1984
DOI: 10.3168/jds.s0022-0302(84)81630-6
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Effect of Processing on Whey Protein Functionality

Abstract: Journal of Dairy Science 67 (1984) 2723-2733. doi:10.3168/jds.S0022-0302(84)81630-6Received by publisher: 1983-08-22Harvest Date: 2016-01-04 12:20:07DOI: 10.3168/jds.S0022-0302(84)81630-6Page Range: 2723-273

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Cited by 128 publications
(98 citation statements)
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“…lactose and ions) by applying diafiltration did not improve the rheological characteristics of the gels. These results contradict the findings of other authors (34,45), who referred to diafiltration as a good method for improving gel hardness and cohesiveness due to the elimination of lactose. However, the higher protein mass fractions used by them (10 %), as opposed to 7 % in this research, may justify the differences, since the protein interaction in the former case can be more effective.…”
Section: Rheological Properties Of the Thermal Gelscontrasting
confidence: 57%
“…lactose and ions) by applying diafiltration did not improve the rheological characteristics of the gels. These results contradict the findings of other authors (34,45), who referred to diafiltration as a good method for improving gel hardness and cohesiveness due to the elimination of lactose. However, the higher protein mass fractions used by them (10 %), as opposed to 7 % in this research, may justify the differences, since the protein interaction in the former case can be more effective.…”
Section: Rheological Properties Of the Thermal Gelscontrasting
confidence: 57%
“…Foam capacity was inversely related to molecular flexibility in terms of the number of disulfide bonds per unit molecular weight (63). Schmidt et al (15) has confirmed that reducing agents decrease foamability of WPC, while oxidizing agents increase it. Hansen and Black Q4) have demonstrated the existence of an optimal level of oxidation beyond which foaming properties deteriorate.…”
Section: Foamingmentioning
confidence: 81%
“…In general, stable foams occur near the isoelectric point of the protein where electrostatic repulsion is minimal (£©. Thus, compositional factors that minimize protein aggregation and increase solubility in the isoelectric range (for example decreased calcium levels) result in improved foaming properties (15). Phillips et al (67) examined the effects of milk proteins on the foaming properties of egg white to identify foam depressant components present in whey and milk powders.…”
Section: Foamingmentioning
confidence: 99%
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“…Exact nature/role of calcium/␤-lactoglobulin interaction is not clear though significant interaction between calcium and free sulfhydryl groups have been reported in whey proteins (Schmidt et al, 1984). Haque and Kinsella (1988) around 70˚C; limited exposure started around 50˚C.…”
mentioning
confidence: 99%