Functional Properties of Purified Vicilins from Cowpea ( Vigna unguiculata ) and Pea ( Pisum sativum ) and Cowpea Protein Isolate
✍ Scribed by Rangel, Alessandra; Domont, Gilberto B.; Pedrosa, Cristiana; Ferreira, Sérgio T.
- Book ID
- 120366347
- Publisher
- American Chemical Society
- Year
- 2003
- Tongue
- English
- Weight
- 93 KB
- Volume
- 51
- Category
- Article
- ISSN
- 0021-8561
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## Abstract The relationship of hydrophobicity and solubility with some functional properties of cowpea protein isolate was determined. Cowpea protein isolate was prepared by alkali extraction followed by precipitation at pH 4.5. The precipitated proteins were then neutralized to pH 7. Heating of t
A partially puriüed globulin from cowpea seeds was polymerised by calcium-independent microbial transglutaminase. The level of free amino groups in the globulin decreased with increase in enzyme concentration, suggesting that the cross-linking reaction involved participation of the amino residues. A