Protein fractions and the effect of cooking on cowpea proteins [Sudan]
1996
Nugdallah, G.A. (University of Khartoum. Faculty of Agriculture, Shambat (Sudan))
Nine cowpea cultivars (Vigna imguiculata): H35-5, 524-B, CB-48, H8-14, H8-8, H8-9, CB-5, H14-10 and CB-46 obtained from Wad Medani Research Station were used in this study. The proximate analysis showed that the moisture content ranged from 7.0 to 7.7, ash content ranged from 3.7 to 4.2, fibre content ranged from 2.5 to 2.9, oil content ranged from 1.3 to 1.7 and protein content from 27.5 to 29.6. The nitrogen solubility of cowpea proteins were (85 at pH 10, 75 at pH 1) The minimum protein solubility of less than 20 were observed at isoelectric pH ranges (4-5) in distilled water. The nitrogen solubility (in the presence of 0.5M NaCl) of cowpea proteins were (98 at pH 10 and 85 at pH 1). Minimum protein solubility of less than 30 was observed at isoelectric pH ranges (4-5). Protein fractions for these cultivars were determined. The values for globulin ranged from 65.7 to 79.7, albumin from 4.0 to 12.3 prolamin from 1.4 to 4.0, G lower 1-glutelin from 0.9 to 3.0, G lower 2-glutelin from 1.4 to 4.0, G lower 3-glutelin from 9.0 to 14.0 and insoluble protein from 0.5 to 3.0. Two selected cultivars: H8-14 and CB-46 according to their albumin content were cooked in 150 ml of boiling distilled water under reflux for 40-45 min. The proteins were fractionated. Results indicated that albumin and globulin decreased significantly (P0.05) for both cultivars after cooking accompanied increase in G lower 3-glutelin fractions.
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