The Optimised Statistical Model for Enzymatic Hydrolysis of Tapioca by Glucoamylase Immobilised on Mesostructured Cellular Foam Silica

*Joni Agustian -  Department of Chemical Engineering, Universitas Lampung, Indonesia
Lilis Hermida -  Department of Chemical Engineering, Universitas Lampung, Indonesia
Received: 15 Aug 2018; Revised: 4 Feb 2019; Accepted: 6 Feb 2019; Published: 1 Aug 2019; Available online: 30 Apr 2019.
Open Access Copyright (c) 2019 Bulletin of Chemical Reaction Engineering & Catalysis
Creative Commons License
This work is licensed under a Creative Commons Attribution-ShareAlike 4.0 International License.
Citation Format:
Cover Image
Abstract

Enzymatic hydrolysis of starches using free glucoamylase to reducing sugars have difficulties in recovering and recycling of the enzyme, hence immobilisation on inert supports were widely studied. However, effectiveness of the immobilised glucoamylase were merely observed only on soluble starches. It was considered a valuable thing to know performance of glucoamylase on Mesostructured Cellular Foam (MCF) silica in hydrolysing of tapioca. An optimised study on enzymatic hydrolysis of tapioca using glucoamylase on MCF silica (9.2T-3D) and its kinetics were described including justification of the predicted model as it was required to develop in large scale operations. Central Composite Design was used to model the process by studying effects of three factors on DE values after enzyme immobilisation.  Immobilisation of glucoamylase on this support gave up to 82% efficiency with the specific activity of 1,856.78 U.g-1. Its used to hydrolysis of tapioca resulted DE values of 1.740-76.303% (w/w) where the highest DE was obtained at pH of 4.1, temperature of 70 ℃ and agitation speed of 140 rpm. The optimisation produced a polynomial quadratic model having insignificant lack-of-fit and low standard deviation, so that it was applicable and reliable in simulating the DE with only 0.80% of data were not described. Temperature affected the process highly, but the buffer pH, agitation speed and factorial interactions were considered not important. KM value for immobilised enzyme was better than the free glucoamylase, however, its reaction rate was slower than the free glucoamylase catalysis. Copyright © 2019 BCREC Group. All rights reserved

 

Keywords
Enzymatic Hydrolysis; Glucoamylase Immobilisation; Mesostructured Cellular Foam Silica; Tapioca; Central Composite Design

Article Metrics:

  1. Wu, Z., Qi, W., Wang, M., Wang, Y., Su, R., He, Z. (2013). Chelate immobilization of amylase on metal ceramic powder: Preparation, characterization and application. Biochemical Engineering Journal, 77: 190-197.
  2. Guo, C., Yunhui, M., Pengfei, S., Baishan, F. (2012). Direct binding glucoamylase onto carboxyl-functioned magnetic nanoparticles. Biochemical Engineering Journal, 67: 120-125.
  3. Zhao, G., Wang, J, Li, Y, Huang, H., Chen, X. (2012). Reversible immobilization of glucoamylase onto metal-ligand functionalized magnetic FeSBA-15. Biochemical Engineering Journal, 68: 159-166.
  4. Kovalenko, G.A., Perminova, L.V. (2008). Immobilization of glucoamylase by adsorption on carbon supports and its application for heterogeneous hydrolysis of dextrin. Carbohydrate Research, 343: 1202-1211.
  5. Sanjay, G., Sugunan, S. (2005). Glucoamylase immobilized on montmorillonite: Synthesis, characterization and starch hydrolysis activity in a fixed bed reactor. Catalysis Communication, 6: 525-530. doi:10.1016/j.catcom.2005.04.016
  6. Milosavić, N.B., Prodanović, R.M., Jovanović, S.M., Vujčić, Z.M. (2007). Immobilization of glucoamylase via its carbohydrate moiety on macroporous poly(GMA-co-EGDMA). Enzyme Microbial Technology, 40: 1422-1426. doi: 10.1016/j.enzmictec. 2006.10.018
  7. Milosavić, N.B., Prodanović, R.M., Jovanović, S.M., Vujčić, Z.M. (2004). Immobilisation of glucoamylase on macroporous spheres. APTEFF, 35: 207-214.
  8. Torres, R., Pessela, B.C., Mateo, C., Fuentes, C.M., Guisan, J.M., Fernandez-Lafuente, R. (2004). Reversible immobilization of glucoamylase by ionic adsorption on sepabeads coated with polyethyleneimine. Biotechnology Progress. 20: 1297-1300. doi:10.1021/bp049943g
  9. Kamal, H., Sabry, G.M., Lofty, S., Abdallah, N.M., Rosiak, J., El-Sayed, A.H. (2008). Immobilization of glucoamylase on polypropylene fibers modified by radiation induced graft copolymerization. Journal of Macromolecular Science Part A: Pure and Applied Chemistry, 45: 65-75. doi: 10.1080/10601320701683322
  10. Wu, Y.G., Sun, W.T., Wang, S.T., Zhou, H., Li, W. (1998). Preparation and stability of glucoamylase immobilized on porous starch graft copolymer beads. Chemistry Journal of Chinese University, 19: 1346-1348. doi:10.1016/S0141-0229(00)00232-5
  11. Tanriseven, A., Olcer, Z. (2008). A novel method for the immobilization of glucoamylaseonto polyglutaraldehyde-activated gelatin. Biochemical Engineering Journal, 39: 430-434. doi:10.1016/S0141-0229(02)00004-2
  12. Rahim, S.N.A., Sulaiman, A., Hamid, K.H.K., Rodhi, M.N.M., Musa, M., Hamzah, F., Edama, N.A. (2013). Nanoclay supporting materials for enzymes immobilization: kinetics investigation of free and immobilized system. Applied Mechanics and Materials, 393: 115-120.
  13. doi:10.4028/www.scientific.net/AMM.393.115
  14. Oros, B.V., Preda, G, Dudas, Z, Dragomirescu, M., Chiriac, A. (2007). Entrapment of glucoamylase by sol-gel technique in PhTES/TEOS hybrid matrixes. Processing and Application of Ceramics, 1: 63-67. doi:10.2298/PAC0702063V
  15. Szymanska, K., Bryjak, J., Mrowiec-Białon, J., Jarzebski, J.B. (2007). Application and properties of siliceous mesostructured cellular foams as enzymes carriers to obtain efficient biocatalysts. Microporous Mesoporous Materials. 99: 167-175
  16. doi:10.1016/j.micromeso.2006.08.035
  17. George, R., Sugunan, S. (2014). Kinetic and thermodynamic parameters of immobilized glucoamylase on different mesoporous silica for starch hydrolysis: a comparative study. Journal of Molecular Catalysis B:
  18. Enzymatic, 106: 81-89. doi:10.1016/ j.molcatb.2014.04.016
  19. George, R., Gopinath, S., Sugunan, S. (2013). Improved stabilities of immobilized glucoamylase on functionalized mesoporous silica synthesized using decane as swelling agent. Bulletin of Chemical Reaction Engineering and Catalysis, 8: 70-76.
  20. doi:10.9767/bcrec.8.1.4208.70-76
  21. Hermida, L., Abdullah, A.Z., Mohamed, A.R. (2013). Nickel functionalized mesostructured cellular foam (mcf) silica as a catalyst for solventless deoxygenation of palmitic acid to produce diesel-like hydrocarbons. In:
  22. Mendez-Vilas, A. ed. Materials and Processes for Energy: Communicating Current Research and Technological Development. Ed. Formatex Research Center C/ Zurbarán 1, 2, Oficina 1 06002. Badajoz Spain.
  23. Panek, A., Pietrow, O., Synowiecki, J. (2012). Characterization of glucoamylase immobilized on magnetic nanoparticles. Starch/Starke, 00: 1-6.
  24. Wang J., Zhao, G., Li, Y., Liu, Y., Hou, H. (2013). Reversible immobilization of glucoamylase onto magnetic chitosan nanocarriers. Applied Microbiology and Biotechnology. 97: 681-692. doi:10.1007/s00253-012-3979-2
  25. Ma, Y.X., Li, Y.F., Zhao, G.H., Yang, L.Q., Wang, J.Z., Shan, X., Yan, X. (2012). Preparation and characterization of graphite nanosheets decorated with Fe3O4 nanoparticles used in the immobilization of glucoamylase. Carbon, 50: 2976-2986.
  26. Zhao, G., Li, Y., Wang, J., Zhu, H. (2011a). Reversible immobilization of glucoamylase onto magnetic carbon nanotubes functionalized with dendrimer. Applied Microbiology and Biotechnology, 91: 591-60. doi: 10.1007/s00253-011-3299-y
  27. Zhao, G., Wang, J., Li, Y., Chen, X., Liu, Y. (2011b). Enzymes Immobilized on Superparamagnetic Fe3O4@Clays Nanocomposites: Preparation, Characterization, and a New Strategy for the Regeneration of Supports. Journal of Physical Chemistry C, 115: 6350-6359. doi: 10.1021/jp200156j
  28. Fayer, M.D., ed. (2013). Ultrafast Infrared Vibrational Spectroscopy. New York: CRC Press.
  29. Kovalenko, G.A., Perminova, L.V., Terent’eva, T.G., Plaksin, G.V. (2007). Catalytic Properties of Glucoamylase Immobilized on Synthetic Carbon Material Sibunit. Applied Biochemistry and Microbiology, 43: 374-378. doi: 10.1134/ S0003683807040023
  30. Milosavić, N.B., Prodanović, R., Jovanović, S., Novakovic, I., Vujčić, Z. (2005). Preparation and characterization of two types of covalently immobilized amyloglucosidase. J. Serb. Chem. Soc. 70(5) 713-719.
  31. Dwevedi, A. (2016). Basic of enzyme immobilization. Switzerland: Springer International Publishing.
  32. Butterfield. D.A., Bhattacharyya, D., Dannert, S., Bachas, L. (2001). Catalytic biofunctional membranes containing site-specifically immobilized enzyme arrays. Journal of Membran Science, 181: 29-37. doi: 10.1016/S0376-7388(00)00342-2
  33. Cao, W., Zhang, C., Hong, P., Ji, H. (2008). Response surface methodology for autolysis parameters optimization of shrimp head and amino acids released during autolysis. Food Chemistry, 109: 176-183. doi: 10.1016/j.foodchem.2007.11.080
  34. Tan, I.A.W., Ahmad, A.L., Hameed, B.H. (2008). Preparation of activated carbon from coconut husk: optimization study on removal of 2,4,6 trichlorophenol using response surface methodology. Journal of Hazardous Materials, 153: 709-717.
  35. Mudgil, D., Sheweta, B., Khatkar, B.S. (2012). Optimization of enzymatic hydrolysis of guar gum using response surface methodology. Journal of Food Science and Technology, 51: 1600-1605. doi: 10.1007/s13197-012-0678-z
  36. Collares, R.M., Miklasevicius, L.V.S., Bassaco, M.M., Salau, N.P.G., MAzutti, M.A., Bisognin, D.A., Terra, L.M. (2012). Optimization of enzymatic hydrolysis of cassava to obtain fermentable sugars. Journal of Zhejiang University Science B, 13: 579-586. doi: 10.1631/jzus.B1100297
  37. Nadir, N., Mel, M., Karim, M.I.A., Yunus, R.M. (2010). Optimisation of hydrolylis conditions for ethanol production from surgom starch. Journal - The Institution of Engineers Malaysia, 71: 26-34.
  38. Peatciyammal, N., Balachandar, B., Kumar, M.D., Tamilarasan, K., Muthukumaran, C. (2010). Statistical optimization of enzymatic hydrolysis of potato (solanum tuberosum) starch by immobilized α-amylase. International Journal of Biological, Biomolecular, Agricultural, Food and Biotechnological Engineering, 4(1): 126-130
  39. Montgomery, D.C. (2001). Design and analysis of experiments. 5th ed. London: John Wiley & Sons, Inc.
  40. Carpio, C., Escobar, F., Batista-Viera, F., Ruales, J. (2011). Bone-bound glucoamylase as a biocatalyst in bench-scale production of glucose syrups from liquefied cassava starch. Food and Bioprocess Technology, 4:566-577.
  41. Copeland, R.A. (2000). Enzymes: A Practical Introduction to Structure, Mechanism, and Data Analysis, New York: Wiley-VCH, Inc.
  42. Bisswanger, H. (2002). Enzyme Kinetics: Principles and Methods. Weinheim: Wiley-VCH Verlag GmbH.
  43. Bayramoglu, G., Yilmaz, M., Arica, M.Y. (2004). Immobilization of a thermostable alfa amylase onto reactive membrans: Kinetics Characterization and Application to Continuous Starch Hydrolysis. Journal of Food Chemistry, 84: 591-599.