Effect of industrial process conditions of fava bean (Vicia faba L.) concentrates on physico-chemical and functional properties

Sharan, Siddharth; Zotzel, Jens; Stadtmüller, Johannes; Bonerz, Daniel; Aschoff, Julian; Olsen, Karsten; Rinnan, Åsmund; Saint-Eve, Anne; Maillard, Marie‐Noëlle; Orlien, Vibeke

doi:10.1016/j.ifset.2022.103142

Cited by 6 publications

(3 citation statements)

References 55 publications

(66 reference statements)

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“…These four commercial legume protein isolates had protein contents in the range of 86–92% (based on the dry matter), and their soluble protein fractions in neutral water (pH 7) were only around 20%, except that the solubility of SPI reached 42% (Figure A1). Conventionally, the extraction of legume protein isolates includes solubilization at an alkaline pH and then precipitation by acidification to the pI region, around pH 4.5–6. − To improve the extraction rate, the temperature might be increased up to 80 °C . Therefore, most commercial legume protein isolates are low in solubility. , From the photos (Figure A2) of individual fractions, the residual pigments in commercial protein isolates mostly bound to insoluble proteins (Sed), and the lyophilized Sup fractions were all well redissolved in natural water.…”

Section: Resultsmentioning

confidence: 99%

“…30−33 To improve the extraction rate, the temperature might be increased up to 80 °C. 31 Therefore, most commercial legume protein isolates are low in solubility. 32,33 From the photos (Figure 1A2) of individual fractions, the residual pigments in commercial protein isolates mostly bound to insoluble proteins (Sed), and the lyophilized Sup fractions were all well redissolved in natural water.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

“…Hence, these proteins probably interact with RNA strongly due to the electrostatic potential generated by the positively charged proteins at pH 7 and the negatively charged phosphate backbone of RNA, thus precipitating together. Aside from ribosomal proteins, most other identified proteins have a pI ranging from pH 4 to 7, as a consequence of the conventional industrial extraction process. − With the help of the LFQ quantification technique, the relative contents of proteins that detected in both fractions are compared. Generally, the proteins that showed higher contents in Sup fractions than in Sed fractions are more hydrophilic and have a scaled solubility above 0.45.…”

Section: Resultsmentioning

confidence: 99%

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Correlation between Protein Features and the Properties of pH-Driven-Assembled Nanoparticles: Control of Particle Size

Mao

Huang

Jia

et al. 2023

J. Agric. Food Chem.

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This study sought to understand how the features of proteins impact the properties of nanoparticles assembled using the pH-shifting approach and the mechanism behind. Four legume protein isolates from faba bean, mung bean, soy, and pea were fractionated into natural aqueous-soluble (Sup) and aqueous-insoluble (Sed) fractions, which were proved to serve as shell and core, respectively, for the pH-driven-assembled nanoparticles. Using zein instead of Sed fractions as the core improved size uniformity, and particle size can be precisely controlled by adjusting core/shell ratios. Using the proteomic technique and silico characterization, the features of identified proteins indicated that hydrophobicity rather than molecular weight, surface charge, etc., mainly determined particle size. With molecular docking, structural analysis, and dissociation tests, the assembly of zein/Sup-based nanoparticles was dominantly driven by hydrophobic interactions. This study provides constructive information on the correlation between protein features and the properties of pH-driven-assembled nanoparticles, achieving a precise control of particle size.

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