Functional and Chemical Characteristics of Bovine Plasma Proteins Isolated as a Metaphosphate Complex

Etheridge, P.A.; Hickson, D. W.; Young, Charles R.; Landmann, W. A.; Dill, C. W.

doi:10.1111/j.1365-2621.1981.tb04484.x

Cited by 15 publications

(14 citation statements)

References 13 publications

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“…BLOOD COLLECTED from meat animals at slaughter has received considerable attention concerning its use as a food ingredient (Satterlee, 1981). Various collection and fractionation techniques have been used to produce both plasma-and red blood cell-based protein preparations (Tybor et al, 1973(Tybor et al, , 1975Donnelly and Delaney, 1977;Graham, 1978;Imeson et al, 1978;Danish Meat Research Institute 1980, 198 I;Etheridge et al, 1981). Plasma functionality has been studied in emulsions (Satterlee and Free, 1973;Tybor et al, 1973Tybor et al, , 1975Comer, 1979;Terre11 et al, 1979;Caldironi and Ockerman, 1982).…”

Section: Introductionmentioning

confidence: 99%

“…Plasma functionality has been studied in emulsions (Satterlee and Free, 1973;Tybor et al, 1973Tybor et al, , 1975Comer, 1979;Terre11 et al, 1979;Caldironi and Ockerman, 1982). foams (Tybor et al, 1975;Etheridge et al, 1981) and gels (Harper et al, 1978;Comer, 1979;Hickson et al, 1980Hickson et al, , 1982. Plasma has also been used as a meat binding agent (Suter et al, 1976;Seideman et al, 1979;Siegel et al, 1979;Howell and Lawrie, 1984).…”

Section: Introductionmentioning

confidence: 99%

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Effect of Heating Rate on Thermally Formed Myosin, Fibrinogen and Albumin Gels

Foegeding

Allen

Dayton

1986

Journal of Food Science

115

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Myosin, fibrinogen and albumin gels were formed by heating in pH 6.0 phosphate buffer at three heating rates. Turbidity (Ahben,,,) and solubility were monitored along with gel strength, as measured with an annular pump. Myosin and fibrinogen suspensions became turbid and solubility decreased as temperatures preceding the development of gel strength. Linearly increasing heating rates of I2"C/hr and 5O"Ci hr produced the strongest myosin and fibrinogen gels at 7O"C, whereas albumin gels formed at 95°C by heating at 12Whr or constant heating for 20 min did not differ in strength.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Effect of Heating Rate on Thermally Formed Myosin, Fibrinogen and Albumin Gels

Foegeding

Allen

Dayton

1986

Journal of Food Science

115

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“…The six isolates were lyophilized. Another isolate was prepared according to Etheridge et al (1981): sodium hexametaphosphate solution (0.6N) added to plasma at a 5:l ratio and pH adjusted to 4.4 with 3N HCl. The precipitate was separated like other isolates and the pH adjusted to 7.0 with 0.125N NaOH and lyophilized.…”

Section: Methodsmentioning

confidence: 99%

“…1980 Protein recovery was over 90% for all isolates except isolate HCl-NaOH pH 4.4 which was 65%. Etheridge et al (1981) reported a higher protein recovery (93%) and a lower phosphorus content (1.8%) for plasma isolate. Isolate HCl-NaOH pH 4.4 was prepared under the same conditions specified by Etheridge et al (1981) except for the centrifugation process which was not specified in their study.…”

Section: Gelationmentioning

confidence: 96%

Evaluation of Gelation and Solubility of Bovine Plasma Protein Isolates

King

Pablo

Montes

1989

Journal of Food Science

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Gelation and solubility of bovine plasma protein isolates prepared from liquid plasma using different acids (HCI, H3P04, H,SOJ and bases (NaOH, Na,CO,) were evaluated and compared to commercial plasma. Protein recovery was over 90%. Solubility at 1% (w/v) war low in pH range 4.0 to 5.5 but similar to commerical plasma in pF range 5.5 to 8.0 (pcO.01). All isolates gelled at a concentration o 6.0%. Only isolate H,P04-Na&O, and commercial plasma gelled at a minimum concentration of 4.0%. This concentration decreased to 2.4% for the same isolate when 0.025M Ca++ ion was added.

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“…There are only a few studies available on the foaming properties of whole blood plasma , Etheridge et al 1981, Hill and Hall 1987. Foaming capacity of blood plasma proteins was reported to be equivalent to that of egg albumen (Tybor et al 1975, Hill andHall 1987) and superior to those of casein, whey proteins, and soy isolate proteins (Hill and Hall 1987).…”

Section: Blood Plasma Proteinsmentioning

confidence: 99%

Functional and cake-baking properties of egg white, bovine blood plasma and their protein fractions

Raeker

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Human consumption of the plasma fraction of blood is well accepted in Canada, the Pacific Rim, and Western European countries (Johnson 1988). Plasma is added to meat products, such as sausages, frankfurters, beefburgers, extended ham, turkey breast and turkey franks, to increase protein levels and to increase fat-and water-holding capacities (Knipe 1988). Bread-baking properties of blood plasma protein isolate (PPI) were studied by Khan et al (1979). Loaf volume of bread made with 2-6% PPI was significantly higher than that of the control bread. However, increasing levels of PPI darkened crust and crumb colors and made the texture coarse and open. When 2% wheat flour was replaced with PPI, the bread protein and lysine content increased by 15 and 75%, respectively. Other commercial uses The major uses for animal blood are as animal feed, pet foods, and fertilizer (Bates et al 1974, Johnson 1988). Blood or blood derivatives are also used in various pharmaceutical applications (Gorbatov 1988) such as tissue and microbiological culture media, RH factor determination, and immunological preparations. Another use of blood is as a binding agent in waterproof glue, in radiator sealing compounds, and in plywood adhesives (Hirchberg, 1957). Blood Plasma Proteins Blood plasma contains a variety of proteins having different functions and structures. The major plasma proteins are classified as serum albumin, globulins. ''Mean values of two replicates, ± one standard deviation. ^'^^Means with the same letter within a column are not significantly different at the 0.05 level.

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Functional and Chemical Characteristics of Bovine Plasma Proteins Isolated as a Metaphosphate Complex

Cited by 15 publications

References 13 publications

Effect of Heating Rate on Thermally Formed Myosin, Fibrinogen and Albumin Gels

Effect of Heating Rate on Thermally Formed Myosin, Fibrinogen and Albumin Gels

Evaluation of Gelation and Solubility of Bovine Plasma Protein Isolates

Functional and cake-baking properties of egg white, bovine blood plasma and their protein fractions

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