The relationships between physicochemical properties and conformational features of succinylated and acetylated kidney bean (Phaseolus vulgaris L.) protein isolates

Yin, Shou-Wei; Tang, Chuan-He; Qi-biao, Wen; Yang, Xiaoquan; Yuan, Dan

doi:10.1016/j.foodres.2009.11.007

Cited by 77 publications

(68 citation statements)

References 41 publications

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“…Despite the presence of high amount of randomness and protein dissociation in 0.6MA and 0.8MA, the drop in hydrophobicity after exhaustive acylation may be due to the dense distribution of negatively charged maleyl residues, inhibiting Coomassie Blue dye (probe used for S 0 measurement) from approaching and binding to the exposed hydrophobic moieties on the protein surfaces (Strange et al 1993). Similar behavior has been reported also for 1-anilino-8-naphthalenesulfonic acid (fluorescence probe for S 0 measurement) in modified soy protein hydrolyzates (Achouri and Zhang 2001) and acylated kidney bean protein (Yin et al 2010). …”

Section: Free Sulfhydryl Group (Sh) and Disulfide Bond (Ss)supporting

confidence: 57%

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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Section: Free Sulfhydryl Group (Sh) and Disulfide Bond (Ss)supporting

confidence: 57%

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

et al. 2016

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“…The function of protein is determined by structure, and the existence of disulfide bonds in molecular structure usually increases the molecular stability (Yin, Tang, Wen, Yang, & Yuan, 2010). Therefore we suggest that the reason for the relative stability of the chitinase probably is related with the disulfide bonds in its molecular conformation (Fig.…”

Section: Thermostabilitymentioning

confidence: 87%

A novel chitinase isolated from Vicia faba and its antifungal activity

Wang

Chen

et al. 2012

Food Research International

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“…Circular dichroism spectra were obtained using a MOS‐450 spectropolarimeter (Bio‐Logic Science Instrument, Grenoble, France), according to the method reported by Yin et al . (). The near‐UV CD spectrum measurements were performed in a quartz cuvette of 10 mm with a protein concentration around 1.0 mg mL −1 .…”

Section: Methodsmentioning

confidence: 97%

Structure, trypsin inhibitor activity and functional properties of germinated soybean protein isolate

Liu

Yin

2013

Int J of Food Sci Tech

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Summary The objective of this research was to investigate the effects of germination on functional and conformational properties as well as the in vitro trypsin digestibility of soy protein isolate (SPI). The influences of germination on the molecular properties of SPI were also evaluated. The germination degraded lipoxygenase, α, α' subunits of β‐conglycinin (7S) and acidic chains of glycinin (11S) of soybean. Concomitantly, the loss of tertiary structures of SPI occurred due to the germination. The trypsin inhibitor activity of germinated SPI presented a decreasing trend, followed by an increase in the growth of hypocotyls. The in vitro trypsin digestibility of germinated SPI followed a consistent trend with the trypsin inhibitor activity. The protein solubility (PS) and emulsifying properties of SPI were improved by the germination, in a hypocotyl length‐dependent manner. The data suggest that some selected functional properties and the in vitro digestibility of soy proteins can be improved by means of the germination.

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The relationships between physicochemical properties and conformational features of succinylated and acetylated kidney bean (Phaseolus vulgaris L.) protein isolates

Cited by 77 publications

References 41 publications

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

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

A novel chitinase isolated from Vicia faba and its antifungal activity

Structure, trypsin inhibitor activity and functional properties of germinated soybean protein isolate

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