Albumin, globulin, and prolamin fractions were extracted from corn meal in water, .5 M NaCl, and 50% (vol/vol) 1-propanol and examined by SDS-PAGE and densitometric scanning to investigate fractional degradation rates of corn proteins. Several protein fractions were identified for globulins, zein prolamins, and glutelins. Ruminal degradability of individual subfractions was evaluated by suspension of corn and corn gluten meal samples in the rumen of lactating dairy cows from 0 to 72 h. Electrophoretic and densitometric analysis of protein residues revealed that the prolamin fraction zein for corn and corn gluten meal was more resistant to ruminal degradation than albumins, globulins, and glutelins. Relative rates of degradation of zein and the fraction containing albumins, globulins, and glutelins were .060, .026, and .018, .015/h for corn and corn gluten meal, respectively. Total degradabilities of corn and corn gluten meal, measured by summation of degradability of subfractional components, were 52.2 and 18.6%. Quantitative measurement of ruminally degradable subfractions and estimation of their degradation rates by electrophoretic and densitometric scanning are useful in understanding ruminal degradability of corn proteins.

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Two wild and eight domesticated cultivars of finger millet were analyzed to determine their proximate composition and calcium, iron, and amino acid content. Wide variations were observed in the protein (mean values ranged from 7.5 to 11.7%), calcium (376 to 515 mg/100 g), and iron (3.7 to 6.8 mg/100 g) content of the wild and domesticated cultivars. A wild progenitor of finger millet, E coracana subsp. africana was significantly higher in protein than four of the six domesticated accessions analyzed. The calcium and iron content of the wild progenitor was also significantly greater than that of two domesticated cultivars. The wild species was also found to be higher in lysine and five other essential amino acids. These results indicate that the nutritional value of finger millet may be significantly improved by selective crossbreeding of the cereal's wild and domesticated cultivars.

Aqueous solutions of natamycin and its beta-cyclodextrin (beta-CD), hydroxypropyl beta-cyclodextrin, and gamma-cyclodextrin (gamma-CD) inclusion complexes were completely degraded after 24 h of exposure to 1000 lx fluorescent lighting at 4 degrees C. After 14 days of storage in darkness at 4 degrees C, 92.2% of natamycin remained in active form. The natamycin:beta-CD complex and natamycin:gamma-CD complex were significantly more stable (p < 0.05) than natamycin in its free state in aqueous solutions stored in darkness at 4 degrees C. Clear poly(ethylene terephthalate) packaging with a UV light absorber allowed 85.0% of natamycin to remain after 14 days of storage under 1000 lx fluorescent lighting at 4 degrees C. Natamycin:cyclodextrin complexes can be dissociated for analysis in methanol/water/acetic acid, 60:40:5, v/v/v. Natamycin and its complexes in dissociated form were quantified by reverse phase HPLC with detection by photodiode array at 304 nm.

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