Journal
FOOD HYDROCOLLOIDS
Volume 23, Issue 3, Pages 973-979Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodhyd.2008.07.009
Keywords
Whey protein; Aggregation; Cold gelation; Disulphide bonds; Zeta potential
Categories
Funding
- Agropur cooperative
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Protein dispersions with different ratios of alpha-lactalbumin to beta-lactoglobulin were heat-denatured at pH 7.5 and then acidified With glucono-delta-lactone to form gels at room temperature. Heat treatment induced the formation of whey protein polymers with reactive thiol group concentrations ranging from I to 50 mu mol/g, depending on protein composition. During acidification, the first sign of aggregation occurred when the zeta potential reached -18.2 mV. Increasing the proportion of alpha-lactalbumin in the polymer dispersions resulted in more turbid gels characterized by an open microstructure. Elastic and viscous moduli were reduced, while the relaxation coefficient and the stress decay rate constants were increased by raising the proportion of alpha-lactalbumin in the gel. After one week of storage at 5 degrees C, gel hardness increased by 12%. The effect of protein composition on acid-induced gelation of whey protein is discussed in relation to the availability and reactivity of thiol groups during gel formation and storage. Crown Copyright (C) 2008 Published by Elsevier Ltd. All rights reserved.
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