Research ArticleOpen AccessGoogle Scholar indexed
Optimization of Penicillin G Acylase Immobilization Process by Surface Response Methodology Using Central Composite Design
Pilot Biotechnology Department, Pasteur Institute of Iran, Tehran, Iran
Pilot Biotechnology Department, Pasteur Institute of Iran, Tehran, Iran
Physiology and Pharmacology Department, Pasteur Institute of Iran, Tehran, Iran
Pilot Biotechnology Department, Pasteur Institute of Iran, Tehran, Iran
Physiology and Pharmacology Department, Pasteur Institute of Iran, Tehran, Iran
Pilot Biotechnology Department, Pasteur Institute of Iran, Tehran, Iran
Pilot Biotechnology Department, Pasteur Institute of Iran, Tehran, Iran
- 1 Pilot Biotechnology Department, Pasteur Institute of Iran, Tehran, Iran
- 2 Pilot Biotechnology Department, Pasteur Institute of Iran, Tehran, Iran
- 3 Physiology and Pharmacology Department, Pasteur Institute of Iran, Tehran, Iran
- 4 Pilot Biotechnology Department, Pasteur Institute of Iran, Tehran, Iran
- 5 Physiology and Pharmacology Department, Pasteur Institute of Iran, Tehran, Iran
- 6 Pilot Biotechnology Department, Pasteur Institute of Iran, Tehran, Iran
- 7 Pilot Biotechnology Department, Pasteur Institute of Iran, Tehran, Iran
Copy link · social · email
Abstract
Penicillin G acylase was immobilized onto superparamagnetite iron oxide nanoparticles employing response surface methodology through central composite design. Polynomial quadratic model was selected as a model. The value of the determination coefficient (R 2 ) calculated from the quadratic regression model was 0.845, while the value of the adjusted (R 2 ) was 0.74. The regression analysis of the data showed that the quadratic model selected were appropriate thereby enzyme concentration (A), reaction temperature (D), enzyme concentration * reaction temperature (AD), quadratics enzyme concentration (A 2 ) and reaction temperature (D 2 ) were found to be significant factors in immobilization process of penicillin G acylase.
KeywordsQuadratic ModelSignificantEnzyme ConcentrationTemperature of the Adsorption
- A. S. M. Chong and X. S. Zhao, “Design of Large Pore Mesoporous Material for Immobilization of Penicillin G Acylase Biocatalysts,” Catalysis Today, Vol. 93-95, No. 1, 2004, pp. 293-299. doi:10.1016/j.cattod.2004.06.064
- D. A. Cecchini, I. Sera, D. Ubiali, M. Terreni and A. M. Albertini, “New Active Site Oriented Glyoxyl-Agarose Derivatives of E. coli Penicillin G Acylase,” BMC Biotechnology, Vol. 7, No. 1, 2007, pp. 54-67. doi:10.1186/1472-6750-7-54
- F. Scaramozzino, I. Estruch, P. Rossolillo, M. Terreni and A. M. Albertini, “Improvement of Catalytic Properties of E. coli Penicillin G Acylase on Glyoxyl Agarose by Addition of a Six Amino Acid Tag,” Journal of Applied and Environmental Microbiology, Vol. 71, No. 12, 2005, pp. 8937-8940.
- W. S. Adriano, E. H. C. Filho, J. A. Silva, R. L. C. Giordano and R. B. Goncalves, “Optimization of Penicillin G Acylase Multipoint Immobilization onto Glutaraldehyde—Chitosan Beads,” Biotechnology and Applied Biochemistry, Vol. 41, No. 3, 2005, pp. 201-207. doi:10.1042/BA20040061
- D. Norouzian, S. Javadpour, N. Moazami and A. Akbarzadeh, “Immobilization of Whole Cell Penicillin G Acylase in Gelatin Open Pore Matrix,” Enzyme and Microbial Technology, Vol. 30, No. 1, 2002, pp. 26-29.
- J. Zhao, Y. Wang, G. Luo and S. Zhu, “Immobilization of Penicillin G Acylase on Macro-Mesoporous Silica Sphers,” Bioresource Technology, Vol. 102, No. 2, 2011, pp. 529-535. doi:10.1016/j.biortech.2010.09.076
- R. V. Bahulekar, A. A. Prabhune, H. SivaRaman and S. Ponrathnams, “Immobilization of Penicillin G Acylase on Functionalized Macroporous Polymer Beads,” Polymer, Vol. 34, No. 1, 1993, pp. 163-166. doi:10.1016/0032-3861(93)90300-Y
- J. Huang, X. Lih, Y. Zheng, Y. Zhong, R. Zhao, X. Gao and H. Yan, “Immobilization of of Penicillin G Acylase on Poly[(Glycidyl Methacrylate)-co-(Glycerol Monomethacrylate)]—Grafted Magnetic Microspheres,” Macromolecular Bioscience, Vol. 8, No. 6, 2008, pp. 508-515.
- F. N. Crespilho, R. M. Lost, S. A. Tavarian and O. N. Oliveira, “Enzyme Immobilization on Ag Nanoparticles/Polyaniline Nanocomposite,” Biosensors and Bioelectronics, Vol. 24, No. 10, 2009, pp. 3072-3077. doi:10.1016/j.bios.2009.03.026
- B. Gao, X. Wang and Y. Shen, “Studies on Characters of Immobilizing Penicillin G Acylase on a Novel Composite Support,” Biochemical Engineering Journal, Vol. 28, No. 2, 2006, pp. 140-147. doi:10.1016/j.bej.2005.10.007
- G. K. Kouassi, J. Lrudayaraj and G. McCarty, “Examination of Cholesterol Oxidase Attachment to Magnetic Nanoparticles,” Journal of Nanobiotechnology, Vol. 3, No. 1, 2005, pp. 1-9. doi:10.1186/1477-3155-3-1