A J Wolnowa

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The reaction of dialdehyde starch with casein and field-bean globulin leads to a blocking of the protein amino groups and to a decrease of free lysine, arginine and histidine. Maximum values are reached at high protein concentrations and great molar reagent excess. At best 80-93% of the amino groups or of the available lysine may be blocked in this way. For(More)
The authors deal with chemical and physico-chemical changes in casein and vegetable globulins after reaction with aldehydes or acylation with carboxylic acid chlorides and anhydrides. The stepwise blocking of the alpha- and epsilon-amino groups leads to modified proteins with lowered isoelectric points and changes in the solubility and precipitability(More)
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