PHYTATE CONCENTRATION IN WHEATweight less than 30,000 (the cut-off point in the ultrafiltration experiments of Knuckles et al., 1975) since it is absent in the diafiltered reteníate. This same impurity is also noncoagulable from neutral or alkaline solutions since it is absent in the heat coagulated protein of Edwards et al. (1975) (see Table II).Reducing agents, such as sodium bisulfite and 2-mercaptoethanol, are frequently used when attempting to isolate soluble active enzymes and undenatured protein fractions (Anderson and Rowan, 1967; Wolf, 1972). In attempting to improve the solubility of the protein precipitated at room temperature, several reducing agents were added to the CBJ (before precipitation) at the following levels: sodium bisulfite, 0.156 M; sodium dithionite, 0.078 M; and mercaptoethanol, 0.40 M. The samples were precipitated and washed at pH 3.5 at room temperature, and the protein reslurried in pH 8.5 borate buffer (0.1 M) for 1 hr. There was no increase in solubility when using the reducing agents compared to the untreated control. In related work, Betschart (1974) reported that mercaptoethanol was ineffective in increasing the solubility of freeze-dried, acid-precipitated alfalfa protein.By acid precipitating the alfalfa protein at 2°, the native solubility is preserved. This protein concentrate, being free from the dark green color and most of the grassy flavor of the typical LPC, and still retaining its native solubility, should have many uses in the food industry. The protein can be further purified by membrane filtration if necessary.

Figure 3. Tetrasaccharides (nystose and fructosylraffinose) in developing cereal grains.maltotriose were present in triticales in very small amounts only, which was unexpected because of the reported high -amylase activity in these grains. It is postulated that any starch degradation due to -amylase activity is minimal. It is unlikely that kernel shriveling in triticale is a result of -amylase degradation of starch.

No abstract

No abstract

No abstract