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 atmosph...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.展开更多
Thermal stability of lysozyme dissolved in aqueous solutions was examined in the presence of water-miscible aprotic ionic liquids consisting of 1-ethyl-3-methylimidazolium cation and several kinds of anions. Addition ...Thermal stability of lysozyme dissolved in aqueous solutions was examined in the presence of water-miscible aprotic ionic liquids consisting of 1-ethyl-3-methylimidazolium cation and several kinds of anions. Addition of ionic liquids to an aqueous solution containing lysozyme prevented unfolded proteins from aggregating irreversibly at high temperatures. The thermal denaturation curve of lysozyme with ionic liquids was entirely shifted to higher temperature, compared with that without ionic liquids. The remaining activity of lysozyme after the heat treatment was markedly dependent upon the kind and concentration of ionic liquids. The remaining activi-ties of lysozyme with 1.5 M 1-ethyl-3-methylimida-zolium tetrafluoroborate ([emim][BF4]) and 0.1 M 1-ethyl-3-methylimidazolium trifluoromethanesulfonate ([emim][Tf]) exhibited 88 and 68% after the heat treatment at 90oC for 30 min, respectively, although that without ionic liquids was perfectly lost.展开更多
文摘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.
文摘Thermal stability of lysozyme dissolved in aqueous solutions was examined in the presence of water-miscible aprotic ionic liquids consisting of 1-ethyl-3-methylimidazolium cation and several kinds of anions. Addition of ionic liquids to an aqueous solution containing lysozyme prevented unfolded proteins from aggregating irreversibly at high temperatures. The thermal denaturation curve of lysozyme with ionic liquids was entirely shifted to higher temperature, compared with that without ionic liquids. The remaining activity of lysozyme after the heat treatment was markedly dependent upon the kind and concentration of ionic liquids. The remaining activi-ties of lysozyme with 1.5 M 1-ethyl-3-methylimida-zolium tetrafluoroborate ([emim][BF4]) and 0.1 M 1-ethyl-3-methylimidazolium trifluoromethanesulfonate ([emim][Tf]) exhibited 88 and 68% after the heat treatment at 90oC for 30 min, respectively, although that without ionic liquids was perfectly lost.
