Structural and functional characterization of kidney bean and field pea protein isolates: A comparative study

Shevkani, Khetan; Singh, Narpinder; Kaur, Amritpal; Rana, Jai Chand

doi:10.1016/j.foodhyd.2014.07.024

Cited by 545 publications

(464 citation statements)

References 62 publications

Supporting

Mentioning

403

Contrasting

Unclassified

Order By: Relevance

“…Once absorbed, the emulsifying agent protects dispersed phase droplets from coalescence by forming a film at the oilwater interface and by reducing the interfacial tension (Phillips 1994). The initial absorption of proteins to the interface will be determined both by the proteins solubility that let protein reach to the interface and by its hydrophobicity to provide optimum contact of non-polar groups with the oil phase (Shevkani et al 2015). Thus, the lower EAI of salmon protein powder can be related to its considerably lower surface hydrophobicity (Fig 1b).…”

Section: Emulsion Activity and Stabilitymentioning

confidence: 99%

Structural, functional, and sensorial properties of protein isolate produced from salmon, cod, and herring by-products

Abdollahi

Undeland

2018

Food Bioprocess Technol

View full text Add to dashboard Cite

Nutritional, structural, functional, and sensorial properties of protein isolate developed from salmon (Salmo salar), cod (Gadus morhua), and herring (Clupea harengus) by-products using the pH-shift method was studied. Function of the proteins in an emulsion system in terms of viscoelastic properties was also evaluated. Regardless of origin, the proteins showed satisfying nutritional value as reflected in their high essential amino acid content. The proteins contained significantly (p < 0.05) higher proportion of active sulfhydryl groups and surface hydrophobicity compared to whey and egg white protein reflecting conformational changes caused by the pH-shift process. Solubility, emulsion, and foaming capacity of the proteins showed a trend similar to soy protein and dependent on their origin. Cod protein had better emulsion and foaming capacity than salmon and herring proteins which was in line with its high surface hydrophobicity and myosin heavy chain content. Emulsions developed from cod and salmon proteins showed substantially better viscoelastic properties, with higher stability and viscosity compared to herring protein emulsions. Cod protein scored low for sensorial attributes related to lipid oxidation while herring protein showed high levels of fishy and rancid flavor and odor. Altogether, results showed that the proteins from fish filleting by-products have potential to be used as food ingredients, but their application would be governed by their origin and sensorial properties.

show abstract

Section: Emulsion Activity and Stabilitymentioning

confidence: 99%

Structural, functional, and sensorial properties of protein isolate produced from salmon, cod, and herring by-products

Abdollahi

Undeland

2018

Food Bioprocess Technol

View full text Add to dashboard Cite

show abstract

“…Secondary structure quantitations were performed by the Gaussian curve-fitting of the spectrum in the Amide I region (Shevkani et al 2015).…”

Section: Surface Hydrophobicity μGmentioning

confidence: 99%

Effect of maleylation on physicochemical and functional properties of rapeseed protein isolate

et al. 2016

View full text Add to dashboard Cite

Influence of maleylation on the physicochemical and functional properties of rapeseed protein isolate was studied. Acylation increased whiteness value and dissociation of proteins, but reduced free sulfhydryl and disulfide content (p < 0.05). Intrinsic fluorescence emission and FTIR spectra revealed distinct perturbations in maleylated proteins' tertiary and secondary conformations. Increase in surface hydrophobicity, foaming capacity, emulsion stability, protein surface load at oil-water interface and decrease in surface tension at air-water interface, occurred till moderate level of modification. While maleylation impaired foam stability, protein solubility and emulsion capacity were markedly ameliorated (p < 0.05), which are concomitant with decreased droplet size distribution (d 32 ). In-vitro digestibility and cytotoxicity tests suggested no severe ill-effects of modified proteins, especially up to low degrees of maleylation. The study shows good potential for maleylated rapeseed proteins as functional food ingredient.

show abstract

“…Lentil proteins possess higher thermal stability than common bean proteins because of their higher β-sheet content (Carbonaro et al 2008). The ΔH of JSG was 12.07 J/g, which was higher than that of protein isolates from kidney beans and field peas (Shevkani et al 2015). JSG may have a more ordered structure than the protein isolates from these plant sources.…”

Section: Thermal Propertiesmentioning

confidence: 72%

Characterization and Structural Identification of an 11S Globulin of Juglans mandshurica Maxim. Kernel from the Changbai Mountains in China

Li¹,

Wang²,

Wang³

et al. 2016

Proceedings of the 2016 5th International Conference on Civil, Architectural and Hydraulic Engineering (ICCAHE 2016)

View full text Add to dashboard Cite

ABSTRACT:The major seed storage protein 11S globulin from Juglans mandshurica Maxim. (JSG) was isolated and purified to identify its structure and analyze its physicochemical properties. JSG was found to be composed of two distinct major polypeptides with molecular masses of ~23 and ~20 kDa, and whose amino acid sequences are highly similar to those of the 11S globulin from J. regia in the NCBI database. JSG contains essential amino acids that correspond to the adult standard recommended by FAO/WTO. Differential scanning calorimetry revealed a single endothermic peak with a denaturation temperature of 96.83 °C and an enthalpy value of 12.07 J/g. The secondary structure of the JSG consists of β-sheets (32.83%) and α-helices (11.67%). A red shift was also observed in the fluorescence spectra with guanidine hydrochloride (GdnHCl) or urea as denaturant; GdnHCl was proven to be a stronger denaturant than urea.

show abstract

Structural and functional characterization of kidney bean and field pea protein isolates: A comparative study

Cited by 545 publications

References 62 publications

Structural, functional, and sensorial properties of protein isolate produced from salmon, cod, and herring by-products

Structural, functional, and sensorial properties of protein isolate produced from salmon, cod, and herring by-products

Effect of maleylation on physicochemical and functional properties of rapeseed protein isolate

Characterization and Structural Identification of an 11S Globulin of Juglans mandshurica Maxim. Kernel from the Changbai Mountains in China

Contact Info

Product

Resources

About