Covalent immobilization and characterization of Rhizopus oryzae lipase on core-shell cobalt ferrite nanoparticles for biodiesel production

doi:10.1016/j.cjche.2020.11.003

中国化学工程学报 ›› 2021, Vol. 37 ›› Issue (9): 128-136.DOI: 10.1016/j.cjche.2020.11.003

• Biotechnology and Bioengineering • 上一篇下一篇

Covalent immobilization and characterization of Rhizopus oryzae lipase on core-shell cobalt ferrite nanoparticles for biodiesel production

Saboura Ashkevarian^1,2, Jalil Badraghi¹, Fatemeh Mamashli², Behdad Delavari², Ali Akbar Saboury^2,3

1. Research Institute of Applied Sciences, ACECR, Shahid Beheshti University, Tehran, Iran;
2. Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran;
3. Center of Excellence in Biothermodynamics, University of Tehran, Tehran, Iran

收稿日期:2020-03-26 修回日期:2020-11-03 出版日期:2021-09-28 发布日期:2021-11-02
通讯作者: Jalil Badraghi, Ali Akbar Saboury
基金资助:
The work, originated from a Ph.D. thesis, was financially supported by Research Institute of Applied Science (RIAS) ACECR, Institute of Biochemistry and Biophysics (IBB) and Iran National Science Foundation (INSF).

Covalent immobilization and characterization of Rhizopus oryzae lipase on core-shell cobalt ferrite nanoparticles for biodiesel production

Saboura Ashkevarian^1,2, Jalil Badraghi¹, Fatemeh Mamashli², Behdad Delavari², Ali Akbar Saboury^2,3

1. Research Institute of Applied Sciences, ACECR, Shahid Beheshti University, Tehran, Iran;
2. Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran;
3. Center of Excellence in Biothermodynamics, University of Tehran, Tehran, Iran

Received:2020-03-26 Revised:2020-11-03 Online:2021-09-28 Published:2021-11-02
Contact: Jalil Badraghi, Ali Akbar Saboury
Supported by:
The work, originated from a Ph.D. thesis, was financially supported by Research Institute of Applied Science (RIAS) ACECR, Institute of Biochemistry and Biophysics (IBB) and Iran National Science Foundation (INSF).

摘要/Abstract

摘要： Rhizopus oryzae lipase (ROL) was immobilized on the surface of silica coated amino modified CoFe₂O₄ nanoparticles and applied for biodiesel production. The results indicated more affinity of the ROL toward its substrate upon immobilization, as revealed by a lower K_m value for the immobilized ROL compared to its free counterpart. Intrinsic fluorescence spectroscopy indicated a lower intensity for ROL immobilized on CoFe₂O₄ nanoparticles. Besides, immobilized ROL steady state anisotropy measurements presented lower values, which implied assembly of ROL molecules on magnetic nanoparticles upon immobilization as well as their restricted rotation upon covalent attachment. Thermal stability analysis revealed improved activity at higher temperatures for the immobilized enzyme compared to its free counterpart. Accordingly, Pace analysis to determine protein thermal stability revealed preservation of the protein conformation in the presence of increasing temperatures upon immobilization on nanoparticles. Finally, ROL immobilized on CoFe₂O₄ nanoparticles exhibited improved efficiency of biodiesel production in agreement with thermal activity profile. Therefore, the authors suggest application of the lipase molecules immobilized on CoFe₂O₄ nanoparticles for more efficient biodiesel production.

关键词: Lipase immobilization, CoFe₂O₄ magnetic nanoparticles, Steady state anisotropy, Biodiesel, Biocatalysis, Protein stability

Abstract: Rhizopus oryzae lipase (ROL) was immobilized on the surface of silica coated amino modified CoFe₂O₄ nanoparticles and applied for biodiesel production. The results indicated more affinity of the ROL toward its substrate upon immobilization, as revealed by a lower K_m value for the immobilized ROL compared to its free counterpart. Intrinsic fluorescence spectroscopy indicated a lower intensity for ROL immobilized on CoFe₂O₄ nanoparticles. Besides, immobilized ROL steady state anisotropy measurements presented lower values, which implied assembly of ROL molecules on magnetic nanoparticles upon immobilization as well as their restricted rotation upon covalent attachment. Thermal stability analysis revealed improved activity at higher temperatures for the immobilized enzyme compared to its free counterpart. Accordingly, Pace analysis to determine protein thermal stability revealed preservation of the protein conformation in the presence of increasing temperatures upon immobilization on nanoparticles. Finally, ROL immobilized on CoFe₂O₄ nanoparticles exhibited improved efficiency of biodiesel production in agreement with thermal activity profile. Therefore, the authors suggest application of the lipase molecules immobilized on CoFe₂O₄ nanoparticles for more efficient biodiesel production.

Key words: Lipase immobilization, CoFe₂O₄ magnetic nanoparticles, Steady state anisotropy, Biodiesel, Biocatalysis, Protein stability

Saboura Ashkevarian, Jalil Badraghi, Fatemeh Mamashli, Behdad Delavari, Ali Akbar Saboury. Covalent immobilization and characterization of Rhizopus oryzae lipase on core-shell cobalt ferrite nanoparticles for biodiesel production[J]. 中国化学工程学报, 2021, 37(9): 128-136.

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Covalent immobilization and characterization of Rhizopus oryzae lipase on core-shell cobalt ferrite nanoparticles for biodiesel production

Covalent immobilization and characterization of Rhizopus oryzae lipase on core-shell cobalt ferrite nanoparticles for biodiesel production

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