Functionality of oilseed protein products: A review

Moure, Andrés; Sineiro, Jorge; Domı́nguez, Herminia; Parajó, Juan Carlos

doi:10.1016/j.foodres.2006.07.002

Cited by 474 publications

(354 citation statements)

References 164 publications

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“…Therefore, protein modification by chemical or enzymatic processes is employed to improve these functional properties (Nir et al 1994;Moure et al 2006;Martínez et al 2009). Enzymes act hydrolyzing peptide bonds in the protein, producing peptides of desired size, charge and surface properties (Moure et al 2006).…”

Section: Foaming and Emulsifying Propertiesmentioning

confidence: 99%

“…Besides its nutritional value as a source of energy and amino acids, proteins are also employed to modulate the physicochemical and sensory properties of foods (Moure et al 2006). The functional properties of proteins can be modified by enzymatic hydrolysis under controlled conditions, since it affects the molecular size, hydrophobicity and exposition of polar groups of the protein.…”

Section: Introductionmentioning

confidence: 99%

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Soy protein hydrolysis with microbial protease to improve antioxidant and functional properties

et al. 2014

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Soybean proteins are widely used as nutritional and functional food ingredients. This investigation evaluated through a 2 3 central composite design the effect of three variables (pH, temperature and enzyme/substrate (E/S) ratio) on the production of soy protein isolate (SPI) hydrolysates with a microbial protease. Soluble peptides, antioxidant activity, and foaming and emulsifying capabilities of the hydrolysates were analyzed. All variables, as well as their interactions, were significant for the soluble peptides content of SPI hydrolysates. Optimal conditions for obtaining soluble peptides were around 30-35°C, pH 6.5-9.5, and E/S ratios of 1,650-6,300 U g −1 . SPI hydrolysates produced at 30-45°C, pH 8.0-9.5, and E/S ratios of 4,000-8,000 U g −1 showed higher capacity to scavenge the 2,2′-azino-bis-(3-ethylbenzothiazoline)-6-sulfonic acid (ABTS) radical. Models for soluble peptides and ABTS activity of hydrolysates were obtained. In the range studied, the variables had not significant influence on the ability of hydrolysates to scavenge the 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical. SPI hydrolysates also presented reducing power and ability to chelate iron. Hydrolysis temperature was significant for the Fe 2+ -chelating ability of hydrolysates. Temperature of hydrolysis was significant for the foaming capacity of hydrolysates, with higher values observed at 45°C and 8,000 U g −1 . For emulsifying capacity, only E/S ratio presented a significant effect. Temperature and E/S ratio appeared to be more significant variables influencing the properties of the SPI hydrolysates. The results of this study indicate that specific hydrolysis conditions should be selected to obtain SPI hydrolysates with preferred characteristics.

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Section: Foaming and Emulsifying Propertiesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Soy protein hydrolysis with microbial protease to improve antioxidant and functional properties

et al. 2014

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“…Heat-induced gel characteristics were also improved with the firmest gels being obtained at intermediate levels of succinylation (Paulson and Tung 1989). Additional advantages of these modifications are related with delayed Maillard reactions, but the resulting derivative could be less susceptible to proteolysis (Moure et al 2006).…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2016

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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.

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“…ii. Health considerations: An example of this is the replacement of meat or soy proteins by (other) vegetable proteins (O'Kane et al, 2004;Pedroche et al, 2004;Vioque et al, 1999; reviewed in Moure et al, 2006). Similar to proteins obtained as by-product from waste material, unmodified plant proteins often have limited functional applicability.…”

Section: Types Of Chemical Protein Engineering -Exploring Potential Fmentioning

confidence: 99%

Application Potential of Food Protein Modification

Jongh¹,

Broersen²

2012

Advances in Chemical Engineering

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Functionality of oilseed protein products: A review

Cited by 474 publications

References 164 publications

Soy protein hydrolysis with microbial protease to improve antioxidant and functional properties

Soy protein hydrolysis with microbial protease to improve antioxidant and functional properties

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

Application Potential of Food Protein Modification

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