‘Dry’, dialysed milk protein was stored for 6 months at 37° C. and 55% relative humidity alone and in the presence of small proportions of glucose, of high proportions of lactose and of sucrose, and of mixtures of these sugars.

The reducing sugars combined with free amino-groups of the protein, apparently in a 1:1 ratio; sucrose did not. The reaction did not proceed to completion, probably owing to difficulty of access of the reactive groups to one another. Only when the sugar-amino reaction occurred did discoloration ensue.

Glucose reacted more rapidly with the protein than did lactose, and the complex formed became discoloured and insoluble in both cold and hot water much more rapidly.

Sucrose and lactose both greatly delayed the onset of glucose-induced insolubility, lactose being the more efficient of the two. They did not prevent discoloration.

The protein alone became insoluble in cold but not in hot water after prolonged storage; but did not discolour. This change was prevented by sucrose. The behaviour of lactose was inconsistent, loss of solubility being accelerated in one experiment and retarded in another.