Nutrition

Download Functionality of Proteins in Food by Joseph F. Zayas PDF

By Joseph F. Zayas

The booklet is dedicated to increasing present perspectives on protein performance in nutrients platforms. a radical account of practical homes of meals proteins and their amendment by means of protein resource, environmental elements and processing stipulations are supplied. the writer describes intimately the real dating among protein affirmation, physico-chemical and sensible houses. precise recognition is given to the impact of protein performance on nutrients caliber, foodstuff creation and comparable not pricey facets and to using quite a few proteins for making improvements to latest and designing new nutrients products.

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Extra info for Functionality of Proteins in Food

Sample text

When radiation-crosslinked peptides were hydrolyzed, amino acid dimers with unique properties not normally observed in foods were obtained [61]. Schuessler and Schilling [62] reported that a combination of irradiation and high oxygen pressure resulted in extensive protein chain scission. The main effect of 10 kGy irradiation on myoglobin studied after treatment and after post-irradiation frozen storage was aggregation and protein precipitation [63]. Myoglobin retention increased with a decrease in pH from 7 to 5 and with the presence of propyl gallate (PG).

Pasteurization and sterilization may change structure and properties of milk whey proteins, either reversibly or irreversibly. , ~-lactoglobulins are very sensitive to heat denaturtion and caseins are highly stable. De Wit and Klarenbeek [90] reported the effect of whey protein denaturation on their functional performance in different foods. 6 is used to recover heatdenatured whey proteins. The functionality and utilization of whey proteins as functional ingredients is limited by the extent of protein denaturation.

2% in untreated soy protein. Enzymatic deamidation with alcalase affected the solubility of soy proteins [113]. 2% for two various conditions of hydrolysis. The pH-solubility profile of deamidated soy protein hydrolysates at a 2% degree of hydrolysis was similar to the hydrolyzed controls, but at a 4% degree of hydrolysis was considerably greater than their respective controls. Structural changes of soy proteins during deamidation caused changes in solubility. The introduction of SH groups (thiolation) into food proteins was said to modify and improve their functionality [I 14].

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