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Size Exclusion/HPLC of Heated Water Soluble Bovine and Porcine Muscle Proteins
Author(s) -
DAVIS CARL E.,
ANDERSON JOHN B.
Publication year - 1984
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.1365-2621.1984.tb12478.x
Subject(s) - high performance liquid chromatography , chemistry , chromatography , myoglobin , size exclusion chromatography , absorbance , solubility , biochemistry , enzyme , organic chemistry
Proteins (280 nm absorbance) in water extracts from bovine semi‐membranosus and porcine longissimiu were separated by size exclusion (SEC) high performance liquid chromatography(HPLC). SEC/HPLC profiles showed six heat sensitive fractions ≥ 10,000 daltons. These fractions ranged from peak 1 at 375,800 daltons in bovine and 170,000 daltons in porcine down to myoglobin, peak 6, at 15,200 and 19,500 daltons for bovine and porcine, respectively. SEC/HPLC showed the loss of certain peaks at specific time/temperature treatments. Heat labile porcine proteins ≥ 10,000 daltons represented about 41.5 area percent of the total extractable components after heating to 60°C. In bovine, this represented about 37.5 area percent. In both species, heating at 70°C for 30 min or at 75°C for 0 min resulted in protein solubility loss to about 1 area percent or less.