Conjugation of soy protein isolate (SPI) with pectin: effects of structural modification of the grafting polysaccharide

Ma, Xiaobin; Chi, Chengdeng; Pu, Yunfeng; Miao, Song; Liu, Donghong

doi:10.1016/j.foodchem.2022.132876

Cited by 35 publications

(18 citation statements)

References 36 publications

(47 reference statements)

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“…Most of the conjugates analyzed in this study were found to be more negatively‐charged compared to their mixture counterparts or individual biopolymer solutions ( p < 0.05) (Table 2). This might be due to some changes in the secondary structure (i.e., denaturation) of proteins in the conjugates increasing the mobility and exposure of a few previously hidden charged groups in addition to the impact of grafting of Pe chains in the conjugates (Ma et al, 2022).…”

Section: Resultsmentioning

confidence: 99%

Tribology and rheology of potato protein and pectin mixtures and Maillard conjugates

Soltanahmadi,

Wang,

Gul

et al. 2023

Sustainable Food Proteins

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This study aimed to compare the tribological and rheological properties of plant proteins versus their mixtures or conjugates with polysaccharides. We hypothesize that combining potato proteins (Po) with pectin (Pe) at various concentrations (0.5–5.0 wt%, ratios 1:1 and 1:2 w/w) will improve the lubrication performance of plant proteins by virtue of viscosity modification and boundary lubrication. Po showed shear thinning behavior with limited concentration‐dependence in boundary and mixed lubricity. Pe on the other hand showed pronounced concentration‐dependent flow and lubrication behavior delivering favorable boundary and viscous lubricity. Pe dominated the lubrication and high shear rate flow behavior in Po + Pe mixtures, governed mainly by the concentration of Pe and the hydrodynamic volume rather than the total concentration of the biopolymers. Maillard reaction (≤33% degree of conjugation) led to more negatively‐charged protein‐polysaccharide conjugates versus the sole biopolymers (p < 0.05). The conjugation decreased the second plateau shear viscosity of the Po + Pe mixtures and led to improvement in boundary and mixed lubricity when a reduced entrainment speed parameter was used. Findings from this study may inspire future studies combining plant proteins with polysaccharides to enhance their lubrication behavior and eventually improve the textural properties of plant‐based foods.

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Section: Resultsmentioning

confidence: 99%

Tribology and rheology of potato protein and pectin mixtures and Maillard conjugates

Soltanahmadi,

Wang,

Gul

et al. 2023

Sustainable Food Proteins

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show abstract

“…This suggested that SSPS with smaller Mw was more favourable for conjugation. It could be explained by two aspects: (i) smaller Mw could reduce the steric‐hindrance effect, which promoted the contact between SSPS and SPI molecule for increasing reaction efficiency (Ma et al ., 2022); (ii) the depolymerisation of SSPS breaks down the linkage of long polysaccharide chains, exposing more reducing end as the conjugation sites for the Maillard reaction (Li et al ., 2013b). Although the Mw of S4 and S5 was similar to S7, the DG of S4‐P‐C (37.3%) was significantly smaller and that of S5‐P‐C (46.8%) was significantly larger than S7 (40.5%).…”

Section: Results and Analysismentioning

confidence: 99%

“…The homogalactan and homoarabinan are linked to the rhamnose of rhamnogalacturonan as the branch chains. Some homogalacturonans are covalently bound with a small amount of xylose, glucose, and protein (Nakamura et al, 2012). The structure of SSPS is illustrated in Fig.…”

Section: Introductionmentioning

confidence: 99%

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Influences of the different chemical components in soybean soluble polysaccharide on the emulsifying performance of its conjugates formed with soybean protein isolate

Lin

Lei

Chen

et al. 2022

Int J of Food Sci Tech

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Summary This work aimed to elucidate the relationship between the chemical components of soybean soluble polysaccharide (SSPS) and its Maillard reaction with soybean protein isolate (SPI). Enzymatic hydrolysis was used to specifically cleave the chemical components of SSPS. Neutral sugar side chain regions of SSPS were easier to conjugate with SPI than the backbone containing galacturonic acid. The modified SSPS with higher content of arabinose showed the highest degree of glycosylation (46.8%). SSPS‐SPI conjugates exhibited lower interfacial tension than SPI, fabricating emulsion with smaller droplets size and better emulsion stability. The improved emulsifying properties could be ascribed to two aspects: (i) a higher percentage of adsorbed protein at the interface to cover more oil droplet surface; (ii) thicker adsorbed layer thickness onto the droplet surface to provide stronger steric‐hindrance effect to prevent droplet coalescence.

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“…It is easily affected by the processing conditions, such as low pH, high temperature, and ionic environment, which greatly restricted its application in actual production. Many strategies have been made to improve the functional properties of soy protein, including physical methods (3,4) and chemical methods (4,5) as well as (6). Recently, It was found that the non-covalent interaction of polyphenols with whey protein could cause the exposure of tryptophan residues, the unfolding of proteins and the decrease of the surface hydrophobicity (7).…”

Section: Introductionmentioning

confidence: 99%

Changes on the conformational and functional properties of soybean protein isolate induced by quercetin

Zhang

Hou²,

Zhu³

et al. 2022

Front. Nutr.

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The conformational changes and functional properties of SPI induced by quercetin was investigated via fourier transform infrared (FTIR) spectroscopy, fluorescence spectroscopy, circular dichroism (CD) spectroscopy and molecular docking. A decrease in the fluorescence intensity and a blue shift in the maximum wavelength were observed due to the binding process with fluorescent residues. The analysis of Stern-Volmer equation showed that the fluorescence quenching induced by quercetin took the form of static quenching, and the binding stoichiometry between SPI and quercetin was 1:1. The values of ΔH and ΔS were both positive illustrating that hydrophobic interaction was the primary binding force between quercetin and SPI. Results of FTIR and CD indicated that the binding with quercetin changed the secondary structure of SPI, resulting in a partially unfolded and more flexible structure. SDS-PAGE confirmed there was no covalent interaction between the two constituents. Molecular docking demonstrated that there were stable configurations and high matching degrees in both 11S and 7S proteins with quercetin via hydrogen bonds and hydrophobic interactions. Meanwhile, modification by quercetin enhanced the foaming and emulsifying capacities of SPI. These findings might provide theory reference for elucidation the mechanism of polyphenols-proteins interaction and development of related food additive products in future.

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Conjugation of soy protein isolate (SPI) with pectin: effects of structural modification of the grafting polysaccharide

Cited by 35 publications

References 36 publications

Tribology and rheology of potato protein and pectin mixtures and Maillard conjugates

Tribology and rheology of potato protein and pectin mixtures and Maillard conjugates

Influences of the different chemical components in soybean soluble polysaccharide on the emulsifying performance of its conjugates formed with soybean protein isolate

Changes on the conformational and functional properties of soybean protein isolate induced by quercetin

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