Thermostability of skimmilk with modified casein/whey protein content

Patocka, G.; Jelen, P.; Kaláb, Miloslav

doi:10.1016/0958-6946(93)90074-a

Cited by 22 publications

(12 citation statements)

References 11 publications

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“…Several commercial dairy-based products are being developed by modifying the casein:whey protein (C:W) ratio of milk, using whey proteins as ingredients (Jelen, 1992). The manipulation of the C:W ratio in milk influences its heat stability (Singh and Fox, 1987;Patocka et al,1993), but little is known about the effects of this modification on heat-induced aggregation of whey proteins. Heating casein micelles below 140 °C has little effect on their stability and stucture (Fox, 1982).…”

Section: Introductionmentioning

confidence: 99%

Thermal Aggregation of Whey Proteins in Model Solutions as Affected by Casein/Whey Protein Ratios

Beaulieu

Pouliot

1999

Journal of Food Science

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Model solutions (32.5 g protein/L) prepared from milk, ultrafiltration permeate, and whey protein isolate were adjusted at pH 6.7 to casein:whey protein (C:W) ratios of 80:20, 60:40, 40:60, 20:80, and 0:100. Heating was performed in test tubes at 95 °C for 5 min. Observations of the heated suspensions revealed the occurrence of heterogeneous particulates from the existing casein micelles complexed with denatured whey proteins and from aggregates essentially consisting of denatured whey proteins. The proportion of whey protein aggregates increased as C:W was changed from 80:20 to 20:80. The results from this study confirmed that heat-induced aggregates were formed not only from casein micelles but also from heat-denatured whey proteins.

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Section: Introductionmentioning

confidence: 99%

Thermal Aggregation of Whey Proteins in Model Solutions as Affected by Casein/Whey Protein Ratios

Beaulieu

Pouliot

1999

Journal of Food Science

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“…Combined aggregates of whey proteins and caseins show higher heat stability than whey protein aggregates. In fact, a solution of acid whey protein prepared by ultrafiltration, containing around 3.2% (w/w) protein, gelled immediately when heated at 93°C; however, a blend of whey protein and caseins, in the proportion 1:1 and heated under the same conditions was stable for up to 30 min of heating at 93°C, i.e., at least 97% of the total protein initially present in solution were still soluble after heating (Patocka, Jelen, & Kalab, 1993). It is generally accepted that this is due to a chaperone-like activity of the caseins.…”

Section: Introductionmentioning

confidence: 99%

Isolation and characterisation of κ-casein/whey protein particles from heated milk protein concentrate and role of κ-casein in whey protein aggregation

Gaspard

Auty

Kelly

et al. 2017

International Dairy Journal

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“…Indeed, there are numerous reports of kinetics studies on the thermal denaturation of major whey proteins (Anema and McKenna, 1996;Dannenberg and Kessler, 1988;Hillier and Lyster, 1979;Oldfield et al, 1998;Park and Lund, 1984;Sawyer et al, 1971), while few of them focused on the effect of casein. And if the effect of casein on fouling is desired, different proportions of casein/whey should be concerned (Kessler and Beyer, 1991;Patocka et al, 1993). In this paper, reconstituted whey protein isolate (WPI) solutions at 0.5 wt% with various casein protein concentrations to have different Casein/WPI proportions were used as model fluids.…”

Section: Introductionmentioning

confidence: 99%

Effect of casein/whey ratio on the thermal denaturation of whey proteins and subsequent fouling in a plate heat exchanger

Liu

Chen

Jeantet

et al. 2021

Journal of Food Engineering

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Dairy fouling is a ubiquitous problem in food processing, however, the fouling mechanism is not fully understood and investigations arose mainly from experiments with model systems that contained only whey proteins, typically reconstituted from whey protein isolate powder (WPI). The effect of casein on fouling has been rarely considered despite it is the major component of milk proteins. To fill this gap, whey protein-based model fluids containing different casein concentrations and fixed content of added calcium were prepared, leading to various Casein/WPI mass ratios. The effect of Casein/WPI on β-lactoglobulin (BLG) denaturation at molecular level and subsequent fouling behavior in the pilot-scale plate heat exchanger during pasteurization treatment was investigated. It was shown that Casein/WPI significantly affects the fouling behavior: at low Casein/WPI, fouling mass dropped dramatically until a minimum value was reached located at Casein/WPI of 0.2. While at higher Casein/ WPI, fouling mass increased with elevated Casein/WPI. Element mapping of the fouling layer also reveals that different structures and fouling mechanisms occur depending on Casein/WPI ratio. Finally, it was established that contrary to WPI solutions, BLG thermal denaturation is poorly correlated to decrease/extent of fouling for casein protein-based solutions showing that the presence of casein deeply modifies mineral and protein interactions and fouling build-up.

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Thermostability of skimmilk with modified casein/whey protein content

Cited by 22 publications

References 11 publications

Thermal Aggregation of Whey Proteins in Model Solutions as Affected by Casein/Whey Protein Ratios

Thermal Aggregation of Whey Proteins in Model Solutions as Affected by Casein/Whey Protein Ratios

Isolation and characterisation of κ-casein/whey protein particles from heated milk protein concentrate and role of κ-casein in whey protein aggregation

Effect of casein/whey ratio on the thermal denaturation of whey proteins and subsequent fouling in a plate heat exchanger

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