The denaturational behaviour of bovine β-lactoglobulin B has been studied in solutions containing guanidine hydrochloride by differential scanning calorimetry. The experiments have shown that complete peaks of cold d...The denaturational behaviour of bovine β-lactoglobulin B has been studied in solutions containing guanidine hydrochloride by differential scanning calorimetry. The experiments have shown that complete peaks of cold denaturation can be recorded also in high concentration of protein solutions. The cold denaturation and the renaturation of the protein are reproducible, but the thermal denaturation is irreversible. The activation energy of thermal denaturation calculated is about 285 kJ/mol.展开更多
基金This project was supported by the National Natural Science Foundation of China
文摘The denaturational behaviour of bovine β-lactoglobulin B has been studied in solutions containing guanidine hydrochloride by differential scanning calorimetry. The experiments have shown that complete peaks of cold denaturation can be recorded also in high concentration of protein solutions. The cold denaturation and the renaturation of the protein are reproducible, but the thermal denaturation is irreversible. The activation energy of thermal denaturation calculated is about 285 kJ/mol.
