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Salts of EDTA potentiate ascorbate in accelerating development of cured meat pigment both in myoglobin model systems and in laboratory prepared sausage. Iron EDTA is more effective than Na, EDTA or CaEDTA. Although EDTA salts stabilize ascorbates in nitrite solution and in buffered myoglobin solution, in the presence of nitrite plus myoglobin EDTA salts accelerate disappearance of ascorbate. This suggests that the rate limiting step in cured meat pigment synthesis is reduction of metmyoglobin to myoglobin and that EDTA salts catalyze the ascorbate reducing agent effect.

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is decomposed in the presence of the substrate and that the enzyme, now devoid of coenzyme, is susceptible to thermal inactivation. A case in point is rabbit muscle glyceraldehyde phosphate dehydrogenase, which Velick, Hayes, and Harting (77) have demonstrated to be very unstable at room temperature when deprived of the coenzyme, diphosphopyridine nucleotide, with which it is normally associated. Beevers (3) reported barley glutamic acid decarboxylase to be subject to thermal inactivation. The failure to observe the anomalous inactivation at pH 6.5 as opposed to lower pH in the absence of pyridoxal phosphate may also be explicable on the basis of the increased sensitivity of the enzyme to

The present and future nutritional rationale for margarine fortification is discussed. The trend to increase the polyunsaturated fat content of margarine coupled with the newer knowledge of vitamin E requirements suggest that vitamin E fortification of margarine be considered; a practice common in Europe. The composition of current margarine is reviewed with respect to PUFA and vitamin E. The vitamin A content, low cost, wide availability and high caloric value of margarine suggest a possible role in feeding the underprivileged. In this connection, the use of margarine as a carrier of lysine to improve the protein quality of cereal foods with which it is used is suggested.