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Study on Preparation of Immobilized Alkaline Protease and Its Performance

Received: 10 May 2017     Published: 10 May 2017
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Abstract

The nano-Fe3O4 particles were prepared by hydrothermal method. Cellulose-based magnetic Fe3O4 was prepared by adding cellulose solution dissolved in sodium hydroxide / thiourea / urea system. The basic protease was used as the catalyst and glutaraldehyde was used as the crosslinking agent, The production of magnetic recyclable immobilized enzyme can greatly reduce the cost of hydrolysis of sludge. The aldehyde groups in the glutaraldehyde and the amino groups in the protein can be stably crosslinked by coupling. The immobilization effect of nanometer Fe3O4 was reflected by investigating the activity of immobilized enzyme and immobilization rate of enzyme under different conditions.

Published in Modern Chemistry (Volume 5, Issue 3)
DOI 10.11648/j.mc.20170503.11
Page(s) 35-42
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

Nano Fe3O4, Glutaraldehyde, Immobilized Enzyme, Alkaline Protease

References
[1] Akhond, M., et al., Efficient Immobilization of Porcine Pancreatic alpha-Amylase on Amino-Functionalized Magnetite Nanoparticles: Characterization and Stability Evaluation of the Immobilized Enzyme. Appl Biochem Biotechnol, 2016. 180(5): p. 954-968.
[2] Amirbandeh, M. and A. Taheri-Kafrani, Immobilization of glucoamylase on triazine-functionalized Fe3O4/graphene oxide nanocomposite: Improved stability and reusability. Int J Biol Macromol, 2016. 93(Pt A): p. 1183-1191.
[3] Dutta, N., S. Biswas, and M. K. Saha, Nano-magnesium aided activity enhancement and biophysical characterization of a psychrophilic alpha-amylase immobilized on graphene oxide nanosupport. J Biosci Bioeng, 2017.
[4] He, L., et al., Functional expression of a novel alpha-amylase from Antarctic psychrotolerant fungus for baking industry and its magnetic immobilization. BMC Biotechnol, 2017. 17(1): p. 22.
[5] Hou, C., et al., Construction of enzyme immobilization system through metal-polyphenol assisted Fe3O4/chitosan hybrid microcapsules. Chemical Engineering Journal, 2016. 283: p. 397-403.
[6] Wu, Z.-C., et al., Removal of Cu(II) ions from aqueous water by l-arginine modifying magnetic chitosan. Colloids and Surfaces A: Physicochemical and Engineering Aspects, 2016. 499: p. 141-149.
[7] Hu, T.-G., et al., Immobilization of Alkaline Protease on Amino-Functionalized Magnetic Nanoparticles and Its Efficient Use for Preparation of Oat Polypeptides. Industrial & Engineering Chemistry Research, 2015. 54(17): p. 4689-4698.
[8] Ibrahim, A., et al., Detergent and solvent compatible alkaline protease nanobiocatalyst immobilized onto functionalized rattle type magnetic core mesoporous shell silica. New Biotechnology, 2016. 33: p. S105.
[9] Ibrahim, A. S., et al., Enhancement of Alkaline Protease Activity and Stability via Covalent Immobilization onto Hollow Core-Mesoporous Shell Silica Nanospheres. Int J Mol Sci, 2016. 17(2).
[10] Junoi, S., Y. Chisti, and N. Hansupalak, Optimal conditions for deproteinizing natural rubber using immobilized alkaline protease. Journal of Chemical Technology & Biotechnology, 2015. 90(1): p. 185-193.
[11] Li, G.-y., et al., Preparation and properties of magnetic Fe3O4–chitosan nanoparticles. Journal of Alloys and Compounds, 2008. 466(1-2): p. 451-456.
[12] Pylypchuk Ie, V., et al., Gd-DTPA Adsorption on Chitosan/Magnetite Nanocomposites. Nanoscale Res Lett, 2016. 11(1): p. 168.
[13] Ling, X. M., et al., Covalent Immobilization of Penicillin G Acylase onto Fe3O4 Chitosan Magnetic Nanoparticles. J Microbiol Biotechnol, 2016. 26(5): p. 829-36.
[14] Naghipour, A. and A. Fakhri, Efficient oxidation of sulfides into sulfoxides catalyzed by a chitosan–Schiff base complex of Cu(II) supported on supramagnetic Fe3O4 nanoparticles. Environmental Chemistry Letters, 2015. 14(2): p. 207-213.
[15] Prasertkittikul, S., Y. Chisti, and N. Hansupalak, Deproteinization of Natural Rubber Using Protease Immobilized on Epichlorohydrin Cross-linked Chitosan Beads. Industrial & Engineering Chemistry Research, 2013. 52(33): p. 11723-11731.
[16] Sahin, S., I. Ozmen, and E. Kir, Purification, immobilization, and characterization of protease from localBacillus subtilis M-11. Asia-Pacific Journal of Chemical Engineering, 2015. 10(2): p. 241-247.
[17] Wang, S.-n., et al., Immobilized alcalase alkaline protease on the magnetic chitosan nanoparticles used for soy protein isolate hydrolysis. European Food Research and Technology, 2014. 239(6): p. 1051-1059.
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    Yiming Li, Fei Xue, Dengxin Li. (2017). Study on Preparation of Immobilized Alkaline Protease and Its Performance. Modern Chemistry, 5(3), 35-42. https://doi.org/10.11648/j.mc.20170503.11

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    ACS Style

    Yiming Li; Fei Xue; Dengxin Li. Study on Preparation of Immobilized Alkaline Protease and Its Performance. Mod. Chem. 2017, 5(3), 35-42. doi: 10.11648/j.mc.20170503.11

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    AMA Style

    Yiming Li, Fei Xue, Dengxin Li. Study on Preparation of Immobilized Alkaline Protease and Its Performance. Mod Chem. 2017;5(3):35-42. doi: 10.11648/j.mc.20170503.11

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  • @article{10.11648/j.mc.20170503.11,
      author = {Yiming Li and Fei Xue and Dengxin Li},
      title = {Study on Preparation of Immobilized Alkaline Protease and Its Performance},
      journal = {Modern Chemistry},
      volume = {5},
      number = {3},
      pages = {35-42},
      doi = {10.11648/j.mc.20170503.11},
      url = {https://doi.org/10.11648/j.mc.20170503.11},
      eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.mc.20170503.11},
      abstract = {The nano-Fe3O4 particles were prepared by hydrothermal method. Cellulose-based magnetic Fe3O4 was prepared by adding cellulose solution dissolved in sodium hydroxide / thiourea / urea system. The basic protease was used as the catalyst and glutaraldehyde was used as the crosslinking agent, The production of magnetic recyclable immobilized enzyme can greatly reduce the cost of hydrolysis of sludge. The aldehyde groups in the glutaraldehyde and the amino groups in the protein can be stably crosslinked by coupling. The immobilization effect of nanometer Fe3O4 was reflected by investigating the activity of immobilized enzyme and immobilization rate of enzyme under different conditions.},
     year = {2017}
    }
    

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  • TY  - JOUR
    T1  - Study on Preparation of Immobilized Alkaline Protease and Its Performance
    AU  - Yiming Li
    AU  - Fei Xue
    AU  - Dengxin Li
    Y1  - 2017/05/10
    PY  - 2017
    N1  - https://doi.org/10.11648/j.mc.20170503.11
    DO  - 10.11648/j.mc.20170503.11
    T2  - Modern Chemistry
    JF  - Modern Chemistry
    JO  - Modern Chemistry
    SP  - 35
    EP  - 42
    PB  - Science Publishing Group
    SN  - 2329-180X
    UR  - https://doi.org/10.11648/j.mc.20170503.11
    AB  - The nano-Fe3O4 particles were prepared by hydrothermal method. Cellulose-based magnetic Fe3O4 was prepared by adding cellulose solution dissolved in sodium hydroxide / thiourea / urea system. The basic protease was used as the catalyst and glutaraldehyde was used as the crosslinking agent, The production of magnetic recyclable immobilized enzyme can greatly reduce the cost of hydrolysis of sludge. The aldehyde groups in the glutaraldehyde and the amino groups in the protein can be stably crosslinked by coupling. The immobilization effect of nanometer Fe3O4 was reflected by investigating the activity of immobilized enzyme and immobilization rate of enzyme under different conditions.
    VL  - 5
    IS  - 3
    ER  - 

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Author Information
  • College of Environmental Science and Engineering, Donghua University, Shanghai, China

  • College of Environmental Science and Engineering, Donghua University, Shanghai, China

  • College of Environmental Science and Engineering, Donghua University, Shanghai, China

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