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Functional and nutritional properties of isolated bovine blood proteins
Author(s) -
Penteado Marilene De Vuono C.,
Lajolo Franco M.,
Santos Nilton Pereira Dos
Publication year - 1979
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740300811
Subject(s) - albumin , globulin , isoleucine , limiting , chemistry , methionine , globin , blood proteins , serum albumin , chromatography , bovine serum albumin , solubility , biochemistry , hemoglobin , amino acid , leucine , biology , endocrinology , organic chemistry , mechanical engineering , engineering
Various properties of freeze‐dried fractions of bovine blood have been compared. Dried whole plasma, albumin, globulin and globin showed high solubility from pH 3 to 8, but this fell sharply with plasma on storage at 40°C and Aw 0.32 or higher. Albumin showed the best foaming properties followed by plasma, globulin and globin. These proteins in 1 % solution were able to emulsify 60, 115, 70 and 45% of their volume of oil, respectively. Net protein ratios were 3.57 for globulin, 1.96 for albumin and negative for globin. Chemical scores indicated that methionine was the most limiting amino acid for globulin and albumin. Isoleucine was limiting for globin.