Influence of Maillard reaction extent on acid induced gels of whey proteins and dextrans

Spotti, María Julia; Loyeau, Paula Andrea; Marangón, Abril; Noir, Hernán; Rubiolo, Amelia Catalina; Carrara, Carlos R.

doi:10.1016/j.foodhyd.2019.01.020

Cited by 66 publications

(36 citation statements)

References 32 publications

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“…This was because the free lysine of WPI and dextran bound to each other during the reaction, resulting in a decrease of the binding site of ANS. The change of H 0 before and after glycosylation reaction was consistent with the literature (Achouri, Boye, Yaylayan, & Yeboah, 2005; Spotti et al., 2019).…”

Section: Resultssupporting

confidence: 91%

“…The free sulfhydryl content of WPI at room temperature was 24.70 ± 0.20 μmol/g. The free sulfhydryl content of WPI and WPI‐D was reduced after heating (Figure 6), because the sulfhydryl groups were oxidized to form aggregates during heating (Spotti et al., 2019). The free sulfhydryl content of WPI‐D was lower than that of WPI at the same reaction temperature because the glycosylation reaction conditions were mild, and the sulfhydryl groups performed oxidation reaction to form intramolecular or intermolecular disulfide bonds.…”

Section: Resultsmentioning

confidence: 99%

“…Spotti et al. (2019) studied the inductive reaction of dextran near the isoelectric point of WPI to form a gel. The results showed that the Maillard reaction inhibited gel formation, changed the mechanical and microstructural properties of the acid gel, and reduced the gel strength.…”

Section: Introductionmentioning

confidence: 99%

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Effect of reaction temperature on the protein structure and the ability to encapsulate β‐carotene of WPI‐dextran conjugates

Chu

Kang

Zhao

et al. 2020

Journal of Food Science

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In this paper, we studied the effect of glycosylation reaction on the molecular structure and functional properties of whey protein isolate (WPI), and studied the effect of reaction temperature (50 to 90 °C) on the molecular structure and functional properties of WPI–dextran conjugates (WPI‐D). The results of the extent of glycation (EG) and sodium dodecyl sulfate–polyacrylamide gel electrophoresis confirmed the formation of WPI‐D. Circular dichroism (CD), Fourier transform infrared spectrum, and fluorescence spectroscopy indicated that the molecular structure of WPI was changed after glycosylation—the β‐sheet content was decreased and the tryptophan content was increased. The emulsifying properties and the ability to encapsulate β‐carotene of WPI‐D were improved compared with WPI (P < 0.05). When the reaction temperature was 70 and 80 °C, the EG and the ability to encapsulate β‐carotene of WPI‐D were better (P < 0.05), which was related to protein unfolding. However, due to the polymerization between the WPI molecules, the emulsion activity index of WPI‐D and the ability to encapsulate β‐carotene were lowered at 90 °C (P < 0.05). Therefore, the glycosylation reaction can change the molecular structure and functional properties of WPI; the emulsifying properties and the ability to encapsulate β‐carotene of WPI‐D can be changed by controlling the reaction temperature of glycosylation. Practical Application The glycosylation reaction can change the molecular structure and functional properties of Whey protein isolate; the emulsifying properties and the ability to encapsulate β‐carotene of WPI‐dextran conjugates can be changed by controlling the reaction temperature of glycosylation.

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Section: Resultssupporting

confidence: 91%

Section: Resultsmentioning

confidence: 99%

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Effect of reaction temperature on the protein structure and the ability to encapsulate β‐carotene of WPI‐dextran conjugates

Chu

Kang

Zhao

et al. 2020

Journal of Food Science

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“…Therefore, the glycosylation of proteins is based on the Maillard reaction. In contrast with the non‐covalent complexes, the bond in covalent complexes or conjugates is not responsive to pH and ionic strength changes, which is advantageous because they can be employed in a wide range of food formulations and processing (Spotti et al , 2019).…”

Section: Introductionmentioning

confidence: 99%

Structural and physicochemical properties of soya bean protein isolate/maltodextrin mixture and glycosylation conjugates

Zhao

Yin

Yan

et al. 2020

Int J of Food Sci Tech

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The effect of mixture and conjugation with maltodextrin (MD) in aqueous solution on the structural and physicochemical properties of soya bean protein isolate (SPI) was investigated. Although the mixing of MD would not change the distribution of secondary structure and tertiary conformation of SPI, the protein aggregation was promoted through hydrophobic interaction, which resulted in the decrease in solubility and the improvement of gel strength and water holding capacity (WHC) of SPI/MD mixture. However, glycosylation decreased a-helix and increased b-structure. The bathochromic shift of the fluorescence emission maximum wavelength for SPI/MD conjugates was promoted, resulting in less compact tertiary conformation. These structural modifications might be the reason for the changes in the physicochemical properties of conjugates. After glycosylation, the surface hydrophobicity and solubility were increased, the average particle size was decreased, and the gelation properties were weakened including gel strength and WHC.

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“…Both 50 μL of Ellman's reagent, which contained Determination of surface hydrophobicity ANS was used to measure the surface hydrophobicity of WPC/PUL gels. 13 The gel was diluted into different concentration (0.1, 0.2, 0.3, 0.4 and 0.5 mg mL -1 ). Then, 3.0 mL of diluted solution that contained 15 μL of ANS solution (8 mmol L -1 ) was maintained at 25°C for 15 min.…”

Section: Determination Of the Sh Groupmentioning

confidence: 99%

Effect of pullulan concentration and pH on the interactions between whey protein concentrate and pullulan during gelation

et al. 2020

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BACKGROUND: Whey protein concentrate (WPC)/pullulan (PUL) hydrogel is applied as a microencapsulation wall material to protect probiotics. However, the interactions between WPC and PUL during gelation have not been clarified. In the present study, the effects of PUL concentration and pH on the interactions between WPC and PUL during gelation were evaluated with respect to appearance, zeta-potential, sulfhydryl group amount, surface hydrophobicity and infrared spectroscopy measurements. The rheological properties of WPC/PUL gels were also determined. RESULTS: The results obtained showed that a proper concentration (0.40 g mL-1) of PUL could improve the gel by enhancing the strength of hydrogen bonding, electrostatic interactions and exposure of hydrophobic groups, whereas too much PUL inhibited the formation of disulfide bonds. Furthermore, hydrophobic interactions, disulfide bonds and hydrogen bonds were destroyed in varying degrees under an alkaline environment. The rheological results also demonstrated a similar effect of PUL concentration and pH on the storage modulus (G') of WPC/PUL gels. CONCLUSION: When the WPC/PUL gel was formed at PUL concentration of 0.40 g mL-1 and pH 7.0, the interaction between WPC and PUL could be enhanced, which is beneficial for the future application of WPC/PUL gels in the food industry.

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Influence of Maillard reaction extent on acid induced gels of whey proteins and dextrans

Cited by 66 publications

References 32 publications

Effect of reaction temperature on the protein structure and the ability to encapsulate β‐carotene of WPI‐dextran conjugates

Effect of reaction temperature on the protein structure and the ability to encapsulate β‐carotene of WPI‐dextran conjugates

Structural and physicochemical properties of soya bean protein isolate/maltodextrin mixture and glycosylation conjugates

Effect of pullulan concentration and pH on the interactions between whey protein concentrate and pullulan during gelation

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