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Functional properties of legume proteins modified by estrification [electronic resource].

By:

Khalil, A.O

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Language: English Summary language: Arabic Description: p.927-945Other title:

الخصائص الوظيفية لبروتينات البقوليات المعدلة كيميائيا بالاسترة [Added title page title]

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Zagazig journal of agricultural research, 2008 v. 35 (4) [electronic resource].

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In: Zagazig Journal of Agricultural Research 2008.v.35(4)Summary: At three legume proteins i.e. soybean protein isolate (SPI), broad bean protein isolate (BPI) and chick pea protein isolate (CPI) were esterified to different extents with methanol, the esterified proteins were analysed for solubility, emulsifying and foaming properties at a pH range of 2-10. These functional properties were changed in the esterified proteins compared to the native ones. The magnitude of change depended on the extent of esterification and the nature of the modified protein. Emulsifying activity and stability of esterified legume proteins at the acidic pH-range of 2-6 were generally higher compared to the corresponding native proteins. The foam activity and stability at the pH-range 2-6 were generally higher compared to the corresponding native proteins. An improvement was associated with the degree of solubility, the enhanced degree of esterification and the nature of the used protein.

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At three legume proteins i.e. soybean protein isolate (SPI), broad bean protein isolate (BPI) and chick pea protein isolate (CPI) were esterified to different extents with methanol, the esterified proteins were analysed for solubility, emulsifying and foaming properties at a pH range of 2-10. These functional properties were changed in the esterified proteins compared to the native ones. The magnitude of change depended on the extent of esterification and the nature of the modified protein. Emulsifying activity and stability of esterified legume proteins at the acidic pH-range of 2-6 were generally higher compared to the corresponding native proteins. The foam activity and stability at the pH-range 2-6 were generally higher compared to the corresponding native proteins. An improvement was associated with the degree of solubility, the enhanced degree of esterification and the nature of the used protein.

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