Antioxidative activity and emulsifying properties of cuttlefish skin gelatin modified by oxidised phenolic compounds

Aewsiri, Tanong; Benjakul, Soottawat; Visessanguan, Wonnop; Eun, Jong‐Bang; Wierenga, Peter A.; Gruppen, Harry

doi:10.1016/j.foodchem.2009.03.092

Cited by 135 publications

(91 citation statements)

References 37 publications

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“…The observation is congruent with the reports of Franzen and Kinsella (1976), and Wanasundara and Shahidi (1997). This dramatic improvement in colour can be explained with the blocking of the nucleophilic amino groups of protein with acyl groups, which can otherwise react with the electrophilic o-quinone (oxidation product of polyphenols) (Aewsiri et al 2009). The pH condition (pH 8-9) used for acylation hindrance) (El-Adawy 2000), and thus cause a significant decrease in the content of colour-forming quinones.…”

Section: Degree Of Whitenesssupporting

confidence: 89%

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: Degree Of Whitenesssupporting

confidence: 89%

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

et al. 2016

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“…As shown in Table 1, DH increased with hydrolytic time p 0.05 , a finding that is in accordance with prior studies 5,12,20,29 . In this work, RBPH with the highest DH of ca.…”

Section: Preparation and Characterization Of Rice Bran Proteinsupporting

confidence: 91%

“…Two hundred μL of the solvent phase was taken out to react with 2. 29 with a slight modification. Thiobarbituric solution was prepared by mixing 0.375 TBA, 15 trichloroacetic acid, and 0.25 N HCl.…”

Section: Oxidative Stability Of Rbph-added Emulsionsmentioning

confidence: 99%

Effects of Rice Bran Protein Hydrolysates on the Physicochemical Stability of Oil-in-Water Emulsions

Cheetangdee

2014

J. Oleo Sci.

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“…tryptophan, introduction of hydrophilic carboxylic residues (phenolic acid) and due to the incorporation of higher number of hydroxyl groups. However Aewsiri et al (2009) reported that phenolic compounds also cause the blocking of hydrophilic groups like amino and thiol groups. On one hand, covalent attachment of phenolic compounds with proteins causes the blocking of hydrophilic groups like thiol and amino and on other side, there is an increase in the amount of apolar groups (benzene ring) and introduction of polar groups (hydroxyl and carboxyl groups as in case of the phenolic acid).…”

Section: Surface Hydrophobicitymentioning

confidence: 99%

Effect of removal of phenolic compounds on structural and thermal properties of sunflower protein isolate

2016

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The present study evaluated the effect of removal of polyphenols on the structural properties of protein isolates extracted from sunflower seed and kernel. The structural and thermal changes in protein upon phenolic interaction were studied using circular dichroism, differential scanning calorimetry, thermal gravimetric analysis, X-ray diffraction, sodium dodecyl sulphatepolyacrylamide gel electrophoresis (SDS-PAGE), and Fourier Transform Infrared (FT-IR) spectroscopy. Presence of phenolic compounds in proteins decreased the ordered structure content with parallel increase in unordered structure content. Denaturation temperature was higher for protein isolates with phenolic compounds while, enthalpy decreased upon phenolic interaction. In the presence of phenolic compounds, higher mass loss was observed upon heating. Crystalinity and crystal size got increased after removal of phenolic compounds. Protein isolates from kernels had higher percentage of crystalinity and crystal size as compared to seed protein isolates. Higher molecular weights were observed for protein isolates with phenolic compounds. Presence of polyphenols reduced the hydrophobicity as well the sulfhydryl content and increased the particle size of proteins.

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Antioxidative activity and emulsifying properties of cuttlefish skin gelatin modified by oxidised phenolic compounds

Cited by 135 publications

References 37 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

Effects of Rice Bran Protein Hydrolysates on the Physicochemical Stability of Oil-in-Water Emulsions

Effect of removal of phenolic compounds on structural and thermal properties of sunflower protein isolate

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