Aqueous fractionation yields chemically stable lupin protein isolates

Berghout, J.A.M.; Marmolejo-Garcia, C.; Berton‐Carabin, Claire C.; Nikiforidis, Constantinos V.; Boom, R.M.; Goot, Atze Jan van der

doi:10.1016/j.foodres.2015.03.039

Cited by 16 publications

(23 citation statements)

References 54 publications

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“…Lipid oxidation was determined by measuring the amount of conjugated diene (CD) hydroperoxides and the aldehyde content (mainly alkene‐2‐als) through the para‐anisidine value (pAV) . The pAV protocol was slightly modified according to Berghout et al and Cengiz et al …”

Section: Methodsmentioning

confidence: 91%

“…Lipid oxidation was determined by measuring the amount of conjugated diene (CD) hydroperoxides 25 and the aldehyde content (mainly alkene-2-als) through the para-anisidine value (pAV). 26 The pAV protocol was slightly modified according to Berghout et al 27 and Cengiz et al 28 For the determination of CD hydroperoxides, 50 μL of W 1 /O/W 2 double emulsion were mixed with 950 μL 2-propanol. This first sample was further diluted ten-fold with 2-propanol.…”

Section: Lipid Oxidationmentioning

confidence: 99%

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Double emulsions for iron encapsulation: is a high concentration of lipophilic emulsifier ideal for physical and chemical stability?

2019

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BACKGROUND Worldwide iron deficiency in diets has led to a growing interest in the development of food‐compatible encapsulation systems for soluble iron, which are able to prevent iron's undesirable off‐taste and pro‐oxidant activity. Here, we explore the use of double emulsions for this purpose, and in particular, how the lipophilic emulsifier (polyglycerol polyricinoleate, PGPR) concentration influences the physicochemical stability of water‐in‐oil‐in‐water (W 1 /O/W 2 ) double emulsions containing ferrous sulphate in the inner water droplets. Double emulsions were prepared with sunflower oil containing 10 to 70 g kg −1 PGPR in the oil phase, and were monitored for droplet size distribution, morphology, encapsulation efficiency (EE) and oxidative stability over time. RESULTS Fresh double emulsions showed an initial EE higher than 88%, but EE decreased upon storage, which occurred particularly fast and to a high extent in the emulsions prepared with low PGPR concentrations. All double emulsions underwent lipid oxidation, in particular those with the highest PGPR concentration, which could be due to the small inner droplet size and thus promoted contact between oil and the internal water phase. CONCLUSION These results show that a too high PGPR concentration is not needed, and sometimes even adverse, when developing double emulsions as iron encapsulation systems. © 2019 The Authors. Journal of The Science of Food and Agriculture published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry.

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Section: Methodsmentioning

confidence: 91%

Section: Lipid Oxidationmentioning

confidence: 99%

Double emulsions for iron encapsulation: is a high concentration of lipophilic emulsifier ideal for physical and chemical stability?

2019

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“…All the tested commercial ingredients had a higher carbonyl content than e.g., lab-made SPI as reported in literature (Chen et al, 2013b;Wu et al, 2009c). Compared to these commercial soy protein ingredients, the carbonyl contents for lupine protein isolate, whey protein isolate (WPI), raw chicken and bovine meat were also lower (Berghout et al, 2015b;Berton-Carabin et al, 2016;Santé-Lhoutellier et al, 2008a;Soyer et al, 2010). Such a variability in the proteinbound carbonyl levels suggests that either the process to obtain soy protein ingredients, and/or the subsequent storage conditions promote protein oxidation.…”

Section: Introductionmentioning

confidence: 61%

“…through the para-anisidine value (pAV) (AOCS, 2017). The pAV protocol was slightly modified according to Berghout et al (2015b) and Cengiz et al (2019).…”

Section: Lipid Oxidationmentioning

confidence: 99%

“…It should be noted that all measurements were done on soluble fractions, which is about 0.8 to 6% of the total protein in the processed protein-based matrices. The measurement on the soluble protein fraction is a fair representation of the levels of carbonyl protein-bounds and it has been commonly used to determine protein oxidation in a broad range of protein-based samples (Berardo et al, 2015;Berghout et al, 2015b;Berton-Carabin et al, 2016;Berton et al, 2012b;Colombo et al, 2016;Duque Estrada et al, 2018;Luo & Wehr, 2009;Santé-Lhoutellier et al, 2008b;Semedo Tavares et al, 2018;Soglia et al, 2016b).…”

Section: Determination Of Protein-bound Carbonyl Contentmentioning

confidence: 99%

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Protein oxidation as an integrated aspect of plant protein-based food

Duque-Estrada¹

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the protein and extracting soluble components (Johnson et al., 2008). The preparation of soy protein isolate (SPI) from the defatted flour involves separation steps under alkaline or acidic conditions (Alibhai et al., 2006;Lawhon et al., 1981).The final step to prepare both SPC and SPI is spray or freeze drying. About 80% of the proteins in SPI are storage globulin proteins: β-conglycinin, formed by three subunits α, α′ and β; and glycinin, composed of acid and basic subunits linked by disulfide bonds (Nishinari et al., 2017). Typically, the protein yield is around 60% of the protein present in the original soybeans (Johnson et al., 2008). Clearly, the isolation process requires a large amount of water and chemicals (van der Goot et al., 2016). Further, the process conditions applied to isolate proteins generally cause protein denaturation and loss of solubility (Jafari et al., 2016;Schutyser & van der Goot, 2011).Given the inefficiency of current fractionation route, there is an interest arising to develop more energy-efficient methods under less severe conditions, such as aqueous or dry fractionation (Geerts et al., 2018;Xing et al., 2018). Such methods do not yield high protein purity, however, some native components and structures are still present in protein-enriched fractions. Fractions obtained under such mild condition can be beneficial for structuring purposes, for instance when making meat analogues with a soy protein ingredient that intrinsically contains fat (Geerts et al., 2018).Recent research has focused on the use of alternative plant protein sources, such as starch-or oil-rich plants (Schreuders et al., 2019). The use of alternatives could increase the variety of food products on the market, in terms of sensory properties and nutritional value. In addition, the use of alternatives would add value to these other crops. Storage stability Bioavailability Water-insoluble iron Water-soluble iron EncapsulationChapter 1 Jacobsen, 2016;Promeyrat et al., 2011). It has been shown that protein oxidation in meat depends on the temperature and time of the treatment. Some related findings are summarized in Table 1. Protein oxidation increased with temperatures above 100 °C for all meat types. Noticeably, cooking bacon led to higher protein oxidation than other meat products and raw bacon already had a substantial level of oxidation.Protein oxidation often leads to changes in the secondary and tertiary structures of proteins, altering their physical properties, such as solubility and hydrophobicity (Santé-Lhoutellier et al., 2007). Table 1, outline studies showing that cooking meat increased hydrophobicity, due to protein denaturation. In meat products, protein oxidation has been associated with a loss of water-holding and gelling capacities, modification in color and flavor, altered texture, loss of essential amino acids and impaired digestion (

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Lupine (Lupinus spp.) proteins: characteristics, safety and food applications

Boukid

Pasqualone

2021

Eur Food Res Technol

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Lupines (Lupinus spp.) have emerged as a cheap functional food with the advantages of being nongenetically modified crop able to adapt to harsh conditions and low-input farming. Lupines are rich in protein and poor in starch, similar to soy. The factor limiting the use of lupine is the presence of quinolizidine alkaloids especially in bitter species. Nevertheless, modern breeding programs ensured the selection of sweet lupine species with reduced alkaloid content (≤ 0.2 g/kg DM). Numerous techniques have been employed to produce lupine protein isolates, concentrates and hydrolysates. Lupine proteins are rich in bioactive peptides associated with health-related benefits and have reported with interesting technofunctional properties. Lupine protein isolates and concentrates are used mostly for developing healthy foods, while hydrolysates are more applied in nutraceutical and cosmetic industries. Further research is needed to ensure better safety and wider spectrum of application through adequate strategies for allergenicity mitigation and improving techno-functionality.

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Aqueous fractionation yields chemically stable lupin protein isolates

Cited by 16 publications

References 54 publications

Double emulsions for iron encapsulation: is a high concentration of lipophilic emulsifier ideal for physical and chemical stability?

Double emulsions for iron encapsulation: is a high concentration of lipophilic emulsifier ideal for physical and chemical stability?

Protein oxidation as an integrated aspect of plant protein-based food

Lupine (Lupinus spp.) proteins: characteristics, safety and food applications

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