Co‐precipitation of whey and pea protein – indication of interactions

Kristensen, H.T.; Møller, Anders Hauer; Christensen, Mette; Hansen, Mikka Stenholdt; Hammershøj, Marianne; Dalsgaard, Trine Kastrup

doi:10.1111/ijfs.14553

Cited by 22 publications

(13 citation statements)

References 35 publications

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“…The same mechanism can partly be expected in the co-precipitation, where proteins were not unfolded by heat, but instead, the precipitated proteins in this study have been subjected to highly alkaline conditions during the initial steps of the precipitation procedure. This induces partial unfolding as shown in our previous study (Kristensen et al, 2020), both ensuring that the free thiols are available for interactions without breakage of the covalent bonds.…”

Section: Covalent Interactionssupporting

confidence: 56%

“…Protein solubility is in general increased if the electrostatic repulsion between molecules is higher than the hydrophobic interactions, but this was not shown in this study. This contradictory result could be ascribed to the alkaline pretreatment of the proteins prior to precipitation leaving the proteins in a semi-like structure as seen for a-la (Kristensen et al, 2020).…”

Section: Noncovalent Interactionsmentioning

confidence: 99%

“…Co-precipitation was performed as described by Kristensen et al, (2020) with modifications (Fig. 1).…”

Section: Co-precipitation Of Whey Protein Isolate and Pea Protein Isolatementioning

confidence: 99%

“…Protein solubility was measured as remaining protein in the supernatant after centrifugation at 2300 x g in a centrifuge (Eppendorf centrifuge 54I7R, Hamburg, Germany) according to Kristensen et al, (2020).…”

Section: Protein Solubilitymentioning

confidence: 99%

“…Mixing of proteins can be performed in different ways ranging from simple blending of proteins, to co-aggregation and co-precipitation. Proteins are mixed and precipitated together in order to achieve new protein products, which previously have been shown to possess value-added functionalities of the resulting product (Thompson, 1977;Kebary, 1993;Alu'datt et al, 2012;Kristensen et al, 2020). Therefore, understanding of the mechanism of protein-protein interactions and understanding how these properties can benefit from selectively mixing are essential.…”

Section: Introductionmentioning

confidence: 99%

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Protein–protein interactions of a whey–pea protein co‐precipitate

Kristensen

Christensen

Hansen

et al. 2021

Int J of Food Sci Tech

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The aim of this study was to investigate the mechanisms behind protein-protein interactions in a coprecipitate of whey protein isolate (WPI) and pea protein isolate (PPI). A co-precipitate and blend, consisting of 80% WPI and 20% PPI, were compared. Covalent disulphide interactions were studied by blocking of free thiols with N-Ethylmaleimide (NEM), while electrostatic interactions were studied in systems with 0.5 M NaCl and hydrophobic interactions with 0.2% SDS. Protein solubility, stability and secondary, tertiary and quaternary protein structures were analysed. Co-precipitation did not introduce different protein-protein interactions than the direct blending of proteins. SDS affected solubility (P < 0.05), secondary and tertiary structure. However, the effects of NEM and NaCl were significant greater (P < 0.05) on the same parameters and thermal stability, especially when combined (P < 0.01). Thus, the protein-protein interactions in a whey-pea co-precipitate and protein blend consisted of disulphide bonds and electrostatic interactions.

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Section: Covalent Interactionssupporting

confidence: 56%

Section: Noncovalent Interactionsmentioning

confidence: 99%

“…Co-precipitation was performed as described by Kristensen et al, (2020) with modifications (Fig. 1).…”

Section: Co-precipitation Of Whey Protein Isolate and Pea Protein Isolatementioning

confidence: 99%

Section: Protein Solubilitymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Protein–protein interactions of a whey–pea protein co‐precipitate

Kristensen

Christensen

Hansen

et al. 2021

Int J of Food Sci Tech

Self Cite

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The potential of coextraction as an emerging trend in the development of new functional food ingredients

Basak,

Singhal

2024

eFood

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The search for new functional ingredients that meet the nutritional and technological requirements from the available resources cost‐effectively has been an ongoing activity by both academia and industry. In this respect, coextraction of the ingredients is a promising approach for valorization of food wastes as can be seen from reports that have been emerging since the last decade. The process can be used for the coextraction of all major food ingredients, namely, lipids, proteins, and polysaccharides. The approach being presented in this review is based on using two or more resources to obtain ingredients through a single process. This review looks into some of these possibilities, presents future perspectives, and calls for attention from the scientific community to explore this area of research with high translational capabilities. Coextraction offers an opportunity for valorization of wastes with energy conservation and minimizing solvent usage, wherein the bioactives present therein can be coextracted with a major food ingredient and used in the formulations, while using the principles of circular economy. Apart from the processing advantage it provides, coextraction from different sources has been reported to positively influence the structural, nutritional, and functional properties of food ingredients.

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Impact of high hydrostatic pressure on casein micelle‐pea protein systems and comparison with heat treatment

Serrano León,

Gravel,

Perreault

et al. 2024

Sustainable Food Proteins

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Developing mixed systems with both plant‐ and animal‐based proteins is crucial to address the limitations in the techno‐functional properties of plant‐based proteins. While the impact of thermal co‐aggregation on mixed systems has been extensively studied, there is limited information on the effects of non‐thermal processes. Therefore, this study aimed to compare the effects of high hydrostatic pressure (HHP, 600 MPa–5 min) and heat (90°C for 60 min) treatments on the protein profiles in a mixed micellar casein (CN):pea protein (PPI) system, while also elucidating the interactions involved in the formation of protein aggregates. Our results showed that both HHP and heat treatments induced the formation of soluble protein aggregates through disulfide bonds. However, protein aggregation was less prominent after application of HHP. In both treatments, the aggregates primarily consisted of convicilin, vicilin, legumin and lipoxygenase. However, albumin PA2 did not contribute to HHP‐induced aggregates, and vicilin played a lesser role in their formation compared to heat‐induced aggregates. CN from the HHP‐treated CN:PPI sample did not participate in aggregate formation, as previously demonstrated after heat treatment. The presence of residual whey proteins in the CN ingredients explained the formation of CN‐whey protein aggregates after heat treatment and, to a lesser extent, after HHP treatment.

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Co‐precipitation of whey and pea protein – indication of interactions

Abstract: Co-precipitation of whey and pea protein -indication of interactions

Cited by 22 publications

References 35 publications

Protein–protein interactions of a whey–pea protein co‐precipitate

Protein–protein interactions of a whey–pea protein co‐precipitate

The potential of coextraction as an emerging trend in the development of new functional food ingredients

Impact of high hydrostatic pressure on casein micelle‐pea protein systems and comparison with heat treatment

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