Characterization of soy β-conglycinin–dextran conjugate prepared by Maillard reaction in crowded liquid system

Zhang, Xi; Qi, Jun‐Ru; Li, Kang-Kang; Yin, Shou-Wei; Wang, Jinmei; Zhu, Jiayin; Yang, Xiaoquan

doi:10.1016/j.foodres.2012.09.001

Cited by 81 publications

(47 citation statements)

References 39 publications

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“…Glycation has been suggested to reduce the exposure of hydrophobic groups buried intramolecularly; additionally, the bonding of hydrophilic straight-chain dextran increases the hydrophilicity on the molecule surface. [35] In our study, we also found a sharp decrease in the surface hydrophobicity of MBPI-D-80 with 4 h of graft treatment, which might be related to protein aggregation. We previously showed that protein denaturation increases the surface hydrophobicity, and that surface hydrophobicity decreases as aggregates are formed.…”

Section: Emulsifying Propertiessupporting

confidence: 65%

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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Section: Emulsifying Propertiessupporting

confidence: 65%

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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“…From the results, it is obvious that the decrease in free amino group was in accordance with the increase in browning at 420 nm ( Fig. 1), which was in accordance with Zhang et al [18] who reported the extent of glycation in soy β-conglycinin-dextran model system was enhanced during the Maillard reaction. …”

Section: Conjugation Of Dextran On Spisupporting

confidence: 87%

Preparation, Characterization and In vitro Evaluation of Theophylline Nanoparticles Prepared with Dextran- Conjugated Soy Protein

Jin¹,

Zhou²,

Chen³

et al. 2015

Trop. J. Pharm Res

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“…Figure 1A exhibits the protein staining SDS-PAGE pattern; the characteristic bands of β-conglycinin (subunits of α′, α, and β) were detected in lane 2, which is consistent with Zhang. 29 However, when it comes to lane 3, a shift of bands toward the top of separating gels was visualized after the Maillard reaction, which is clear evidence that compounds with high molecular weight were developed. The migration of dextran can be elided because it carries no charge, the effect of noncovalent interactions on SDS-PAGE may be ignored because they were disrupted in the reducing condition, and an intense bank accumulated on the top of separating gels in carbohydrate staining pattern ( Figure 1B, lane 3), all of which strongly verified the covalent attachment of dextran to β-conglycinin.…”

Section: ■ Results and Discussionmentioning

confidence: 96%

Fabrication and Characterization of Stable Soy β-Conglycinin–Dextran Core–Shell Nanogels Prepared via a Self-Assembly Approach at the Isoelectric Point

Feng

Yin

et al. 2015

J. Agric. Food Chem.

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The preparation of soy β-conglycinin-dextran nanogels (∼90 nm) went through two stages, which are safe, facile, and green. First, amphiphilic graft copolymers were formed by dextran covalently attaching to β-conglycinin via Maillard dry-heating reaction. Second, the synthesized conjugates were heated above the denaturation temperature at the isoelectric point (pH4.8) so as to assemble nanogels. The effects of pH, concentration, heating temperature, and time on the fabrication of nanogels were examined. The morphology study displayed that the nanogels exhibited spherical shape with core-shell structures, which was reconfirmed by zeta-potential investigation. Both circular dichroism spectra and surface hydrophobicity analyses indicated that the conformations of β-conglycinin in the core of nanogels were changed, and the latter experiment further revealed that the hydrophobic groups of β-conglycinin were exposed to the surface of protein. The nanogels were stable against various conditions and might be useful to deliver hydrophobic bioactive compounds.

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Characterization of soy β-conglycinin–dextran conjugate prepared by Maillard reaction in crowded liquid system

Cited by 81 publications

References 39 publications

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

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

Preparation, Characterization and In vitro Evaluation of Theophylline Nanoparticles Prepared with Dextran- Conjugated Soy Protein

Fabrication and Characterization of Stable Soy β-Conglycinin–Dextran Core–Shell Nanogels Prepared via a Self-Assembly Approach at the Isoelectric Point

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