Chem., 2008, 110: 1046.

[3] Israel K., Yu W., Sanders B. G., Kline K. Nutrition Cancer, 2000, 36: 90.

[4] Quin J., Engle D., Litwiller A., Peralta E., Grasch A., Boley T., Hazelrigg S. J. Surgical Res., 2005, 127: 139.

[5] Prasad K. N., Kumar B., Yan X. D., Hanson A. J., Cole W. C. J. Am. Coll. Nutrition, 2003, 22: 108.

[6] Bonrath W., Cirillo F., Process for the Preparation of Tocol Acylates and Tocopherol Acylates, US6444098B2, 2002

[7] Torres P., Reyes D. D., Lopez C. N., Ferrer M., Ballesteros A., Plou F. J. Process Biochem., 2008, 43: 145.

[8] Xin J., Chen L., Zhang Y., Wen R. R., Zhao D. M., Xia C. G. Food Biotechnol., 2011, 25: 43.

[9] Yin C. H., Zhang C., Gao M. Chinese. J. Chem. Eng., 2011, 19: 135.

[10] Castillo E., Pezzotti F., Navarro A., López-Munguía A. J. Biotechnol., 2003, 102: 251.

[11] Kaewprapan K., Tuchinda P., Marie E., Durandc A., Inprakhon P. J. Mol. Catal. B: Enzymatic, 2007, 47: 135.

[12] Ferreira L., Gil M. H., Cabrita A., Dordick J. S. Biomaterials, 2005, 26: 4707.

[13] Ferreira L., Gil M. H., Dordick J. S. Biomaterials, 2002, 23: 3957.

[14] Laane C., Boeren S., Vos K., Veeger C. Biotechnol. Bioeng., 1987, 30: 81.

[15] Klibanov A. M. Nature, 2001, 409: 241.

[16] Carrea G., Riva S. Angew. Chem. Int. Ed., 2000, 39: 2226.

[17] Klibanov A. M. Acc. Chem. Res., 1990, 23: 114.

[18] Rubio E., Fernandez M. A., Klibanov A. M. J. Am. Chem. Soc., 1991, 113: 695.

[19] Gogoi P., Hazarika S., Dutta N. N., Rao P. G. Chem. Eng. J., 2009, 155: 810.

[20] Hazarika S., Goswami P., Dutta N. N. Chem. Eng. J., 2003, 94: 1.

[21] Lu J. K., Nie K. L., Wang F., Tan T. W. Bioresour. Technol., 2008, 99: 6070.

[22] Yang T., Rebsdorf M., Engelrud U., Xu X. J. Food Lipids, 2005, 12: 299.

[23] Duan Z. Q., Du W., Liu D. H. Process Biochem., 2010, 45: 1923.

[24] Wolff A., Zhu L., Wong Y., Straathof A., Jongejan J., Heijnen J. Biotechnol. Bioeng., 1999, 62: 125.

[25] Han S. Y., Pan Z. Y., Huang D. F., Ueda M., Wang X. N. J. Mol. Catal. B: Enzymatic, 2009, 59: 16.