Publication | Closed Access
On the gelation of Vicia faba protein in dependence on the acetylation degree
12
Citations
4
References
1981
Year
Vicia Faba ProteinMolecular BiologyAnalytical UltracentrifugationChemical BiologyProtein SynthesisGelation DegreeProtein FoldingRheologyShear ModulusBiophysicsProtein ChemistryBiochemistryMathematical PlanningProtein BiosynthesisBiopolymer GelAcetylation DegreeNatural SciencesCellular BiochemistryMedicineCarbohydrate-protein Interaction
Abstract Using the method of mathematical planning of experiments and taking the shear modulus of the gels as an equivalent of the gelation degree, the conditions of the thermal denaturation at the maximum shear modulus were found to be T D ≈︁ 100 °C and t D ≈︁ 60 min for the non‐acetylated Vicia faba protein and T D ≈︁ 100 °C and t D ≈︁ 40 min for the acetylated Vicia faba protein. On these conditions the dependence of the shear modulus (G) on the protein concentration (C) is expressed by exponential functions G = α C4.3 and G = α C5.0, respectively. By an increasing acetylation of the Vicia faba protein the shear modulus, the thickness of the many‐line chains, and the net density of gels are increased; the same is valid for the shear modulus and the masking of disulfide groups by an increasing concentration of non‐acetylated and acetylated Vicia faba proteins.
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