| Peer-Reviewed

Optimum Immobilization of Candida Antartica B Lipase on Natural Silica by RSM

Received: 22 February 2017     Accepted: 30 March 2017     Published: 23 May 2017
Views:       Downloads:
Abstract

The immobilization of the lipase of Candida antartica B (LCAB) by adsorption on a natural silica support carried out to develop the adsorbent local supports. Immobilization conditions and characterization of the immobilized enzyme were investigated. Response surface methodology (RSM) and 3-level–3-factor fractional factorial design were employed to evaluate the effects of immobilization parameters, such as immobilization time (5-25 hour), immobilization temperature (25-45°C), and enzyme/support ratio (0.1-0.5, w/w), on yield of lipase immobilization on the support. The optimum immobilization conditions were as follows: immobilization time 18 hours, immobilization temperature 20°C, and enzyme / support ratio 0.5 (w/w); with a yield immobilization of 56,13 mg / g. The immobilization lipase shows hydrolytic and synthesis satisfactory activity.

Published in American Journal of Chemical Engineering (Volume 5, Issue 3)
DOI 10.11648/j.ajche.20170503.13
Page(s) 43-48
Creative Commons

This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.

Copyright

Copyright © The Author(s), 2017. Published by Science Publishing Group

Keywords

Immobilization, Lipase, Natural Silica Support, RSM

References
[1] C. C. Akoh, S. Chang, G. Lee G, J. Shaw. “Enzymatic approach to biodiesel production”, Agric Food Chem, (2007) 55: 8995-9005.
[2] S. K. Narwal, R. Gupta, “Biodiesel production by transesterification using immobilized lipase”, Biotechnol Lett, 35, (2013), 479-490.
[3] R. Richard. “Transestérification éthanolique d'huile végétale dans des microréacteurs: transposition du batch au continu ”, Thèse doctorale (2011), Université de Toulouse.
[4] R. R. de Souza, R. D. M. Ferreira, “Immobilization of Lipase from Candida rugosa on Mesoporous MCM 41”, Journal of Biosciences and Medicines, 2 (2014), 69-73.
[5] W. Kaewthong, S. Sarote, P. Poonsuk, H. Aran, “Continuous production of monoacylglycerols by glycerolysis of palm olein with immobilized lipase”, Process Biochem, 40 (2005), 1525-1530.
[6] S. K. Khare, M. Nakajima, “Immobilization of Rhizopus japonicus lipase on celite and its application for enrichment of docosahexaenoic acid in soybean oil”, Food Chem, 68 (2000), 153-157.
[7] P. C. Oliveira, G. M Alves, H. F. Castro, “Immobilisation studies and catalytic properties of microbial lipase onto styrene-divinylbenzene copolymer”, Biochem. Eng. J. 5 (2000), 63–71.
[8] M. Person, E. Wehtje, P. Adlercreutz, “Immobilisation of lipases by adsorption and deposition: high protein loading gives lower water activity optimum”, Biotechnol Lett. 22 (2000), 1571–1575.
[9] C. M. F. Soares, H. F. Castro, F. F. Moraes, G. M. Zanin, “Characterization and utilization of Candida rugosa lipase immobilized on controlled pore silica”, Appl. Biochem. Biotechnol. 77 (1999), 745-757.
[10] M. Miranda, M. L. C. P. Silva, H. F. de Castro “Optimised immobilisation of microbial lipase on hydrous niobium oxide”, J. Chem. Technol. Biotechnol, 81 (2006), 566-572.
[11] C. M. F. Soares, O. A Santos, J. E. Olivo, H. F. Castro, F. F. Moraes, G. M. Zanin, “Influence of the alkyl-substituted silane precursor on sol–gel encapsulated lipase activity”, J. Mol. Catal. B: Enzym. 29 (2004), 69-79.
[12] M. T. Reetz, “Lipases as practical biocatalysts”, Curr. Opin. Chem. Biol. 6 (2002), 145-150.
[13] W. A. M. Alloue, M. Agouedo, J. Destain, H. Ghalft, C. Blecker, J-P. Wathelet, P. Thonart, “Les lipases immobilisées et leurs applications “, Biotechnol. Agron. Soc. Environ, 12 (2008), 57-68.
[14] P. C. M. Da Rós, G. A. M. Silva, A. A. Mendes, J. C. Santos, H. F. de Castro, “Evaluation of the catalytic properties of Burkholderia cepacia lipase immobilized on non-commercial matrices to be used in biodiesel synthesis from different feedstocks”, Bioresource Technology, 101 (2010), 5508–5516.
[15] X. Zou, C. F. Chen, H. F. Hang, J. Chu, Y. P. Zhuang, S. L. Zhang, “Response Surface Methodology for optimization of the erythromycin production by fed-batch fermentation using an inexpensive biological nitrogen source”, Chem. Biochem. Eng, 24 (2010), 95-100.
[16] S. F Cheng, S. W. Chang, Y. H. Yen, C. J. Hsieh, “Optimum immobilization of Candida rugosa lipase on Celite by RSM”, Applied Clay Science, 37 (2007), 67-73.
[17] R. E Wrolstad, “Anthocyanins”, In F. J. Francis, G. J. Lauro, Eds. New York: Natural Food Colorants, (2000), 237-252.
[18] R. Bovara, G. O. Carrea, G. Ottolina, S. Riva, “Effects of water activity on Vmax and Km of lipase catalyzed transesterification in organic media”, Biotechnology Letters, 15(1993): 937-942.
[19] H. Ghamgui, N. Miled, M. Karra-chaabouni, Y. Gargouri, “Immobilization studies and biochemical properties of free and immobilized Rhizopus oryzae lipase onto CaCO3: A comparative study”, Biochemical Engineering Journal, 37 (2007), 34-41.
[20] A. Hiol, M. D. Jonzo, N. Rugani, D. Druet, L. Sarda, L. C. Comeau, “Purification and characterization of an extracellular lipase from a thermophilic Rhizopus oryzae strain isolated from palm fruit”, Enzyme Microb. Technol, 26 (2000), 421-430.
[21] S. Montero, A. Blanco, M. D. Virto, L. C. Landeta, I. Agud, R. Solozabal, ”Immobilization of Candida rugosa lipase and some properties of the immobilized enzyme”, Enzyme Microb. Technol, 15 (1993) 239-247.
[22] Y. Gao, T. Tian-Wei, N. F. Kai-Li, “Wang Immobilization of lipase on macroporous resin and its application in synthesis of biodiesel in low aqueous media”, Chin J Biotech, 22 (2006), 114-118.
[23] C. Calgaroto, R. P. Scherer, S. Calgaroto, J. V. Oliveira, D. de Oliveira, S. B. C. Pergher “Immobilization of porcine pancreatic lipase in zeolite MCM 22 with different Si/Al ratios”,Applied Catalysis A: General 394, (2011) 101–104.
Cite This Article
  • APA Style

    Djossou Andriano Jospin, Mazou Mouaïmine, Tchobo Fidèle Paul, Toukourou Akanho Chakirou, Blin Joel, et al. (2017). Optimum Immobilization of Candida Antartica B Lipase on Natural Silica by RSM. American Journal of Chemical Engineering, 5(3), 43-48. https://doi.org/10.11648/j.ajche.20170503.13

    Copy | Download

    ACS Style

    Djossou Andriano Jospin; Mazou Mouaïmine; Tchobo Fidèle Paul; Toukourou Akanho Chakirou; Blin Joel, et al. Optimum Immobilization of Candida Antartica B Lipase on Natural Silica by RSM. Am. J. Chem. Eng. 2017, 5(3), 43-48. doi: 10.11648/j.ajche.20170503.13

    Copy | Download

    AMA Style

    Djossou Andriano Jospin, Mazou Mouaïmine, Tchobo Fidèle Paul, Toukourou Akanho Chakirou, Blin Joel, et al. Optimum Immobilization of Candida Antartica B Lipase on Natural Silica by RSM. Am J Chem Eng. 2017;5(3):43-48. doi: 10.11648/j.ajche.20170503.13

    Copy | Download

  • @article{10.11648/j.ajche.20170503.13,
      author = {Djossou Andriano Jospin and Mazou Mouaïmine and Tchobo Fidèle Paul and Toukourou Akanho Chakirou and Blin Joel and Yao Kouassi Benjamin and Soumanou Mansourou Mohamed},
      title = {Optimum Immobilization of Candida Antartica B Lipase on Natural Silica by RSM},
      journal = {American Journal of Chemical Engineering},
      volume = {5},
      number = {3},
      pages = {43-48},
      doi = {10.11648/j.ajche.20170503.13},
      url = {https://doi.org/10.11648/j.ajche.20170503.13},
      eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ajche.20170503.13},
      abstract = {The immobilization of the lipase of Candida antartica B (LCAB) by adsorption on a natural silica support carried out to develop the adsorbent local supports. Immobilization conditions and characterization of the immobilized enzyme were investigated. Response surface methodology (RSM) and 3-level–3-factor fractional factorial design were employed to evaluate the effects of immobilization parameters, such as immobilization time (5-25 hour), immobilization temperature (25-45°C), and enzyme/support ratio (0.1-0.5, w/w), on yield of lipase immobilization on the support. The optimum immobilization conditions were as follows: immobilization time 18 hours, immobilization temperature 20°C, and enzyme / support ratio 0.5 (w/w); with a yield immobilization of 56,13 mg / g. The immobilization lipase shows hydrolytic and synthesis satisfactory activity.},
     year = {2017}
    }
    

    Copy | Download

  • TY  - JOUR
    T1  - Optimum Immobilization of Candida Antartica B Lipase on Natural Silica by RSM
    AU  - Djossou Andriano Jospin
    AU  - Mazou Mouaïmine
    AU  - Tchobo Fidèle Paul
    AU  - Toukourou Akanho Chakirou
    AU  - Blin Joel
    AU  - Yao Kouassi Benjamin
    AU  - Soumanou Mansourou Mohamed
    Y1  - 2017/05/23
    PY  - 2017
    N1  - https://doi.org/10.11648/j.ajche.20170503.13
    DO  - 10.11648/j.ajche.20170503.13
    T2  - American Journal of Chemical Engineering
    JF  - American Journal of Chemical Engineering
    JO  - American Journal of Chemical Engineering
    SP  - 43
    EP  - 48
    PB  - Science Publishing Group
    SN  - 2330-8613
    UR  - https://doi.org/10.11648/j.ajche.20170503.13
    AB  - The immobilization of the lipase of Candida antartica B (LCAB) by adsorption on a natural silica support carried out to develop the adsorbent local supports. Immobilization conditions and characterization of the immobilized enzyme were investigated. Response surface methodology (RSM) and 3-level–3-factor fractional factorial design were employed to evaluate the effects of immobilization parameters, such as immobilization time (5-25 hour), immobilization temperature (25-45°C), and enzyme/support ratio (0.1-0.5, w/w), on yield of lipase immobilization on the support. The optimum immobilization conditions were as follows: immobilization time 18 hours, immobilization temperature 20°C, and enzyme / support ratio 0.5 (w/w); with a yield immobilization of 56,13 mg / g. The immobilization lipase shows hydrolytic and synthesis satisfactory activity.
    VL  - 5
    IS  - 3
    ER  - 

    Copy | Download

Author Information
  • Unit of Research in Enzymatic and Food Engineering (URGEA), Polytechnic School of Abomey-Calavi (EPAC), Cotonou, Bénin

  • Unit of Research in Enzymatic and Food Engineering (URGEA), Polytechnic School of Abomey-Calavi (EPAC), Cotonou, Bénin

  • Laboratory of Energy and Applied Mechanics (LEMA), Polytechnic School of Abomey-Calavi (EPAC), Cotonou, Bénin

  • Mixed Unit of Research Engineering of Agropolymères and Emergent Technologies, (UMRIATE / CIRAD), Montpellier, France

  • Laboratory of Industrial Processes, of Synthesis, of Environment and New Energies, Yamoussoukro, C?te d’Ivoire

  • Unit of Research in Enzymatic and Food Engineering (URGEA), Polytechnic School of Abomey-Calavi (EPAC), Cotonou, Bénin

  • Sections