Heat-Induced Soluble Protein Aggregates from Mixed Pea Globulins and β-Lactoglobulin

Chihi, Mohamed–Lazhar; Mession, Jean-Luc; Sok, Nicolas; Saurel, Rémi

doi:10.1021/acs.jafc.6b00087

Cited by 103 publications

(73 citation statements)

References 49 publications

(195 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Previous works have also shown that heat treatment of cowpea protein isolate at 70°C and 90°C (Peyrano et al, 2016) or whey proteins at 72°C and 140°C (Patel, Singh, Anema, & Creamer, 2004) did not produce changes in the polypeptide patterns after SDS-ME PAGE analysis. However, some of the proteins extracted by the SDS-ME buffer were too large to enter the gel as shown by the band at the origin (top of gel), which corroborates the data from native-PAGE and is consistent with previous reports (Chihi, Mession, Sok, & Saurel, 2016;Mession, Sok, Assifaoui, & Saurel, 2013;Shand et al, 2007).…”

Section: Polyacrylamide Gel Electrophoresissupporting

confidence: 91%

Modification of the structural, emulsifying, and foaming properties of an isolated pea protein by thermal pretreatment

Chao

Aluko

2018

CyTA - Journal of Food

View full text Add to dashboard Cite

Pea protein isolate (PPI) prepared through isoelectric protein precipitation was heat-treated between 50°C and 100°C. The effect of heat treatment on the structural and functional properties of proteins was evaluated. Native gel electrophoresis showed the formation of protein aggregates (molecular weight ≫ 200 kDa) in the temperature range of 80-100°C. Intrinsic fluorescence data suggested that protein denaturation reached its highest level at pH 3.0. The formation of oil-inwater emulsions (1:5 oil:water volume ratio) was positively impacted by pH increase as evidenced by the decrease of minimum oil droplet size (d 4,3 ) from 26 μm at pH 5.0 to 22 μm at pH 7.0 (P < 0.05). In contrast, heat pretreatment led to decreasing emulsion properties at pH 3.0 with d 4,3 values increasing from 27 μm to 80 μm (P < 0.05). Regardless of pH applied, all heated PPI samples displayed low foaming properties.Modificación mediante pretratamiento térmico de las propiedades estructurales, emulsificantes y espumantes de una proteína de arveja [guisante] aislada RESUMEN El aislado de proteína de arveja (PPI), preparado mediante precipitación isoeléctrica de proteínas, se sometió a un tratamiento térmico con temperaturas de entre 50 y 100°C. Posteriormente, se evaluó el efecto del tratamiento térmico en las propiedades estructurales y funcionales de las proteínas. La electroforesis nativa en gel reveló la formación de agregados proteicos (peso molecular ≫ 200 kDa) en el rango de temperatura de 80 a 100°C. Los datos obtenidos de la fluorescencia intrínseca sugieren que la desnaturalización de las proteínas alcanzó su nivel más elevado cuando el pH era 3.0. La formación de emulsiones de aceite en agua (ratio del volumen aceite:agua 1:5) se vio afectada positivamente por el aumento del pH, lo que se evidenció por la disminución del tamaño mínimo de la gota de aceite (d 4,3 ), que pasó de 26 μm con pH de 5.0 a 22 μm con pH de 7.0 (P < 0.05). En contraste, el pretratamiento térmico produjo una disminución de las propiedades de emulsión cuando el pH era 3.0, pues los valores d 4,3 aumentaron de 27 μm a 80 μm (P < 0.05). Independientemente del pH utilizado, todas las muestras de PPI calentadas presentaron limitadas propiedades espumantes. ARTICLE HISTORY

show abstract

Section: Polyacrylamide Gel Electrophoresissupporting

confidence: 91%

Modification of the structural, emulsifying, and foaming properties of an isolated pea protein by thermal pretreatment

Chao

Aluko

2018

CyTA - Journal of Food

View full text Add to dashboard Cite

show abstract

“…Whatever the pH studied, the thermal treatment led to increase significantly H o of the albumin protein particles, about one‐and‐half times as compared with NA. The thermal treatment caused the exposition of hydrophobic groups initially buried in the structure of NA molecules, resulting in an increase in surface hydrophobicity in accordance with the general behavior of globular proteins (Chihi et al., ).…”

Section: Resultsmentioning

confidence: 73%

“…Whatever the pH studied, the thermal treatment led to increase significantly H o of the albumin protein particles, about one-andhalf times as compared with NA. The thermal treatment caused the exposition of hydrophobic groups initially buried in the structure of NA molecules, resulting in an increase in surface hydrophobicity in accordance with the general behavior of globular proteins (Chihi et al, 2016 It is important to note that the present determination of H o was done from protein samples containing soluble and insoluble fractions of aggregates in order to be representative of the protein material used for foam preparation.…”

Section: Surface Hydrophobicitymentioning

confidence: 92%

See 1 more Smart Citation

The Effect of High‐Pressure Microfluidization Treatment on the Foaming Properties of Pea Albumin Aggregates

Djemaoune

Cases

Saurel

2019

Journal of Food Science

Self Cite

View full text Add to dashboard Cite

The effect of dynamic high‐pressure treatment, also named microfluidization, on the surface properties of thermal pea albumin aggregates (AA) and their foaming ability was investigated at pH 3, 5, and 7. The solubility of albumin particles was not affected by the increase in microfluidization pressure from 70 to 130 MPa. Particle charge depended only on the pH, whereas protein surface hydrophobicity was stable at pH 5, decreased at pH 3, but increased at pH 7 after microfluidization treatment and with the applied pressure. Surface tension of AA measured at air/water interface was favorably affected by the microfluidization treatment at each pH preferentially due to size reduction and increased flexibility of protein particles. The foaming capacity and stability of AA depended on the pH conditions and the microfluidization treatment. The high‐pressure treatment had little influence in foaming properties at acidic pHs, probably related to a more compact form of AA at these pHs. At neutral pH, the foaming properties of pea AA were strongly influenced by their surface properties and size associated with significant modifications in AA structure with microfluidization. Changes in albumin aggregate characteristics with pH and microfluidization pressure are also expected to modulate other techno‐functional properties, such as emulsifying property. Practical Application Albumins are known for their interesting nutritional values because they are rich in essential amino acids. This fraction is not currently marketed as a protein isolate for human consumption, but can be considered as a potential new vegetable protein ingredient. This document demonstrated that heat treatment or dynamic high‐pressure technology can control the foaming properties of this protein for possible use in expanded foods.

show abstract

“…Nevertheless, the mechanism of such aggregate formation for soluble MnP still needs further study. Chihi et al [54] demonstrated that the hydrophobic interactions and the formation of new disulfide bridges resulted in soluble protein aggregates; while, Wang et al [55] emphasized the importance of the hydrophobic interaction in promoting the protein aggregate, as compared with disulfide bonds. Therefore, we will shed light on the intriguing mechanism of polymerization for soluble MnP in the future.…”

Section: Discussionmentioning

confidence: 99%

Expression of a fungal manganese peroxidase in Escherichia coli: a comparison between the soluble and refolded enzymes

et al. 2016

View full text Add to dashboard Cite

BackgroundManganese peroxidase (MnP) from Irpex lacteus F17 has been shown to have a strong ability to degrade recalcitrant aromatic pollutants. In this study, a recombinant MnP from I. lacteus F17 was expressed in Escherichia coli Rosetta (DE3) in the form of inclusion bodies, which were refolded to achieve an active enzyme. Further, we optimized the in vitro refolding conditions to increase the recovery yield of the recombinant protein production. Additionally, we attempted to express recombinant MnP in soluble form in E. coli, and compared its activity with that of refolded MnP.ResultsRefolded MnP was obtained by optimizing the in vitro refolding conditions, and soluble MnP was produced in the presence of four additives, TritonX-100, Tween-80, ethanol, and glycerol, through incubation at 16 °C. Hemin and Ca2+ supplementation was crucial for the activity of the recombinant protein. Compared with refolded MnP, soluble MnP showed low catalytic efficiencies for Mn2+ and H2O2 substrates, but the two enzymes had an identical, broad range substrate specificity, and the ability to decolorize azo dyes. Furthermore, their enzymatic spectral characteristics were analysed by circular dichroism (CD), electronic absorption spectrum (UV-VIS), fluorescence and Raman spectra, indicating the differences in protein conformation between soluble and refolded MnP. Subsequently, size exclusion chromatography (SEC) and dynamic light scattering (DLS) analyses demonstrated that refolded MnP was a good monomer in solution, while soluble MnP predominantly existed in the oligomeric status.ConclusionsOur results showed that two forms of recombinant MnP could be expressed in E. coli by varying the culture conditions during protein expression.Electronic supplementary materialThe online version of this article (doi:10.1186/s12896-016-0317-2) contains supplementary material, which is available to authorized users.

show abstract

Heat-Induced Soluble Protein Aggregates from Mixed Pea Globulins and β-Lactoglobulin

Cited by 103 publications

References 49 publications

Modification of the structural, emulsifying, and foaming properties of an isolated pea protein by thermal pretreatment

Modification of the structural, emulsifying, and foaming properties of an isolated pea protein by thermal pretreatment

The Effect of High‐Pressure Microfluidization Treatment on the Foaming Properties of Pea Albumin Aggregates

Expression of a fungal manganese peroxidase in Escherichia coli: a comparison between the soluble and refolded enzymes

Contact Info

Product

Resources

About