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Denaturation of Bovine Serum Albumin (BSA) and Ovalbumin by High Pressure, Heat and Chemicals
Author(s) -
HAYAKAWA ISAO,
KAJIHARA JUNKO,
MORIKAWA KEISUKE,
ODA MITSUHIKO,
FUJIO YUSAKU
Publication year - 1992
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1992.tb05478.x
Subject(s) - ovalbumin , denaturation (fissile materials) , chemistry , differential scanning calorimetry , bovine serum albumin , endothermic process , chromatography , electrophoresis , enthalpy , fluorescence , gel electrophoresis , polyacrylamide gel electrophoresis , serum albumin , biochemistry , nuclear chemistry , organic chemistry , biology , antigen , thermodynamics , genetics , physics , adsorption , quantum mechanics , enzyme
Both native and denatured protein samples were examined by determining fluorescence and specific rotation, and by polyacrylamide gel electrophoresis (PAGE) and differential scanning calorimetry (DSC). Denaturation of ovalbumin by pressure was much less than by heat or by the chemical denaturants. Ovalbumin was denatured under high pressure, as confirmed by the decrease in its a‐helical content to 72% and DSC endothermic enthalpy to 61%, but it showed no change in the PAGE pattern. With bovine serum albumin decrease in fluorescence was observed after denaturation by chemicals, but it did not change under high pressure.