Denaturation of plant proteins. I

By denaturation of potato albumin by pyridine or by heat the viscosity increases; simultaneously the capability of the denatured protein t o reduce iodine increases, which, according to Anson, is due to the liberation of SH groups. A similar increase of viscosity was observed by the conversion of legumin into a water‐soluble modification, and further by heating the solution of this protein; the volume of iodine required for oxidation of the denatured protein is greater than that of the native legumin. This denatured protein can be reconverted into its native state, whereupon the reducing capacity again decreases. Several fractions of green pen and horse bean legumin were denatured by urea and it was found that the viscosity and the reducing capacity thereby increase. In the case of legumelin the viscosity is low but the reducing power high; this indicates that legumelin is a degradation product having globular molecules.