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


ABSTRACT: 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.

SUBMITTER: Das Purkayastha M 

PROVIDER: S-EPMC4926928 | biostudies-literature | 2016 Apr

REPOSITORIES: biostudies-literature

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

Das Purkayastha Manashi M   Borah Anuj Kumar AK   Saha Sougata S   Manhar Ajay Kumar AK   Mandal Manabendra M   Mahanta Charu Lata CL  

Journal of food science and technology 20160418 4


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 interf  ...[more]

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