Issue

Vol. 33 No. 10 (2021): Vol 33 Issue 10, 2021

Copyright (c) 2021 AJC

Creative Commons License

This work is licensed under a Creative Commons Attribution 4.0 International License.

Highly Efficient Synthesis of Glucose Fatty Acid Esters Catalyzed by High Performance Lipase Preparations

https://doi.org/10.14233/ajchem.2021.23391
Benu Arora
Department of Applied Sciences and Humanities, Bhagwan Parshuram Institute of Technology, Guru Gobind Singh Indraprastha University, New Delhi-110089, India ; Department of Chemistry, Indian Institute of Technology Delhi, Hauz Khas, New Delhi-110016, India

Corresponding Author(s) : Benu Arora

benu.arora01@gmail.com

Asian Journal of Chemistry, Vol. 33 No. 10 (2021): Vol 33 Issue 10, 2021

Abstract

Glucose fatty acid esters were synthesized using cross-linked enzyme aggregates (CLEAs), protein coated microcrystals (PCMCs) and cross-linked protein coated microcrystals (CLPCMCs) of Candida antarctica lipase B (CALB) as biocatalyst designs in single and mixed solvent systems. Up to 90% conversion and more than 99% regioselectivity were obtained using vinyl acetate as the acyl donor in a solvent system composed of 2-methyl-2-butanol (2M2B) and 30% (v/v) DMSO, with CALB CLEAs within 45 min. Similar results were obtained with CALB CLPCMCs as the biocatalyst under the same reaction conditions. This approach was then extended to the synthesis of glucose esters with higher acyl chain length. The synthetic strategy used in this work can potentially be extended for the fast and regioselective esterification/transesterification of other sugars as well.

Keywords

Lipase Glucose-6-O-acetate High activity biocatalyst designs Transesterification Regioselective synthesis
Arora, B. (2021). Highly Efficient Synthesis of Glucose Fatty Acid Esters Catalyzed by High Performance Lipase Preparations. Asian Journal of Chemistry, 33(10), 2489–2497. https://doi.org/10.14233/ajchem.2021.23391
Download Citation
Endnote/Zotero/Mendeley (RIS)
BibTeX
References
  1. S.W. Chang and J.F. Shaw, N. Biotechnol., 26, 109 (2009); https://doi.org/10.1016/j.nbt.2009.07.003
  2. A.M. Gumel, M.S.M. Annuar, T. Heidelberg and Y. Chisti, Process Biochem., 46, 2079 (2011); https://doi.org/10.1016/j.procbio.2011.07.021
  3. N.S. Neta, J.A. Teixeira and L.R. Rodrigues, Crit. Rev. Food Sci. Nutr., 55, 595 (2015); https://doi.org/10.1080/10408398.2012.667461
  4. G.J. Puterka, W. Farone, T. Palmer and A. Barrington, J. Econ. Entomol., 96, 636 (2003); https://doi.org/10.1093/jee/96.3.636
  5. M. Pacwa-Plociniczak, G.A. Plaza, Z. Piotrowska-Seget and S.S. Cameotra, Int. J. Mol. Sci., 12, 633 (2011); https://doi.org/10.3390/ijms12010633
  6. J. Staron, J.M. Dabrowski, E. Cichon and M. Guzik, Crit. Rev. Biotechnol., 38, 245 (2017). https://doi.org/10.1080/07388551.2017.1332571
  7. D.R. Perinelli, S. Lucarini, L. Fagioli, R. Campana, D. Vllasaliu, A. Duranti and L. Casettari, Eur. J. Pharm. Biopharm., 124, 55 (2018); https://doi.org/10.1016/j.ejpb.2017.12.008
  8. J.A. Arcos, M. Bernabe and C. Otero, Biotechnol. Bioeng., 57, 505 (1998); https://doi.org/10.1002/(SICI)1097-0290(19980305)57:5<505::AIDBIT1>3.0.CO;2-K
  9. N.R. Khan and V.K. Rathod, Process Biochem., 50, 1793 (2015); https://doi.org/10.1016/j.procbio.2015.07.014
  10. P. Inprakhon, N. Wongthongdee, T. Amornsakchai, T. Pongtharankul, P. Sunintaboon, L.O. Wiemann, A. Durand and V. Sieber, J. Biotechnol., 259, 182 (2017); https://doi.org/10.1016/j.jbiotec.2017.07.021
  11. K.-H. Zhao, Y.-Z. Cai, X.-S. Lin, J. Xiong, P. J. Halling and Z. Yang, Molecules, 21, 1294 (2016); https://doi.org/10.3390/molecules21101294
  12. E. Abdulmalek, N.F. Hamidon and M.B. Abdul Rahman, J. Mol. Catal. B: Enzym., 132, 1 (2016); https://doi.org/10.1016/j.molcatb.2016.06.010
  13. V.M. Pappalardo, C.G. Boeriu, F. Zaccheriaa and N. Ravasio, Mol. Catal., 433, 383 (2017); https://doi.org/10.1016/j.mcat.2017.02.029
  14. D.W. Shin, N.L. Mai, S.-W. Bae and Y.- M. Koo, Enzyme Microb. Technol., 126, 18 (2019). https://doi.org/10.1016/j.enzmictec.2019.03.004
  15. A. Zaks and A.M. Klibanov, Proc. Natl. Acad. Sci. USA, 82, 3192 (1985); https://doi.org/10.1073/pnas.82.10.3192
  16. E.P. Hudson, R.K. Eppler and D.S. Clark, Curr. Opin. Biotechnol., 16, 637 (2005); https://doi.org/10.1016/j.copbio.2005.10.004
  17. S. Riva, J. Chopineau, A.P.G. Kieboom and A.M. Klibanov, J. Am. Chem. Soc., 110, 584 (1988); https://doi.org/10.1021/ja00210a045
  18. L. Ferreira, M.A. Ramos, M.H. Gil and J.S. Dordick, Biotechnol. Prog., 18, 986 (2002); https://doi.org/10.1021/bp0255457
  19. N.R. Pedersen, R. Wimmer, R. Matthiesen, L.H. Pedersen and A. Gessesse, Tetrahedron Asymm., 14, 667 (2003); https://doi.org/10.1016/S0957-4166(03)00086-7
  20. S. Ritthitham, R. Wimmer, A. Stensballe and L.H. Pedersen, J. Mol. Catal. B Enzym., 59, 266 (2009); https://doi.org/10.1016/j.molcatb.2008.09.008
  21. Y.-F. Wang, J.J. Lalonde, M. Momongan, D.E. Bergbreiter and C.H. Wong, J. Am. Chem. Soc., 110, 7200 (1988); https://doi.org/10.1021/ja00229a041
  22. A.B. Majumder and M.N. Gupta, Bioresour. Technol., 101, 2877 (2010); https://doi.org/10.1016/j.biortech.2009.09.088
  23. A. Ghanem, Tetrahedron, 63, 1721 (2007); https://doi.org/10.1016/j.tet.2006.09.110
  24. E. Castillo, F. Pezzotti, A. Navarro and L. Lopez-Munguia, J. Biotechnol., 102, 251 (2003); https://doi.org/10.1016/S0168-1656(03)00050-6
  25. M. Ferrer, J. Soliveri, F.J. Plou, N. Lopez-Cortes, M. Christensen, D. ReyesDuarte, J.L. Copa-Patiño and A. Ballesteros, Enzyme Microb. Technol., 36, 391 (2005); https://doi.org/10.1016/j.enzmictec.2004.02.009
  26. D. Reyes-Duarte, N. Lopez-Cortes, M. Ferrer, F.J. Plou and A. Ballesteros, Biocatal. Biotransform., 23, 19 (2005); https://doi.org/10.1080/10242420500071763
  27. X. Yang, P. Zheng, Y. Ni and Z. Sun, J. Biotechnol., 161, 27 (2012); https://doi.org/10.1016/j.jbiotec.2012.05.014
  28. G. Ljunger, P. Adlercreutz and B. Mattiasson, Biotechnol. Lett., 16, 1167 (1994); https://doi.org/10.1007/BF01020845
  29. L. Cao, A. Fischer, U.T. Bornscheuer and R.D. Schmid, Biocatal. Biotransform., 14, 269 (1996); https://doi.org/10.3109/10242429609110280
  30. S. Park and R.J. Kazlauskas, J. Org. Chem., 66, 8395 (2001); https://doi.org/10.1021/jo015761e
  31. F. Ganske and U.T. Bornscheuer, Org. Lett., 7, 3097 (2005); https://doi.org/10.1021/ol0511169
  32. S.H. Lee, D.T. Dang, S.H. Ha, W.-J. Chang and Y.-M. Koo, Biotechnol. Bioeng., 99, 1 (2008); https://doi.org/10.1002/bit.21534
  33. A.M. Sebatini, M. Jain, P. Radha, S. Kiruthika and K. Tamilarasan, 3 Biotech., 6, 184 (2016). https://doi.org/10.1007/s13205-016-0501-z
  34. R.T. Otto, U.T. Bornscheuer, C. Syldatk and R.D. Schmid, J. Biotechnol., 64, 231 (1998); https://doi.org/10.1016/S0168-1656(98)00125-4
  35. P.Y. Goueth, P. Gogalis, R. Bikanga, P. Gode, D. Postel, G. Ronco and P. Villa, J. Carbohydr. Chem., 13, 249 (1994); https://doi.org/10.1080/07328309408009191
  36. M. Kreiner, M.C. Parker and B.D. Moore, Chem. Commun., 1096 (2001); https://doi.org/10.1039/b100722j
  37. R. Sheldon, Biochem. Soc. Trans., 35, 1583 (2007); https://doi.org/10.1042/BST0351583
  38. S. Shah, A. Sharma and M.N. Gupta, Biocatal. Biotransform., 26, 266 (2008); https://doi.org/10.1080/10242420801897429
  39. M. Kapoor and M.N. Gupta, Process Biochem., 47, 503 (2012); https://doi.org/10.1016/j.procbio.2011.12.009
  40. A.B. Majumder, K. Mondal, T.P. Singh and M.N. Gupta, Biocatal. Biotransform., 26, 235 (2008); https://doi.org/10.1080/10242420701685601
  41. R. Schoevaart, M.W. Wolbers, M. Golubovic, M. Ottens, A.P.G. Kieboom, F. van Rantwijk, L.A.M. van der Wielen and R.A. Sheldon, Biotechnol. Bioeng., 87, 754 (2004); https://doi.org/10.1002/bit.20184
  42. K. Solanki, M.N. Gupta and P.J. Halling, Bioresour. Technol., 115, 147 (2012); https://doi.org/10.1016/j.biortech.2011.12.066
  43. C.C. Sweeley, R. Bentley, M. Makita and W.W. Wells, J. Am. Chem. Soc., 85, 2497 (1963); https://doi.org/10.1021/ja00899a032
  44. K. Yoshimoto, Y. Itatani and Y. Tsuda, Chem. Pharm. Bull., 28, 2065 (1980); https://doi.org/10.1248/cpb.28.2065
  45. C. Laane, S. Boeren, K. Vos and C. Veeger, Biotech. Bioeng., 30, 81 (1987); https://doi.org/10.1002/bit.260300112
  46. P. Degn and W. Zimmermann, Biotechnol. Bioeng., 74, 483 (2001); https://doi.org/10.1002/bit.1139
  47. Arora Asian J. Chem.
  48. N. Sanders, Eds.: N.B. Jones and T.R. Nolt, Food Legislation and the Scope for Increased Use of Near-critical Fluid Extraction Operations in the Food, Flavouring and Pharmaceutical Industries, In: Extraction of Natural Products using Near Critical Solvents, Chapman & Hall: London, pp. 34-38 (1993).
  49. P. Degn, L.H. Pedersen, J.Q. Duus and W. Zimmermann, Biotechnol. Lett., 21, 275 (1999); https://doi.org/10.1023/A:1005439801354
  50. M.V. Flores, K. Naraghi, J.-M. Engasser and P.J. Halling, Biotechnol. Bioeng., 78, 815 (2002); https://doi.org/10.1002/bit.10263
  51. K. Ren and B.P. Lamsal, Food Chem., 214, 556 (2017); https://doi.org/10.1016/j.foodchem.2016.07.031
  52. S. Ritthitham, R. Wimmer and L.H. Pedersen, Process Biochem., 46, 931 (2011); https://doi.org/10.1016/j.procbio.2011.01.004
  53. R. Pelagalli, I. Chiarotto, M. Feroci and S. Vecchio, Green Chem., 14, 2251 (2012); https://doi.org/10.1039/c2gc35485c
  54. D. An and Z. Ye, J. Dispersion Sci. Technol., 38, 1181 (2017); https://doi.org/10.1080/01932691.2016.1170609
  55. X.-S. Lin, K.-H. Zhao, Q.-L. Zhou, K.-Q. Xie, P.J. Halling and Z. Yang, Bioresour. Bioprocess., 3, 2 (2016); https://doi.org/10.1186/s40643-015-0080-6
Read More
Author biographies is not available.
Download
PDF
Statistic
Read Counter : 1 Download : 1