Effect of Processing on Whey Protein Functionality

Schmidt, Ronald H.; Packard, V. S.; Morris, Howard A.

doi:10.3168/jds.s0022-0302(84)81630-6

Cited by 128 publications

(98 citation statements)

References 45 publications

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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%

Liquid Whey Protein Concentrates Produced by Ultrafiltration as Primary Raw Materials for Thermal Dairy Gels

Henriques

Gomes

Pereira

2017

Food Technol. Biotechnol.

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SummaryThe aim of this work is to study the gelation properties of liquid whey protein concentrates (LWPC) produced by ultrafiltration (UF) as raw material for thermally induced gels intended for food applications. LWPC thermal gelation was performed using different types of LWPC (non--defatted, defatted and diafiltered) of different protein mass fractions and pH. Most of the produced gels showed viscoelastic behaviour. Non-defatted LWPC gave stronger heat-induced gels with a more cohesive microstructure, a higher water holding capacity and also higher elastic modulus (G') and viscous modulus (G''). Gel properties were not improved in products with lower content of non-protein compounds. As expected, the increase in protein mass fraction positively influences protein interactions. However, the pH is responsible for the equilibrium between attraction and repulsion forces in the gel components that influence gel hardness and water holding capacity.

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Section: Rheological Properties Of the Thermal Gelscontrasting

confidence: 57%

Liquid Whey Protein Concentrates Produced by Ultrafiltration as Primary Raw Materials for Thermal Dairy Gels

Henriques

Gomes

Pereira

2017

Food Technol. Biotechnol.

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“…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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Relationship of Composition to Protein Functionality

Fligner

Mangino

1991

ACS Symposium Series

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Proteins are responsible for many of the desirable attributes associated with food products. Performance results from the interactions of proteins with other proteins or food components. Food proteins are commonly composed of several fractions, often having different properties. Thus, a particular functional property may be a manifestation of a specific component of the food protein used. Functionality has been defined as "any property of a food or food ingredient, except its nutritional ones, that affects its utilization" (1). The domain of physical functions associated with the presence of proteins in a food system typically includes: (a) increased hydration and water binding which affect viscosity and gelation, (b) modification of surface tension and interfacial activity which control emulsification and foaming ability and (c) chemical reactivity leading to altered states of cohesion/adhesion and a potential for texturization. Functional properties are influenced by intrinsic factors, such as composition, conformation and homogeneity of the protein source, as well as by processing methods and environmental conditions (2). There are several specific papers that relate protein structure to function (1-5). Reports that relate composition to function are rare. This chapter will discuss the effects of compositional factors of proteins, with emphasis on whey proteins, on gelation, foaming and emulsification. Composition encompasses certain physicochemical properties such as, hydrophobicity and sulfhydryl content, as well as specific ratios of protein components, ratios of protein to other constituents, such as lipid, carbohydrate and mineral components and the presence of other components in the food product including added emulsifiers. GelationProtein gelation is a two stage-process involving an initial denaturation or unfolding of protein molecules followed by subsequent aggregation. Gel formation can occur when protein-protein interactions lead to the formation of a three-dimensional network capable of entraining water molecules. A balance between the attractive forces necessary to form a network and the repulsive forces necessary to prevent its collapse is

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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%

Influence of Cation Sequestering and pH on Quiescent Thermal Association of .BETA.-Lacto-globulin NB from Fresh Cheddar Whey: An Insight into Gelation Mechanism.

Haque

Sharma

2002

FSTR

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Freshly fractionated ␤-lactoglobulin AB (␤-Lg) from Cheddar whey was dispersed at pH 3.5, 7, and 9 buffers containing 20 mM EDTA, and circulated at 25˚C through a closed loop containing a 200 nm pore size membrane, to remove traces of dust and large aggregates, and an water jacketed cuvette placed within a Dynamic Light Scattering (DLS) device for real-time data acquisition. Filtered samples were step-wise heated from 25˚C to 90˚C with continuous data acquisition to study dynamic changes in mean aggregate diameter (MAD). Data were analyzed by cumulant method for apparent MAD and CONTIN for size distribution. Initial MAD (IMAD) of about 200 nm, reflecting the pore size of the filter used, was observed for all experiments prior to heating. Mid-range aggregate, Agg3 (100-599 nm), was ubiquitous in all distributions and Agg1 (monomer-dimer) was only seen at pH 7 and 25˚C. Increased temperatures gave rise to larger aggregates (>micron) (Agg4 and 5) with concomitant disappearance of Agg3. The greatest increase in MAD was at pH 3.5 and the lowest was at pH 9. Pre-gelation (<70˚C) kinetic rates were 4.29, 1.53, and -0.11¥ ¥ ¥ ¥10 -4 s -1 for pH 3.5, 7.0, and 9.0, respectively, giving MADs that were 3.5, 2.2 and 0.8 fold compared to IMAD. Above 70˚C (apparent gelation range), relative aggregate enlargement was greatest at pH 3.5 being 55, 21, and 4.2 fold of IMAD, respectively, for pH 3.5, 7, and 9 at 90˚C. An apparent gel formed at pH 3.5 and a turbid gel/coagulum formed at pH 7 and none at pH 9. It is conceivable that increased association at pre-gelation temperatures is required for gelation. A mechanism has been postulated.

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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

Cited by 128 publications

References 45 publications

Liquid Whey Protein Concentrates Produced by Ultrafiltration as Primary Raw Materials for Thermal Dairy Gels

Liquid Whey Protein Concentrates Produced by Ultrafiltration as Primary Raw Materials for Thermal Dairy Gels

Relationship of Composition to Protein Functionality

Influence of Cation Sequestering and pH on Quiescent Thermal Association of .BETA.-Lacto-globulin NB from Fresh Cheddar Whey: An Insight into Gelation Mechanism.

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