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Volkin, D.B. and Klibanov, A.M. (1989) Minimizing protein inactivation. In: Creighton T.E. Ed., Protein function: practical approach, IRL Press, Oxford, 1-24.

has been cited by the following article:

• TITLE: Increase in thermal stability of proteins adsorbed on biomass charcoal powder prepared from plant biomass wastes

  AUTHORS: Hidetaka Noritomi, Ryotaro Kai, Daiki Iwai, Hirotaka Tanaka, Reo Kamiya, Masahiko Tanaka, Kohichiroh Muneki, Satoru Kato

  KEYWORDS: Adsorption; Biomass Charcoal Powder; Lysozyme; Refolding; Remaining Activity; Thermal Stability

  JOURNAL NAME: Journal of Biomedical Science and Engineering, Vol.4 No.11, November 17, 2011

  ABSTRACT: Thermal stability of lysozyme adsorbed on biomass charcoal powder (BCP), which was prepared from plant biomass wastes such as dumped adzuki bean, bamboo, and wood by pyrolysis without combustion under nitrogen atmosphere and comminution with a jet mill, was examined. Adsorbing lysozyme on BCP could sufficiently prevent proteins from denaturing and aggregating in an aqueous solution at high temperatures, and enhanced the refolding of thermally denatured proteins by cooling treatment. The remaining activities of lysozyme adsorbed on BCP of adzuki bean exhibited 51% by cooling treatment after the heat treatment at 90?C for 30 min, although that of native lysozyme was almost lost under the same experimental conditions. The thermostabilization effect of BCP on the remaining activity of adsorbed lysozyme was markedly dependent upon the kind of plant biomass wastes.