Incompatibility of amylose and amylopectin in aqueous solution
β Scribed by Monica T. Kalichevsky; Stephen G. Ring
- Publisher
- Elsevier Science
- Year
- 1987
- Tongue
- English
- Weight
- 373 KB
- Volume
- 162
- Category
- Article
- ISSN
- 0008-6215
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Tlie ability of periodate-oxidized amylose to form aggregates in aqueous solution was studied by sedimentation, light scattering, and viscosity analyses. Ultracentrifuge schlieren patterns show that aggregation can be appreciable at pH 3.0 and 1.0. The hydroxyl ion-catalyzed degradation of the oxidi
Two amylose samples, amylose V (DP, = 2300) and amylose HE 15 (a low-substituted hydroxyethylamylose, DP, = 1600) were studied. The intrinsic viscosity of the polymers in aqueous solution was measured with regard to its dependence on the alkalinity (0 to SMNaOH), the ionic strength (0 to 5 M , and t