Physical and Chemical Interactions in Cold Gelation of Food Proteins

Alting, Arno C.; Jongh, H.H.J. de; Visschers, Ronald W.; Simons, J. W.

doi:10.1021/jf011657m

Cited by 139 publications

(87 citation statements)

References 25 publications

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“…Cold-set gelation is a 2-step process, in which the Wrst step involves unfolding of the protein (usually done by heating at a relatively low salt concentration) and the second step consists either of lowering the pH [13] or addition of salts. In case of the latter, mainly NaCl and CaCl 2 were studied with regard to cold-set gelation [14][15][16][17][18].…”

Section: Introductionmentioning

confidence: 99%

Impact of protein pre-treatment conditions on the iron encapsulation efficiency of whey protein cold-set gel particles

Martin¹,

Jong²

2012

Eur Food Res Technol

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This paper investigates the possibility for iron fortiWcation of food using protein gel particles in which iron is entrapped using cold-set gelation. The aim is to optimize the iron encapsulation eYciency of whey protein by giving the whey protein diVerent heat treatment prior to gelation with iron. The eVect of the heat treatment conditions (mild-intermediate-severe) on the iron-induced coldset gelation process was studied to optimize the gel strength in relation to the iron concentration. Rheology was used to study the protein gel formation, and the stability of the gel particles and iron encapsulation eYciency was determined by measuring the protein and iron content at diVerent pH. Both the iron concentration and the heat treatment conditions appear to aVect the gel formation process and gel strength of the iron-induced cold-set gels. With the protein gel particles being stable at a broad pH range, the release of iron from the particles was studied as a function of time. The low release of iron at neutral pH indicated good encapsulation eYciency and capability of whey protein to keep iron bound. At low pH the release of iron increased, as is desired for bio-accessibility. In addition to diVerences in gel strength, the most relevant result caused by the pretreatment of the whey protein is revealed in the amount of iron that can be entrapped per protein. It is shown that the amount of iron can be increased going from mild to severe heat treatment conditions. This suggests that the concept of using whey protein particles with iron can eVectively be used to fortify food products with iron for human consumption.

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Section: Introductionmentioning

confidence: 99%

Impact of protein pre-treatment conditions on the iron encapsulation efficiency of whey protein cold-set gel particles

Martin¹,

Jong²

2012

Eur Food Res Technol

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“…25,38 Subsequently, intra-particle disulfide bonds are formed, leading to a covalent stabilisation of the structure. [39][40][41] The sum of all these interactions explains the remarkable stability of the whey protein microgels against physical treatments such as spray drying and homogenization. Further measurements by UV/VIS spectrophotometry revealed that only about 6.2% of the total protein content were released from the microgels at pH 2.0, 6.0 or 8.0, confirming that the cross-linking density within the WPM was high.…”

mentioning

confidence: 99%

Internal structure and colloidal behaviour of covalent whey protein microgels obtained by heat treatment

et al. 2010

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Covalently cross-linked whey protein microgels (WPM) were produced without the use of a chemical cross-linking agent. The hierarchical structure of WPM is formed by a complex interplay of heat denaturation, aggregation, electrostatic repulsion, and formation of disulfide bonds. Therefore, welldefined spherical particles with a diameter of several hundreds of nanometers and with relatively low polydispersity are formed in a narrow pH regime (5.8-6.2) only. WPM production was carried out on large scale by heating a protein solution in a plate-plate heat exchanger. Thereafter, the microgels were concentrated by microfiltration and spray dried into a powder. The spherical structure of the WPM was conserved in the powder. After re-dispersion, the microgel dispersions fully recovered their initial structure and size distribution. Due to the formation of disulfide bonds the particles were internally covalently cross-linked and were remarkably stable in a large pH range. Because of the pH dependent charge of the constituents the particles underwent significant size changes upon shifting the pH. Small angle X-ray scattering experiments were used to reveal their internal structure, and we report on the pH-induced structural changes occurring on different length scale. Our experiments showed that close analogies could be drawn to internally cross-linked and pH-responsive microgels based on weak polyelectrolytes. WPM also exhibited a pronounced swelling at pH values below the isoelectric point (IEP), and a collapse at the IEP. However, in contrast to classical microgels, WPM are not build up by simple polymer chains but possess a complex hierarchical structure consisting of strands formed by clusters of aggregated denatured proteins that act as primary building blocks. They were flexible enough to respond to changes of the environment, and were stable enough to tolerate pH values where the proteins were highly charged and the strands were stretched.

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“…A similar pattern was observed for the other two factors considered (pH, PI). Porcine plasma protein has been shown to exhibit high hydrophilic character compared with dairy or meat proteins (Alting et al, 2002;Howell & Lawrie, 1984;Zayas, 1985). PPP has been used to substitute STP and caseinate in frankfurters, where it was found that neither moisture nor WHC, as well as cooking losses showed significant differences (Hurtado et al, 2012).…”

Section: Significant Effectsmentioning

confidence: 99%

Plackett-Burman Experimental Design for Investigating the Effect of Porcine Plasma Protein, Trehalose and Bovine Meat Protein Isolate on Cook Yield and Texture of Minced Bovine Meat

Vareltzis¹,

Petridis²,

Petropoulou³

et al. 2013

JFR

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A common additive to counter the cooking losses considerations in the muscle food industry is sodium tripolyphosphate (STP), which however may pose health risk for certain segments of the population. This paper employs a Plackett-Burman design to investigate the effect of porcine plasma protein (PPP), protein isolate from bovine meat (PI), trehalose and pH of the additive mixture on cook yield and textural characteristics of minced beef during frozen storage. Results show that PI and PPP significantly (p < 0.05) increase the cooking yield throughout the storage period compared to the control sample. Fresh samples with PPP, PI and STP had ~90% cooking yield, while control sample had only 75%. PI and PPP can improve the cooking yield of minced beef for the first two months of storage by at least 20%, in a similar and comparable pattern with STP. Upon optimization the optimal values were achieved at PI concentration 2.3-5.0% and PPP levels 1.7-4.7%.

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Physical and Chemical Interactions in Cold Gelation of Food Proteins

Cited by 139 publications

References 25 publications

Impact of protein pre-treatment conditions on the iron encapsulation efficiency of whey protein cold-set gel particles

Impact of protein pre-treatment conditions on the iron encapsulation efficiency of whey protein cold-set gel particles

Internal structure and colloidal behaviour of covalent whey protein microgels obtained by heat treatment

Plackett-Burman Experimental Design for Investigating the Effect of Porcine Plasma Protein, Trehalose and Bovine Meat Protein Isolate on Cook Yield and Texture of Minced Bovine Meat

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