THE COAGULABLE PROTEIN OF SWEET WORT*

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Abstract
The protein isolated from sweet wort by Hopkins, Amphlett and Berridge and described by them (this Journ., 1941, 106) has been investigated further. Its most out standing feature is its susceptibility to calcium salts, in presence of which it is coagulated at much greater rates than in salt-free solution. It also binds calcium. Coagulation is greatly accelerated by the first small quantities of coagulum to be formed, and initial precipitation is facilitated by surface activity and by calcium, which reduce the lag period. The lower the value of pH the more rapidly does coagulation take place. Maximum turbidity is given at pH 3.8, but turbidity is reduced by the presence of salts, including those of calcium, over the range of pH 3–5. Precipitates and coagula contain nucleic acid, the proportions of which tend to increase with fall in pH. This nucleic acid is responsible for the formation of turbidity and may be associated with the sensitivity of the protein complex to calcium.

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