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Mateo, C., Palomo, J.M., Fernandez-Lorente, G., Guisan, J.M. and Fernandez-Lorente, R. (2007) Improvement of Enzyme Activity, Stability and Selectivity via Immobilization Techniques. Enzyme and Microbial Technology, 40, 1451-1463.
http://dx.doi.org/10.1016/j.enzmictec.2007.01.018

has been cited by the following article:

• TITLE: Heat-Resistant Properties of α-Chymotrypsin Adsorbed onto Biomass Charcoal Powder

  AUTHORS: Hidetaka Noritomi, Shunichi Kurihara, Nobuyuki Endo, Satoru Kato

  KEYWORDS: Adsorption, Biomass Charcoal Powder, α-Chymotrypsin, Activity, Thermal Stability

  JOURNAL NAME: Journal of Biomaterials and Nanobiotechnology, Vol.5 No.3, July 21, 2014

  ABSTRACT: Biomass charcoal powder (BCP) was used as a carrier for immobilization of α-chymotrypsin through adsorption. BCP was derived from plant biomass wastes such as dumped bamboos by oxygen-free pyrolysis at low temperatures and grinding with a jet mill. The activity of adsorbed α-chymotrypsin was strongly dependent upon the kind of BCP. The thermal denaturation curve of adsorbed α-chymotrypsin was shifted to high temperature, compared to that of free one. When α-chymotrypsin adsorbed onto BCP of bamboos was incubated at 45°C, the half-life of adsorbed α-chymotrypsin was 2.6 times greater than that of free one. After incubation at 45°C, the remaining activity of adsorbed α-chymotrypsin markedly depended on the kind of BCP.