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Functional properties of enzymatically modified buffalo milk protein products [electronic resource].

By:

Hassan, Z. M. R

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Language: English Summary language: Arabic Description: p.551 -563Other title:

الخواص الوظيفية لمستحضرات بروتينات اللبن الجاموسي المعدلة انزيميا [Added title page title]

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Annals of agricultural science, 2002 v. 47 (2) [electronic resource].

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In: Annals of Agricultural Science 2002.v.47(2)Summary: Buffalo milk protein products (Total milk proteinate (TMP), casein-co- precipitate, acid casein) were enzymatically modified using Maxrien enzyme. The chemical composition was determind and some properties (solubility, emulsion activity, foam expansion, buffer capacity, viscosity and freezing point) of these products were investigated at different rates of hydrolysis. The TMP possessed the lowest ash & moisture with highest lactose and protein contents compared to the other protein products. The enzymatic hydrolysis up to eight h markedly improved the protein solubility while the changes were slight after that The pattern of electrophoresis showed that casein-co-precipitate was more resistant to hydrolysis than total milk proteinate or acid casein. Foam expansion of milk protein products was enhanced by the enzymatic modification being increased with increasing the time of hydrolysis. At zero time the acid casein showed the lowest foam expansion compared to the other two products.

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Buffalo milk protein products (Total milk proteinate (TMP), casein-co- precipitate, acid casein) were enzymatically modified using Maxrien enzyme. The chemical composition was determind and some properties (solubility, emulsion activity, foam expansion, buffer capacity, viscosity and freezing point) of these products were investigated at different rates of hydrolysis. The TMP possessed the lowest ash & moisture with highest lactose and protein contents compared to the other protein products. The enzymatic hydrolysis up to eight h markedly improved the protein solubility while the changes were slight after that The pattern of electrophoresis showed that casein-co-precipitate was more resistant to hydrolysis than total milk proteinate or acid casein. Foam expansion of milk protein products was enhanced by the enzymatic modification being increased with increasing the time of hydrolysis. At zero time the acid casein showed the lowest foam expansion compared to the other two products.

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