Industrial whole animal blood. Characterization studies and quantitative protein removal by chemical coagulation

Vandegrift, Vaughn; Ratermann, A. L.

doi:10.1021/jf60226a066

Cited by 2 publications

(11 citation statements)

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“…The increased weight of the two complexes, coupled with the low values of nitrogen and coagulant ion composition, suggests significant contributions to the dry weight of the complexes by agents other than protein or metal ion. That this weight increase is not due to organic material is indicated by the comparable total organic carbon levels remaining in the centrates after treatment with any of the metal coagulants ( Vandegrift and Ratermann, 1979;Ratermann et al, 1980). Thus, the weight of complex produced per unit of blood may be affected by the amount of associated ion (e.g., Na+, C1-, or S O : -) removed from solution with the coagulant used.…”

Section: Resultsmentioning

confidence: 99%

“…Conventional methods of blood meal production include procedures, such as steam coagulation, vat drying, ring drying, and spray drying, that utilize large amounts of heat energy and may affect the quality of protein in the meal (Waibel et al, 1977;Kramer et al, 1978). As an alternative, we have proposed and investigated the use of chemical coagulants to effect protein removal from industrial animal blood (Vandegrift and Ratermann, 1979;Ratermann et al, 1980;Vandegrift et al, 1981). Our results have demonstrated that sodium polyphosphate, ferric chloride, aluminum sulfate, and zinc sulfate quantitatively remove protein from animal blood and that sodium lignosulfonate treatment results in near-quantitative protein removal, under specified conditions.…”

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confidence: 99%

“…Protein coagulation was effected by adding the coagulant as a solid (SPP) or as a solution (zinc sulfate, aluminum sulfate, ferric chloride) to diluted blood at the optimal pH and coagulant concentration previously described ( Vandegrift and Ratermann, 1979;Ratermann et al, 1980). Ferric sulfate was added as a 10% solution [9.5% Fe2(S0& plus 0.5% FeSO, to enhance solubility], whereas ferri-floc was added as a 10% slurry.…”

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confidence: 99%

“…By using standardized H2S04 to produce the optimum pH for complex formation (pH 3.5), it was possible to monitor the amount of PRA-1 actually present in the complex. The use of other acids for pH adjustment was precluded, since other acids altered the optimum conditions for coagulation previously characterized (Vandegrift and Ratermann, 1979).…”

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confidence: 99%

“…Control experiments, performed by using blood samples that differed only as to whether or not they had undergone freezing and thawing prior to coagulant treatment, dem-Department of Chemistry, Murray State University, Murray, Kentucky 42071. 0021-8561 /82/1430-0715$01.25/0 onstrated that freezing and thawing of blood did not alter the coagulant concentrations or pH conditions required to effect quantitative protein removal (Vandegrift and Ratermann, 1979). Storage at -20 °C for up to 3 months did not affect the quality of the blood.…”

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Characterization of coagulant-protein complexes produced by chemical coagulation of industrial whole animal blood

Jones¹,

Clark²,

Beale³

et al. 1982

J. Agric. Food Chem.

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Protein-coagulant complexes were prepared from industrial whole animal blood by using zinc sulfate, aluminum sulfate, ferric chloride, ferric sulfate, sodium polyphosphate, and sodium lignosulfonate, under conditions which resulted in quantitative removal of protein from the blood. The amount of coagulant found with protein in the complexes produced represented from about 80% (polyphosphate, lignosulfonate) to greater than 95% (zinc, aluminum, or iron ion) of input. The nitrogen and coagulant compositions of the aluminum sulfate and iron chloride generated complexes were significantly lower than expected compared to those of complexes generated by using zinc sulfate and ferric sulfate. Sodium lignosulfonate-protein complexes were characterized by a method using sulfur analysis, since nitrogen was found to be present in the commercial preparation used. The results demonstrate that all of the coagulant-protein complexes studied form under conditions that require only a small excess of coagulant and that the complexes contain low percentages of heavy metal ions or nutritionally beneficial (sodium polyphosphate) or nontoxic (sodium lignosulfonate) coagulants.

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Characterization of coagulant-protein complexes produced by chemical coagulation of industrial whole animal blood

Jones¹,

Clark²,

Beale³

et al. 1982

J. Agric. Food Chem.

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Chemical preservation of protein in industrial whole animal blood

Vandegrift¹,

Kirk²

1981

J. Agric. Food Chem.

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1(NOE) is -3.93 (Witanowski and Webb, 1973). The signal to noise (S/N) enhancement will be maximum if dipoledipole interactions dominate the relaxation mechanism. If the dipole-dipole interactions are not dominant, the NOE enhancement factor will range from 1 to -3.93, proportional to the magnitude of the dipole-dipole interactions' contribution to the relaxation mechanism. In general, a single bond dipole-dipole interaction gives rise to maximum NOE enhancement. In Figure 2, the a-and c-nitrogen would be expected to have identical intensities as they do in Figure 1. The a-nitrogen signal, however, is only half that of the c-nitrogen. The binding of lysine in the polymer may alter the importance of the various relaxation mechanisms. The c-nitrogen bound in the matrix has intramolecular dipole-dipole interactions, whereas the a-nitrogen has only the intermolecular interactions which are limited in the polymer. These NOE differences are useful for deducing structural changes but make quantitation difficult. Numerous other peaks occur downfield from the urea reference and probably are from urea substituted with methylene derived from formaldehyde. No assignments have been made yet, but one could speculate that the peaks occurring at 0.4 and 1.0 ppm are due to unsubstituted urea nitrogen resonances. The peaks between 4.9-5.6 and 18.7-20.6 ppm likewise could be assigned to mono-and disubstituted urea nitrogen resonances, respectively, since substitution of electron donors larger than methyl is known to cause downfield displacement of the nitrogen resonance in ureas and amines (Witanowski et al., 1973). ACKNOWLEDGMENT We gratefully acknowledge M. J. Albright and R. 0. Obenauf of JEOL, Cranford, NJ, for taking the 15N spectra on their instrument. LITERATURE CITED Amos, H. E.; Little, C. 0.; Digenis, G. A.; Schelling, G. T.; Tucker,

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Industrial whole animal blood. Characterization studies and quantitative protein removal by chemical coagulation

Cited by 2 publications

References 8 publications

Characterization of coagulant-protein complexes produced by chemical coagulation of industrial whole animal blood

Characterization of coagulant-protein complexes produced by chemical coagulation of industrial whole animal blood

Chemical preservation of protein in industrial whole animal blood

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