Protein–Saccharide Interaction

Saeki, Hiroki

doi:10.1201/b11768-10

Cited by 5 publications

(6 citation statements)

References 125 publications

(121 reference statements)

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“…The solubility of proteins is closely interrelated with their functions, such as gelation and emulsification behavior . Oxidized MPs had significantly lower solubility than control (Figure ).…”

Section: Resultsmentioning

confidence: 99%

“…The solubility of proteins is closely interrelated with their functions, such as gelation and emulsification behavior. 18 Oxidized MPs had significantly lower solubility than control (Figure 2). The addition of 80 μM/g epigallocatechin-3-gallate further decreased the solubility of the oxidized MPs, indicating aggregation of MPs induced by interactions between epigallocatechin-3-gallate and the oxidized MPs.…”

Section: ■ Materials and Methodsmentioning

confidence: 95%

“…Researchers reported that glycation of serum albumin via the Maillard reaction inhibited protein aggregation caused by epigallocatechin-3-gallate . The Maillard reaction does not require a chemical catalyst, making it superior to other catalyst-dependent systems used to modify proteins . Unfortunately, there are difficulties in controlling the glycation levels, undesirable color changes, and the formation of antinutritional compounds during the Maillard reaction due to the requirements of dry heating and relatively long reaction time .…”

Section: Introductionmentioning

confidence: 99%

“…17 The Maillard reaction does not require a chemical catalyst, making it superior to other catalystdependent systems used to modify proteins. 18 Unfortunately, there are difficulties in controlling the glycation levels, undesirable color changes, and the formation of antinutritional compounds during the Maillard reaction due to the requirements of dry heating and relatively long reaction time. 19 For these reasons, the application of glycation via the Maillard reaction is limited in the food industry.…”

Section: ■ Introductionmentioning

confidence: 99%

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Inhibition of Epigallocatechin-3-gallate/Protein Interaction by Methyl-β-cyclodextrin in Myofibrillar Protein Emulsion Gels under Oxidative Stress

Zhang

Chen

et al. 2018

J. Agric. Food Chem.

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Nowadays, natural antioxidants abundant in polyphenols have been widely used to substitute synthetic antioxidants in meat products. In general, high doses of natural antioxidants are required to provide comparative antioxidant effects as synthetic antioxidants. Noticeably, the qualities of meat products can be jeopardized due to interactions between polyphenols and myofibrillar proteins (MPs). In this study, methyl-β-cyclodextrin was used to increase the polyphenol loading amount by preventing interactions between polyphenols and proteins. Solubility, electrophoresis, fluorescence spectroscopy, and surface hydrophobicity analyses indicated that methyl-β-cyclodextrin could dose-dependently inhibit epigallocatechin-3-gallate-induced attacks on MPs under oxidative stress. Gel strength, cooking loss, confocal laser scanning microscopy, dynamic rheological testing, and Raman spectrum during gelation were further analyzed to investigate the effects of methyl-β-cyclodextrin on the qualities of epigallocatechin-3-gallate-treated emulsion gel. Methyl-β-cyclodextrin addition prevented modification of the secondary structure of MPs caused by epigallocatechin-3-gallate. In consequence, the gel and emulsifying properties of MPs were significantly improved. Moreover, β-cyclodextrins could partly inhibit oxidative attacks on MPs and thus increase their solubility. These results indicated that methyl-β-cyclodextrin addition effectively enhanced epigallocatechin-3-gallate loading capacity in meat products.

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Section: Resultsmentioning

confidence: 99%

Section: ■ Materials and Methodsmentioning

confidence: 95%

Section: Introductionmentioning

confidence: 99%

Section: ■ Introductionmentioning

confidence: 99%

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Inhibition of Epigallocatechin-3-gallate/Protein Interaction by Methyl-β-cyclodextrin in Myofibrillar Protein Emulsion Gels under Oxidative Stress

Zhang

Chen

et al. 2018

J. Agric. Food Chem.

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“…It has been reported that the antioxidant components present in various foods have beneficial effects on human health, and several of these antioxidants have been identified [ 1 , 2 ]. Additionally, protein glycation using the Maillard reaction effectively improved the functions of the food proteins, especially their antioxidant activity [ 3 , 4 ]. Thus far, numerous reducing sugars, including monosaccharides [ 5 ], oligosaccharides [ 6 ], and polysaccharides [ 7 ], have been employed in Maillard-type glycation to enhance the antioxidant activities of various food proteins, such as casein [ 5 ], whey protein [ 6 ], and longan pulp protein [ 7 ].…”

Section: Introductionmentioning

confidence: 99%

Comparison of Maillard-Type Glycated Collagen with Alginate Oligosaccharide and Glucose: Its Characterization, Antioxidant Activity, and Cytoprotective Activity on H2O2-Induced Cell Oxidative Damage

Yang

Joe

et al. 2022

Foods

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To improve the antioxidant activity of collagen molecules using Maillard-type glycation, the relation between antioxidant activity and progress indexes for the Maillard reaction must be understood. In this study, lyophilized tilapia scale collagen was mixed with a half weight of alginate oligosaccharide (AO) or glucose and incubated at 60 °C and 35% relative humidity for up to 18 h to produce the Maillard-type glycated collagen (C-AO and C-Glu, respectively). As glycation progressed, the amount of conjugated sugar coupled with UV-vis absorbance at 294 nm and 420 nm increased more rapidly in C-Glu than in C-AO, and the available lysine decreased rapidly in C-Glu compared with C-AO. The early-to-middle- and late-stage products of the Maillard reaction were involved in enhanced antioxidant activity of digested C-AO and digested C-Glu, respectively. Additionally, C-AO acquired the antioxidant activity without marked available lysine loss. The cytoprotective effect of collagen in H2O2-induced damage was enhanced by glycation, achieved by reducing malondialdehyde content and increasing superoxide dismutase and catalase activities. These results indicate that AO is an excellent reducing sugar that enhances the health benefits of collagen without excessive loss of lysine, which is a nutritional problem of the Maillard-type glycation.

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The gelation properties of myofibrillar proteins prepared with malondialdehyde and (−)-epigallocatechin-3-gallate

Feng

Wang

et al. 2021

Food Chemistry

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Protein–Saccharide Interaction

Cited by 5 publications

References 125 publications

Inhibition of Epigallocatechin-3-gallate/Protein Interaction by Methyl-β-cyclodextrin in Myofibrillar Protein Emulsion Gels under Oxidative Stress

Inhibition of Epigallocatechin-3-gallate/Protein Interaction by Methyl-β-cyclodextrin in Myofibrillar Protein Emulsion Gels under Oxidative Stress

Comparison of Maillard-Type Glycated Collagen with Alginate Oligosaccharide and Glucose: Its Characterization, Antioxidant Activity, and Cytoprotective Activity on H2O2-Induced Cell Oxidative Damage

The gelation properties of myofibrillar proteins prepared with malondialdehyde and (−)-epigallocatechin-3-gallate

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