Immobilization of Lysozyme on Biomass Charcoal Powder Derived from Plant Biomass Wastes
Affiliation(s)
Department of Applied Chemistry, Tokyo Metropolitan University, Tokyo, Japan. EEN Co., Ltd., Tokyo, Japan.
Department of Applied Chemistry, Tokyo Metropolitan University, Tokyo, Japan. EEN Co., Ltd., Tokyo, Japan.
ABSTRACT
Biomass charcoal powder (BCP) was used as a carrier matrix for immobilization of chicken egg white lysozyme. BCP was derived from plant biomass wastes such as dumped adzuki beans by pyrolysis without combustion under nitrogen atmosphere and grinding with a jet mill. The amount of lysozyme immobilized on BCP of adzuki beans by adsorption was 11 μmol/g (0.16 g/g) at pH 7.0. The optimum pH values for free and immobilized lysozyme activities were 6.8 and 7.2, respectively. The optimum temperature for both free and immobilized lysozyme activities was 25℃. The half-life of immobilized lysozyme exhibited 1.8-fold compared to that of free lysozyme at 5℃. Moreover, the half life of immobilized lysozyme was 7 times greater than that of lysozyme at 90℃.
Biomass charcoal powder (BCP) was used as a carrier matrix for immobilization of chicken egg white lysozyme. BCP was derived from plant biomass wastes such as dumped adzuki beans by pyrolysis without combustion under nitrogen atmosphere and grinding with a jet mill. The amount of lysozyme immobilized on BCP of adzuki beans by adsorption was 11 μmol/g (0.16 g/g) at pH 7.0. The optimum pH values for free and immobilized lysozyme activities were 6.8 and 7.2, respectively. The optimum temperature for both free and immobilized lysozyme activities was 25℃. The half-life of immobilized lysozyme exhibited 1.8-fold compared to that of free lysozyme at 5℃. Moreover, the half life of immobilized lysozyme was 7 times greater than that of lysozyme at 90℃.
Cite this paper
H. Noritomi, R. Ishiyama, R. Kai, D. Iwai, M. Tanaka and S. Kato, "Immobilization of Lysozyme on Biomass Charcoal Powder Derived from Plant Biomass Wastes," Journal of Biomaterials and Nanobiotechnology, Vol. 3 No. 4, 2012, pp. 446-451. doi: 10.4236/jbnb.2012.34045.
H. Noritomi, R. Ishiyama, R. Kai, D. Iwai, M. Tanaka and S. Kato, "Immobilization of Lysozyme on Biomass Charcoal Powder Derived from Plant Biomass Wastes," Journal of Biomaterials and Nanobiotechnology, Vol. 3 No. 4, 2012, pp. 446-451. doi: 10.4236/jbnb.2012.34045.
References
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[1] C. Mateo, J. M. Palomo, G. Fernandez-Lorente, J. M. Guisan and R. Fernandez-Lorente, “Improvement of Enzyme Activity, Stability and Selectivity via Immobilization Techniques,” Enzyme and Microbial Technology, Vol. 40, No. 6, 2007, pp. 1451-1463. doi:10.1016/j.enzmictec.2007.01.018 [2] M. M. M. Elnashar, “Review Article: Immobilized Molecules Using Biomaterials and Nanobiotechnology,” Journal of Biomaterials and Nano-biotechnology, Vol. 1, No. 1, 2010, pp. 61-77. doi:10.4236/jbnb.2010.11008 [3] L. H. Noszko′, A. Bo′ta, A′. Simay and L. G. Nagy, “Preparation of Activated Carbon from the By-Products of Agricultural Industry,” Periodica Polytechnica, Vol. 28, 1984, pp. 293-297. [4] J. Rivera-Utrilla, E. Ultera-Hidalgo, M. A. Ferro-Garcia and C. Mereno-Castilla, “Comparison of Activated Carbons Prepared from Agricultural Raw Materials and Spanish Lignites When Removing Chlorophenols from Aqueous Solution,” Carbon, Vol. 29, No. 4-5, 1991, pp. 613-619. doi:10.1016/0008-6223(91)90128-6 [5] A. Cross and S. P. Sohi, “The Priming Potential of Biochar Products in Relation to Labile Carbon Contents and Soil Organic Matter Status,” Soil Biology & Biochemistry, Vol. 43, No. 10, 2011, pp. 2127-2134. doi:10.1016/j.soilbio.2011.06.016 [6] P. Jollès, “Lysozymes: Model Enzymes in Biochemistry and Biology,” 1st Edition, Birkhauser Verlag, Basel, 1996. [7] B. H. Ragatz, D. K. Werth and J. F. Bonner Jr., “Factors Influencing the Rate of an Enzyme Catalyzed Reaction: A Student Laboratory Experiment,” Biochemical Education, Vol. 12, No. 2, 1984, pp. 60-64. doi:10.1016/0307-4412(84)90004-9 [8] H. Yano, M. Kiyama and K. Ueno, “Physical Properties Comparison and Functional Evaluation Examination of Charcoals,” Kumamotoken Hoken Kankyo Kagaku Kenkyushoho, Vol. 33, 2004, pp. 70-72. [9] M. F. Chaplin and C. Bucke, “Enzyme Technology,” Cambridge University Press, Cambridge, 1990. [10] D. B. Volkin and A. M. Klibanov, “Minimizing Protein Inactivation,” In: T. E. Creighton, Ed., Protein Function: Practical Approach, IRL Press, Oxford, 1989, pp. 1-24. [11] H. Noritomi, K. Minamisawa, R. Kamiya and S. Kato, “Thermal Stability of Proteins in the Presence of Aprotic Ionic Liquids,” Journal of Biomedical Science and Engineering, Vol. 4, No. 2, 2011, pp. 94-99. doi:10.4236/jbise.2011.42013