Comparative studies on the physicochemical properties of peanut protein isolate–polysaccharide conjugates prepared by ultrasonic treatment or classical heating

Li, Chen; Xue, Haoran; Chen, Zhiyan; Ding, Qiao; Wang, Xingguo

doi:10.1016/j.foodres.2013.12.038

Cited by 157 publications

(83 citation statements)

References 46 publications

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“…This might be the reason why conjugates showed lower H 0 index results and why a higher degree of glycation caused the index results to reduce more quickly. However, a few studies found that the glycated proteins obtained by classical wet heating or by an ultrasound‐assisted Maillard reaction showed higher H 0 index readings than the control proteins . During incubation and the Maillard reaction there were two effects on H 0 : (i) the incubation exposed hydrophobic groups because the protein was partially denatured by the heating, so H 0 increased; (ii) glycosylation decreased H 0 because the hydrophilic groups of the polysaccharide (or mono, di, or oligosaccharide) were attached to the protein surface and increased the hydrophilic behavior .…”

Section: Resultsmentioning

confidence: 99%

Time effect on structural and functional properties of whey protein isolate‐gum acacia conjugates prepared via Maillard reaction

Chen

Wang

et al. 2019

J Sci Food Agric

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BACKGROUND The functional properties of whey protein isolate (WPI) are sensitive to pH, ionic strength, and temperature. This prevents its application in various food systems and processing technologies. The conjugation of proteins with polysaccharides via the Maillard reaction is an efficient method to improve the functionality of proteins. The purpose of this work was to conjugate gum acacia (GA) with WPI via the dry‐heating Maillard reaction and to investigate the effect of reaction time on the physicochemical and functional properties of WPI‐GA conjugates. RESULTS Sodium dodecyl sulfate‐polyacrylamide gel electrophoresis and high‐performance size exclusion chromatography confirmed the formation of higher molecular weight conjugates. The degrees of glycation for WPI‐GA conjugates incubated for 1, 3, 5, and 7 days were 28.14%, 44.98%, 49.50%, and 51.20%, respectively. The glycation reaction reduced the surface hydrophobicity and fluorescence intensity of WPI significantly (P < 0.05). Functional properties of the conjugates, such as solubility, stability against heat‐induced insolubility, and emulsion properties were all superior to the control WPI. However, a reaction time longer than a day resulted in a high degree of browning and decreased the functionality of the conjugate significantly (P < 0.05). CONCLUSION The results indicated that conjugation of WPI with GA can be a promising way to enhance its functional properties. However, the reaction time suitable for producing conjugates with superior functional properties was not necessarily the highest glycation degree that could be reached. © 2019 Society of Chemical Industry

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Section: Resultsmentioning

confidence: 99%

Time effect on structural and functional properties of whey protein isolate‐gum acacia conjugates prepared via Maillard reaction

Chen

Wang

et al. 2019

J Sci Food Agric

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“…Figure shows that glycation induces a decrease in the fluorescence intensity of the MBPIs. This result was similar to the fluorescence features of the products of Maillard reactions as given in previous literature, indicating that the polysaccharide chain shielded the area around the Trp residues.…”

Section: Resultsmentioning

confidence: 99%

Effect of ultrasound treatment on the wet heating Maillard reaction between mung bean [Vigna radiate (L.)] protein isolates and glucose and on structural and physico‐chemical properties of conjugates

et al. 2015

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“…Vicilin (8S) was found to be the main component in MBPI, and legumin type (11S) globulins were the other main proteins. A general decrease in the intensities of subunits with molecular weights of 60, [43][44][45][46][47][48]32, and 26 kDa attributed to vicilin was observed in MBPI-D; the intensities of all these subunits decreased with conjugation time, which suggested that these subunits participated in the graft reaction between MBPI and dextran. The bands in MBPI-D-80 corresponding to 32 and 26 kDa even disappeared after 5 h of treatment, and the 60 kDa band faded away after 4 h of conjugation; the 21 kDa bands could hardly be found after 2 h of treatment.…”

Section: Sds-page Profilementioning

confidence: 91%

“…Consistent with this, previously, Hattori et al [42] indicated that the polysaccharide chains shield the area around the Trp residues and thus decrease the fluorescence intensity of Trp. Li et al [43] showed that high degree of graft during glycation leads to a higher decrease in fluorescence intensity. These reports also explain why fluorescence intensity of MBPI-D-90 with same graft time was markedly decreased.…”

Section: Fluorescence Spectrummentioning

confidence: 99%

Structural and functional properties of Maillard reaction products of protein isolate (mung bean,Vigna radiate(L.)) with dextran

Zhou

Zhang

et al. 2017

International Journal of Food Properties

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The objective of this study was to determine the functional and structural properties of Maillard reaction products of mung bean [Vigna radiate (L.)] protein isolate with dextran obtained under the temperature of 80°C or 90°C with different times (0, 1, 2, 3, 4, 5, and 6 h). The mung bean protein isolate-dextran conjugate had better solubility, emulsifying activity, and emulsifying stability than mung bean protein isolate; however, the protein aggregation decreased the solubility, surface hydrophobicity, emulsifying activity, and emulsifying stability of mung bean protein isolate-dextran conjugate. In general, these functional properties of mung bean protein isolate-dextran conjugate obtained at 80°C with lower degree of glycosylation and browning degree were better than mung bean protein isolatedextran conjugate obtained at 90°C. Both vicilin (8S) and legumin type (11S) globulins both participated in the graft reaction, the subunit with a molecular weight of 21 kDa that contributed to 11S globulin might be the most vulnerable to dextran followed by the 60, 32, and 26 kDa subunits. Maillard reaction between mung bean protein isolate and dextran led to a decreased fluorescence intensity and a bathochromic shift. The fluorescence intensity of mung bean protein isolate-dextran conjugate generally decreased, and λ max of mung bean protein isolate-dextran conjugate first increased and then decreased. The grafted mung bean protein isolates had lower α-helix content but higher β-sheet content. As the Maillard reaction between mung bean protein isolate and dextran proceeded, the α-helix contents of the mung bean protein isolate-dextran conjugates were significantly increased and then decreased, and the β-sheet content generally decreased and then increased. Excessive grafted dextran and more protein aggregation was observed in mung bean protein isolate-dextran conjugate obtained at 90°C, which induced structural changes that might have impaired the functions. Our findings suggest that conjugation of mung bean protein isolate with dextran through the Maillard reaction is an effective way of improving the functional properties of mung bean protein isolate for its application in the food industry. ARTICLE HISTORY

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Comparative studies on the physicochemical properties of peanut protein isolate–polysaccharide conjugates prepared by ultrasonic treatment or classical heating

Cited by 157 publications

References 46 publications

Time effect on structural and functional properties of whey protein isolate‐gum acacia conjugates prepared via Maillard reaction

Time effect on structural and functional properties of whey protein isolate‐gum acacia conjugates prepared via Maillard reaction

Effect of ultrasound treatment on the wet heating Maillard reaction between mung bean [Vigna radiate (L.)] protein isolates and glucose and on structural and physico‐chemical properties of conjugates

Structural and functional properties of Maillard reaction products of protein isolate (mung bean,Vigna radiate(L.)) with dextran

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