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.
Highlights
Proteins are biomolecules of great importance in the medical, pharmaceutical, and food fields, since they exhibit their outstanding biological activities under mild condition
If proteins are steadily adsorbed on biomass charcoal powder (BCP), and the aggregation among unfolded proteins adsorbed on BCP is sufficiently hindered, it is expected that unfolded proteins adsorbed on BCP are refolded by cooling treatment, and the high remaining activity is obtained
The remaining activity of lysozyme adsorbed on BCP of adzuki bean dropped in the range from 70 ̊C to 98 ̊C, and still exhibited 3% at 98 ̊C. These results indicated that adsorbing lysozyme on BCP of adzuki bean effectively improved the thermal stability of lysozyme at high temperatures
Summary
Proteins are biomolecules of great importance in the medical, pharmaceutical, and food fields, since they exhibit their outstanding biological activities under mild condition. Several strategies have so far been proposed in order to prevent thermal denaturation of proteins They include chemical modification, immobilization, genetic modification, and addition of stabilizing agents. It has been reported that inorganic salts, polyols, sugars, amino acids, amino acid derivatives, chaotropic reagents, and water-miscible organic solvents are available for improving protein stability. These additives do not sufficiently prevent irreversible protein aggregation or some of them are no longer stable at high temperatures. We have focused on the remaining activity of proteins after heat treatment in order to address a question of whether or not adsorbing proteins on BCP affects the thermal stability of proteins in aqueous solutions. Chicken eggwhite lysozyme has been employed, since it is well investigated regarding its structure, properties, functions, and thermal stability [23,24,25]
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