Efficient production of diltiazem chiral intermediate using immobilized lipase from Serratia marcescens
Tóm tắt
The lipase from Serratia marcescence ECU1010 (Sml) was capable of enantioselectively catalyzing the synthesis of many chiral drug precursors. This paper investigated the immobilization of Sml on appropriate supporting materials and its performance in bioreactor. Chitosan, Celite 545, and DEAE-cellulose were found to be the ideal supports among 8 carriers tested with respect to enzyme load and activity recovery of lipase. When Sml was immobilized, significant improvements of stability against pH, thermal, and operational deactivation were observed with all the 3 better supports, and the best stability was observed when the lipase was immobilized on glutaraldehyde activated chitosan. As for the effect of organic solvent in the biphasic reaction system, the hydrolytic activity of the immobilized lipase on trans-3-(4′-methoxyphenyl)glycidic acid methyl ester ((±)-MPGM) observed in isopropyl ether was 6 and 3 times higher than those in toluene and methyl tert-butyl ether. The lipasecatalyzed production of (−)-MPGM by enzymatic resolution of (±)-MPGM with chitosan-Sml in isopropyl etherwater biphasic system was carried out in a 2 L stirred-tank reactor. The batch operation was more efficient operation mode for the enantioselective hydrolysis of (±)-MPGM, affording enantiopure (−)-MPGM in 44.3% overall yield, in contrast to 29.3% in a continuous reactor.
Tài liệu tham khảo
Nagao, T., M. Sato, H. Nakajima, and A. Kiyomoto (1972) Studies on a new 1, 5-benzothiazepine derivative (CRD-401). II. Vasodilator actions. Jpn. J. Pharmacol. 22: 1–10.
Abe, K., H. Inoue, and T. Nagao (1988) Diltiazem hydrochloride: synthetic and pharmacological studies and development. Yakugaku Zasshi 108: 716–732.
Lopez, J. L. and S. L. Matson (1997) A multiphase/extractive enzyme membrane reactor for production of diltiazem chiral intermediate. J. Membr. Sci. 125: 189–211.
Shibatani, T., K. Omori, H. Akatsuka, E. Kawai, and H. Matsumae (2000) Enzymatic resolution of diltiazem intermediate by Serratia marcescens lipase: molecular mechanism of lipase secretion and its industrial application. J. Mol. Catal. B: Enzymatic 10: 141–149.
Dodds, D. R. and J. L. Lopez (1993) Enzymatic hydrolysis of glycidate esters in the presence of bisulfite anion. US Patent 5,274,300.
Hulshof, L. A. and J. H. Roskan (1989) Phenylglycidate stereoisomers, conversion products thereof with e.g. 2-nitrothiophenol and preparation of diltiazem. WO Patent 343,714.
Matsumae, H., M. Furui, T. Shibatani, and T. Tosa (1994) Production of optically active 3-phenylglycidic acid ester by the Serratia marcescens lipase on a hollow fibre membrane reactor. J. Ferment. Bioeng. 78: 59–63.
Shibatani, T. and K. Nakamichi (1990) Method for preparing optically active 3-phenylglycidic acid esters. WO Patent 362,556.
Rosu, R., Y. Vozaki, Y. Iwasaki, and T. Yamane (1997) Repeated use of immobilized lipase for monoacylglycerol production by solid-phase glycerolysis of olive oil. J. Am. Oil Chem. Soc. 74: 445–450.
Bornscheuer, U. T. and T. Yamane (1994) Activity and stability of lipase in the solid-phase glycerolysis of triolein. Enzym. Microb. Technol. 16: 864–869.
Brady, C., L. Metcalfe, D. Slaboszewski, and D. Frank (1988) Lipase immobilized on a hydrophobic microporous supports for the hydrolysis of fats. J. Am. Oil Chem. Soc. 65: 917–921.
Gao, L., J. H. Xu, X. J. Li and Z. Z. Liu (2004) Optimization of Serratia marcescens lipase production for enantioselective hydrolysis of 3-phenylglycidic acid ester. J. Ind. Microbiol. Biotechnol. 31: 525–530.
Zhao, L. L., J. H. Xu, J. Zhao, J. Pan, and Z. L. Wang (2008) Biochemical properties and potential applications of an organic solvent tolerant lipase isolated from Serratia marcescens ECU1010. Process Biochem. 43: 626–633.
Long, Z. D., J. H. Xu, and J. Pan (2007) Immobilization of Serratia marcescens lipase and catalytic resolution of trans-3-(4′-methoxyphenyl)glycidic acid methyl ester. Chin. J. Catal. 28: 175–179.
Crotti, P., M. Terretti, F. Macchia, and A. Stoppioni (1986) Ring-opening reaction of cis- and trans-2,3-bis(4-methoxybenzyl) oxirane: competition between assistance by and migration of an aryl group. J. Org. Chem. 51: 2759–2766.
Long, Z. D., J. H. Xu, and J. Pan (2007) Significant improvement of Serratia marcescens lipase fermentation, by optimizing medium, induction, and oxygen supply. Appl. Biochem. Biotechnol. 142: 148–157.
Arruda, E. J. and C. C. Santana (2003) Phenylboronate-chitosan resins for adsorption of β-amylase from soybean extracts. Appl. Biochem. Biotechnol. 105: 829–842.
Kosaka, P. M., Y. Kawano, O. A. El Seoud, and D. F. S. Petri (2007) Catalytic activity of lipase immobilized onto ultrathin films of cellulose esters. Langmuir 23: 12167–12173.
Kosugi, Y., H. Tanaka, and N. Tomizuka (1990) Continuous hydrolysis of oil by immobilized lipase in a counter current reactor. Biotechnol. Bioeng. 36: 617–622.
Matsumae, H., M. Furui, and T. Shibatani (1993) Lipase-catalyzed asymmetric hydrolysis of 3-Phenylglycidic acid ester, the key intermediate in the synthesis of Diltiazem hydrochloride. J. Ferment. Bioeng. 75: 93–98.
Alloue, W. A., J. Destain, T. El Medjoub, H. Ghalfi, P. Kabran, and P. Thonart (2008) Comparison of Yarrowia lipolytica lipase immobilization yield of entrapment, adsorption, and covalent bond techniques. Appl. Biochem. Biotechnol. 150: 51–63.
Deng, H. T., Z. K. Xu, Z. M. Liu, J. Wu, and P. Ye (2004) Adsorption immobilization of Candida rugosa lipases on polypropylene hollow fiber microfiltration membranes modified by hydrophobic polypeptides. Enzym. Microb. Technol. 35: 437–443.
Knezevic, Z., N. Milosavic, D. Bezbradica, Z. Jakovljevic, and R. Prodanovic (2006) Immobilization of lipase from Candida rugosa on Eupergit® supports by covalent attachment. Biochem. Eng. J. 30: 269–278.
Palomo, J. M., R. L. Segura, G. F. Lorente, R. F. Lafuente, and J. M. Guisan (2007) Glutaraldehyde modification of lipases adsorbed on aminated supports: a simple way to improve their behavior as enantioselective biocatalyst. Enzym. Microb. Technol. 40: 704–707.
Krajewska, B. (2004) Application of chitin- and chitosan-based materials for enzyme immobilizations: a review. Enzym. Microb. Technol. 35: 126–139.
Munjal, N. and S. K. Sawhney (2002) Stability and properties of mushroom tyrosinase entrapped in alginate, polyacrylamide and gelatin gels. Enzym. Microb. Technol. 30: 613–619.
Montero, S., A. Blanco, M. D. Virto, L. C. Landeta, I. Agud, and R. Solozabal (1993) Immobilization of Candida rugosa lipase and some properties of the immobilized enzyme. Enzym. Microb. Technol. 15: 239–247.
Hilterhaus, L., O. Thum, and A. Liese (2008) Reactor concept for lipase-catalyzed solvent-free conversion of highly viscous reactants forming two-phase systems. Org. Process Res. Dev. 12: 618–625.
Van Aken, B. P., L. Henry, N. Spiros, and N. Agathos (2000) Co-immobilization of manganese peroxidase from Phlebia radiata on porous silica beads. Biotechnol. Lett. 8: 641–646.
Seyhan, T. S. and O. Alptekin (2004) Immobilization and kinetics of catalase onto magnesium silicate. Process Biochem. 39: 2149–2155.
Lamas, E. M., R. M. Barros, V. M. Balcão, and F. X. Malcata (2001) Hydrolysis of whey proteins by proteases extracted from Cynara cardunculus and immobilized onto highly activated supports. Enzym. Microb. Technol.28: 642–652.
Mohammad, T. B. and M. T. Bustard (2008) Fed batch bioconversion of 2-propanol by a solvent tolerant strain of Alcaligenes faecalis entrapped in Ca-alginate gel. J. Ind. Microbiol. Biotechnol. 35: 677–684.
Biró, E., A. Sz. Németh, C. Sisak, T. Feczkó, and J. Gyenis (2008) Preparation of chitosan particles suitable for enzyme immobilization. J. Biochem. Biophys. Methods 70: 1240–1246.
Kasche, V. (1983) Correlation of experimental and theoretical data for artificial and natural systems with immobilized biocatalysts. Enzym. Microb. Technol. 5: 2–13.