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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 28 (1980), S. 394-398 
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 52 (1987), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The interaction between condensed grape tannins and some proteins was studied turbidimetrically. Tannins precipitated protein efficiently at pH values up to the isoelectric point of the individual protein. At slightly higher pH values there was a sharp decrease in complex formation. This “critical pH” was usually observed within approximately 0.5 pH unit of the isoelectric point. A close correlation (r = 0.96) was obtained between the isoelectric point and the critical pH of proteins. The effects of pH and ionic strength on turbidity formation by tannins and bovine serum albumin showed that an increasing salt concentration tended to increase turbidity at pH 3, but it had no significant effect at pH 4. In contrast at pH 5 high salt concentration tended to decrease turbidity. Employing an ultrafiltration technique, the binding behavior of interacting tannin and protein was described by a typical Brunauer type II adsorption curve.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 50 (1985), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Condensed tannins from grapes immobilized on Sepharose 4B were found to have protein binding properties similar to tannins in free solution. Proteins bound to the gel at pH values below their individual isoelectric points and were eluted when the pH was increased. A good correlation was obtained between the isoelectric point and the elution pH for the following enzymes and proteins: alkaline phosphatase, ovalbumin, β-lactoglobulin, bovine serum albumin, α-amylase,γ-globulin, and cytochrome c. Trypsin represented an exception to the rule, α-Amylase retained enzymatic activity after elution from the gel.
    Type of Medium: Electronic Resource
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