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UTILIZATION OF SLAUGHTER PLANT WASTE PROTEINS: AN INVESTIGATION ON THE NATURE AND SOME FUNCTIONAL PROPERTIES OF BOVINE RUMEN TISSUE PROTEINS
Author(s) -
PERERA CONRAD O.,
ANGLEMIER ALLEN F.
Publication year - 1980
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.1365-2621.1980.tb04114.x
Subject(s) - tropomyosin , rumen , myosin , chemistry , solubility , biochemistry , actin , troponin , denaturation (fissile materials) , bovine serum albumin , myoglobin , skeletal muscle , albumin , chromatography , food science , biology , anatomy , organic chemistry , myocardial infarction , fermentation , nuclear chemistry , psychology , psychiatry
Bovine rumen and skeletal muscle proteins were studied and compared. Solubility studies indicated that about 90% of the rumen proteins could be extracted at pH 3 or 10, when the tissue was well homogenized. They were least soluble in the pH range 5‐6 (11 – 14%). Two protein isolates of distinct compositional differences were obtained from the pH 10 aqueous extract by successive lowering of pH to 7.0 and 5.4. The isolate at pH 7.0 contained predominantly actin and myosin, but no troponin and tropomyosin. Actin, myosin, troponin, and tropomyosin were completely precipitated at pH 5.4. The emulsifying capacity of the rumen proteins were about 30% lower than those of the skeletal muscle proteins; however, they had excellent solubility and consistency. Their whippability and foam stability were also superior to those of purified egg albumin.