Mixing whey and soy proteins: Consequences for the gel mechanical response and water holding

Jose, Jissy; Pouvreau, Laurice; Martin, A.H.

doi:10.1016/j.foodhyd.2016.03.031

Cited by 74 publications

(45 citation statements)

References 37 publications

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“…For singe WP systems, gels formed both at 95 o C and 80 o C were strong enough to be handled efficiently for large deformation measurements when the concentration was ≥ 6% w/w. At 95 o C the fracture strain(Fig.5.C)of the mixtures did not follow a very logical trend when compared to the single protein gels and generally there is greater variability in the fracture strain data compared to the other parameters Jose et al (2016). reported uncertainties in the trend of the fracture strain in WP and SP mixtures.…”

mentioning

confidence: 88%

“…Sample preparation for CLSM analysis was performed similarly to the procedure described elsewhere (Ersch et al, 2015;Jose et al, 2016;Urbonaite et al, 2016). Prior to heating, protein samples were mixed with fluorescent dye Rhodamine B (final dye concentration 0.001% w/w).…”

Section: Confocal Laser Scanning Microscopymentioning

confidence: 99%

“…Textural properties of heat-induced gelled systems based on mixtures of animal proteins with plant proteins, such as soy proteins (SP) (Comfort & Howell, 2002;Ersch, ter Laak, van der Linden, Venema, & Martin, 2015;Jose, Pouvreau, & Martin, 2016;Roesch & Corredig, 2005) pea proteins (Wong, Vasanthan, & Ozimek, 2013) and rapeseed proteins (RP) (Ainis, Ersch, & Ipsen, 2017) have been investigated and described. Most of these studies have focused on the alteration of the rheological properties in mixed gels and reported that at specific mixing ratios the stiffness or fracture stress of the mixed gels was higher compared to the gels produced by the individual proteins resulting to synergistic gels.…”

Section: Introductionmentioning

confidence: 99%

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Rheological and water holding alterations in mixed gels prepared from whey proteins and rapeseed proteins

et al. 2019

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confidence: 88%

Section: Confocal Laser Scanning Microscopymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Rheological and water holding alterations in mixed gels prepared from whey proteins and rapeseed proteins

et al. 2019

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“…Previous studies have shown that the properties of SPI films can be improved by blending with other surfactants 5 . Whey protein isolate (WPI), which is recovered from milk whey, contains ~90 wt% protein and is amphiphilic, whereby it can act as an emulsifier to stabilize oil/water interfaces 6 .…”

Section: Introductionmentioning

confidence: 99%

Soy/whey protein isolates: interfacial properties and effects on the stability of oil‐in‐water emulsions

Zhang

Xie

et al. 2020

J Sci Food Agric

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BACKGROUND The adsorption of proteins at oil/water interfaces can reduce interfacial tension and increase emulsion stability. However, emulsions stabilized by soy protein isolate (SPI) are not sufficiently stable. Using SPI as a control, a theoretical basis for the adsorption behavior of mixed SPI and whey protein isolate (WPI) at the oil/water interface was established and the effects of the protein ratio and content on the emulsion stability were studied. RESULTS Compared to SPI solution, SPI–WPI mixed solutions were found to reduce the size distribution of emulsion droplets and significantly improve the emulsion stability. Among the studied protein contents and ratios, the protein content of 0.2 g kg−1 and SPI/WPI mass ratio of 1:9 offered the lowest creaming stability index (15%), the smallest droplet size (278 nm), and the largest absolute value ζ‐potential (35 mV), i.e. the emulsion stability was excellent. The largest dilatational modulus (10.08 mN m−1), dilatational elasticity (10.01 mN m−1), and dilatational viscosity (1.18 mN m−1), were observed with a protein content of 0.15 g kg−1 (SPI/WPI ratio of 1:9), along with a high interfacial protein adsorption capacity (47.33%). SPI–WPI complexes form a thick adsorption layer around oil droplets, resulting in an increase of the expansion modulus of the interfacial layer. CONCLUSION SPI–WPI complexes can form a thick adsorption layer around oil droplets, resulting in increased expansion modulus of the interfacial layer, which improves emulsion stability. © 2020 Society of Chemical Industry

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“…The aggregation and gelation behavior of proteins from whey (Li & Zhong, 2016, Zhang, Arrighi, Campbell, Lonchamp, & Euston, 2016aZhang, Arrighi, Campbell, Lonchamp, Euston, & 2016b), soy (Chen, Zhao, Chassenieux, & Nicolai, 2016), quinoa (Ruiz, Xiao, Boekel, Minor, & Stieger, 2016), canola (Yang, Wang, Vasanthan, & Chen, 2014), oat (Yang, Wang, & Chen, 2017) and chicken (Zhao et al, 2016) have been widely studied. Whey and soy proteins were widely investigated to produce beverages, infant foods, tofu, shoyu, baked goods and other products (Maubois & Lorient, 2016;Singh, Kumar, Sabapathy, & Bawa, 2008;Zhou, Liu, & Tang, 2017) because of their high content of essential amino acids, good digestibility, and health benefits (Jose, Pouvreau, & Martin, 2016;Li & Zhong, 2016;Yang, Wang, Vasanthan, & Chen, 2014). These proteins have also been studied because of their capacity to entrap important molecules within gel networks (Chen et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

Effects of pH modification in proteins from fish (Whitemouth croaker) and their application in food packaging films

et al. 2018

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The commercial use of biodegradable proteins films is still limited due to their poor mechanical and barrier performance. However, processing of proteins to modify their structure may have a significant impact on films properties. Thus, the effect of thermal or pH-induced denaturation on the gelation behavior of Withemouth Croacker proteins was investigated in the development of films for packaging. Denaturation at pH 2 and pH 10 yielded the toughest protein gels. Gelation through pH modification is related to conformational changes in the structure of fish proteins, especially in secondary structure. Rheology tests demonstrated that a stronger gel was formed at pH 2, which might be due to the positively charged proteins. This behavior is related to the lower mesh size of the gel as demonstrated by small-angle X-ray scattering experiments. Gels prepared at both pH 2 and pH 10 had the ability to form cohesive films; however, no significant differences were observed between these treatments for water vapor permeability and mechanical properties. The modification of protein structure through gelation produced more soluble and less permeable films.

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Mixing whey and soy proteins: Consequences for the gel mechanical response and water holding

Cited by 74 publications

References 37 publications

Rheological and water holding alterations in mixed gels prepared from whey proteins and rapeseed proteins

Rheological and water holding alterations in mixed gels prepared from whey proteins and rapeseed proteins

Soy/whey protein isolates: interfacial properties and effects on the stability of oil‐in‐water emulsions

Effects of pH modification in proteins from fish (Whitemouth croaker) and their application in food packaging films

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