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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

has been cited by the following article:

• TITLE: Immobilization of Lysozyme on Biomass Charcoal Powder Derived from Plant Biomass Wastes

  AUTHORS: Hidetaka Noritomi, Reona Ishiyama, Ryotaro Kai, Daiki Iwai, Masahiko Tanaka, Satoru Kato

  KEYWORDS: Immobilization; Biomass Charcoal Powder; Lysozyme; Activity; Stability

  JOURNAL NAME: Journal of Biomaterials and Nanobiotechnology, Vol.3 No.4, October 31, 2012

  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℃.