Two-step process for preparation of oligosaccharide propionates and acrylates using lipase and Cyclodextrin Glycosyl Transferase (CGTase)
Tóm tắt
Oligosaccharide esters are attractive candidates for applications as surfactants, hydrogels and other materials, but direct enzymatic acylation is difficult with carbohydrates longer than disaccharides. A combination of one lipase-catalyzed step and one transglycosylation step catalyzed by a cyclodextrin glycosyl transferase (CGTase) was used to synthesize oligosaccharide esters. The conversion of glucose and maltose with vinyl propionate catalyzed by Candida antarctica lipase B (Novozym 435) in dioxane proceeded to full conversion to mixtures of mono and diesters. When ethyl acrylate was used as acyl donor, mono and diesters were formed, but full conversion was not reached. The CGTase catalyzed reactions between the glucose and maltose esters and α-cyclodextrin were carried out in water. In the initial phase, addition of the glucose residues of the cyclodextrin to the ester substrate occurred (coupling reaction), followed by disproportionation reactions yielding a range of oligosaccharide esters with varying chain length. The monoesters were efficient acceptors in the CGTase-catalyzed reactions, while the diesters were not converted to a significant extent. As a consequence, the glucose propionate which contained large amounts of diesters was converted to 40% conversion while the maltose propionate which contained mainly monoesters was converted to 86% conversion. A two-step enzymatic process for preparation of oligosaccharide esters has been developed. Oligosaccharide propionates were produced in high yield with a total reaction time of 5 h. The double bond of the acrylate moiety reduced the reaction rate of the lipase catalyzed transesterification, but in both cases, the CGTase efficiently converted the monoesters to oligosaccharide esters.
Tài liệu tham khảo
Martin BD, Ampofo SA, Linhardt RJ, Dordick JS: Biocatalytic synthesis of sugar-containing poly(acrylate)-based hydrogels. Macromolecules. 1992, 25: 7081-7085. 10.1021/ma00052a001.
Patil NS, Li YZ, Rethwisch DG, Dordick JS: Sucrose diacrylate: a unique chemically and biologically degradable crosslinker for polymeric hydrogels. J Polymer Sci Part a-Polymer Chem. 1997, 35: 2221-2229. 10.1002/(SICI)1099-0518(199708)35:11<2221::AID-POLA12>3.0.CO;2-G.
Croitoru R, Fitigau F, van den Broek LAM, Frissen AE, Davidescu CM, Boeriu CG, Peter F: Biocatalytic acylation of sugar alcohols by 3-(4-hydroxyphenyl)propionic acid. Process Biochem. 2012, 47: 1894-1902. 10.1016/j.procbio.2012.06.015.
Ljunger G, Adlercreutz P, Mattiasson B: Lipase catalyzed acylation of glucose. Biotechnol Lett. 1994, 16: 1167-1172. 10.1007/BF01020845.
Cao L, Fischer A, Bornscheuer UT, Schmid RD: Lipase-catalyzed solid phase synthesis of sugar fatty acid esters. Biocatal Biotransform. 1997, 14: 269-283.
Gumel AM, Annuar MSM, Heidelberg T, Chisti Y: Lipase mediated synthesis of sugar fatty acid esters. Process Biochem (Amsterdam, Neth). 2011, 46: 2079-2090.
Degn P, Pedersen LH, Duus JO, Zimmermann W: Lipase-catalysed synthesis of glucose fatty acid esters in tert-butanol. Biotechnol Lett. 1999, 21: 275-280. 10.1023/A:1005439801354.
Ferrer M, Cruces MA, Plou FJ, Bernabe M, Ballesteros A: A simple procedure for the regioselective synthesis of fatty acid esters of maltose, leucrose, maltotriose and n-dodecyl maltosides. Tetrahedron. 2000, 56: 4053-4061. 10.1016/S0040-4020(00)00319-7.
Alissandratos A, Baudendistel N, Flitsch SL, Hauer B, Halling PJ: Lipase-catalysed acylation of starch and determination of the degree of substitution by methanolysis and GC. BMC Biotechnol. 2010, 10: 82-10.1186/1472-6750-10-82.
Okada K, Zhao H, Izumi M, Nakajima S, Baba N: Glucosylation of sucrose laurate with cyclodextrin glucanotransferase. Biosci Biotechnol Biochem. 2007, 71: 826-829. 10.1271/bbb.60646.
Svensson D, Ulvenlund S, Adlercreutz P: Enzymatic route to alkyl glycosides having oligomeric head groups. Green Chem. 2009, 11: 1222-1226. 10.1039/b904849a.
Svensson D, Ulvenlund S, Adlercreutz P: Efficient synthesis of a long carbohydrate chain alkyl glycoside catalyzed by Cyclodextrin Glycosyltransferase (CGTase). Biotechnol Bioeng. 2009, 104: 854-861. 10.1002/bit.22472.
Anderson EM, Karin M, Kirk O: One biocatalyst - many applications: the use of Candida antarctica B-lipase in organic synthesis. Biocatal Biotransform. 1998, 16: 181-204. 10.3109/10242429809003198.
Nordblad M, Adlercreutz P: Efficient enzymatic acrylation through transesterification at controlled water activity. Biotechnol Bioeng. 2008, 99: 1518-1524. 10.1002/bit.21706.
Hanefeld U: Reagents for (ir) reversible enzymatic acylations. Org Biomol Chem. 2003, 1: 2405-2415. 10.1039/b302109b.
Ohrner N, Martinelle M, Mattson A, Norin T, Hult K: Displacement of the equilibrium in lipase catalyzed transesterification in ethyl octanoate by continuous evaporation of ethanol. Biotechnol Lett. 1992, 14: 263-268. 10.1007/BF01022321.
Nordblad M, Adlercreutz P: Effects of acid concentration and solvent choice on enzymatic acrylation by Candida antarctica lipase B. J Biotechnol. 2008, 133: 127-133. 10.1016/j.jbiotec.2007.09.002.
Syren PO, Hult K: Substrate conformations set the rate of enzymatic acrylation by lipases. ChemBioChem. 2010, 11: 802-810. 10.1002/cbic.200900758.
Yan YC, Bornscheuer UT, Stadler G, Lutz-Wahl S, Otto RT, Reuss M, Schmid RD: Regioselective lipase-catalyzed synthesis of glucose ester on a preparative scale. Eur J Lipid Sci Technol. 2001, 103: 583-587. 10.1002/1438-9312(200109)103:9<583::AID-EJLT5830>3.0.CO;2-4.
Woudenberg-van Oosterom M, van Rantwijk F, Sheldon RA: Regioselective acylation of disaccharides in tert-butyl alcohol catalyzed by Candida antarctica lipase. Biotechnol Bioeng. 1996, 49: 328-333.
Vetter D, Thorn W: Chain length specificity of cyclodextrin glycosyltransferase. Starch/Stärke. 1992, 44: 229-233.
Gitlesen T, Bauer M, Adlercreutz P: Adsorption of lipase on polypropylene powder. Biochim Biophys Acta. 1997, 1345: 188-196. 10.1016/S0005-2760(96)00176-2.