Interaction between Kidney-Bean Polysaccharides and Duck Myofibrillar Protein as Affected by Ultrasonication: Effects on Gel Properties and Structure

Wu, Yang Chang; Du, Qiwei; Fan, Xiankang; Zhou, Changyu; He, Jun; Sun, Yunfei; Xia, Qiang; Pan, Daodong

doi:10.3390/foods11243998

Cited by 17 publications

(13 citation statements)

References 46 publications

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“…Wu et al . improved the gel strength of duck myofibrillar protein by 52.67% using 1% kidney‐bean polysaccharides, however, LNT had a better effect compared to it 23 . Lentinan was therefore beneficial for improving MP gel properties.…”

Section: Resultsmentioning

confidence: 91%

“…By using PIPES, the resulting supernatant was diluted 10 times. The absorbance at 595 nm was determined 23 . The equation to calculate the hydrophobicity of the MPs surface was as follows:

BPB (μg) = \frac{200 \times (A_{normalc} - A_{normals})}{A_{c}}

where A C represents the absorbance of the control, and A S represents the absorbance of the sample.…”

Section: Methodsmentioning

confidence: 99%

“…The absorbance at 595 nm was determined. 23 The equation to calculate the hydrophobicity of the MPs surface was as follows:…”

Section: Surface Hydrophobicitymentioning

confidence: 99%

“…The creation of a homogeneous .67% using 1% kidney-bean polysaccharides, however, LNT had a better effect compared to it. 23 Lentinan was therefore beneficial for improving MP gel properties. A denser and uniform gel structure could advance the WHC and then enhance the output of meat products.…”

Section: Gelling Propertiesmentioning

confidence: 99%

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Effect of lentinan on gelling properties and structural changes of goose myofibrillar protein under oxidative stress

Fan

Liu

et al. 2023

J Sci Food Agric

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BACKGROUND The reduction of protein oxidation is important for maintaining the product quality of reconstituted meat. In this study, the dose‐dependent effects of lentinan (LNT) on gelling properties and chemical changes in oxidatively stressed goose myofibrillar protein were investigated. RESULTS Myofibrillar protein (MP) with 200 μmol g−1 protein LNT increased gel strength by 87.90 ± 9.26% in comparison with LNT‐free myofibrillar protein after oxidation. Scanning electron microscopy analysis revealed that the gel network containing LNT was compact, with small pores and uniform distribution. The absolute value of the zeta potential reduced significantly following oxidation of LNT with 200 μmol g−1 protein at 4 °C for 12 h compared with the zeta potential without LNT, according to the laser particle size analyzer. The incorporation of LNT increased protein solubility and –SH content, inhibited carbonyl formation, enhanced α‐helix content and tryptophan intrinsic fluorescence intensity, and reduced exposure of hydrophobic groups and protein aggregation. CONCLUSION The results indicated that adding LNT to myofibrillar protein could improve gel. This is related to its protective effect on conformational changes in the oxidation system. Lentinan is therefore recommended for oxidatively stressed goose meat processing to enhance the MP gelling potential. © 2023 Society of Chemical Industry.

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Section: Resultsmentioning

confidence: 91%

“…By using PIPES, the resulting supernatant was diluted 10 times. The absorbance at 595 nm was determined 23 . The equation to calculate the hydrophobicity of the MPs surface was as follows:

BPB (μg) = \frac{200 \times (A_{normalc} - A_{normals})}{A_{c}}

where A C represents the absorbance of the control, and A S represents the absorbance of the sample.…”

Section: Methodsmentioning

confidence: 99%

“…The absorbance at 595 nm was determined. 23 The equation to calculate the hydrophobicity of the MPs surface was as follows:…”

Section: Surface Hydrophobicitymentioning

confidence: 99%

Section: Gelling Propertiesmentioning

confidence: 99%

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Effect of lentinan on gelling properties and structural changes of goose myofibrillar protein under oxidative stress

Fan

Liu

et al. 2023

J Sci Food Agric

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“…Protein–polysaccharide gels are defined that the different nanoscale molecules (protein/polysaccharide) self-assemble and aggregate into micron-scale phase behavior structures [ 6 ]. The gel structures of low-fat processed meat products mainly include the skeleton structure (myofibrillar protein gel network) and the dispersed phase structure of polysaccharides.…”

Section: Introductionmentioning

confidence: 99%

Insight into the Mechanism of Porcine Myofibrillar Protein Gel Properties Modulated by κ-Carrageenan

Chen

Luo

Wang

et al. 2023

Foods

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The purpose of this study is to explain the mechanism of porcine myofibrillar protein gel properties modulated by κ-carrageenan. The textural properties results showed that the stress at fracture of the composite gel with 0.4% κ-carrageenan had the highest value (91.33 g), which suggested that the 0.4% κ-carrageenan addition was the limitation. The strain at fracture was significantly reduced with κ-carrageenan addition. The composite gel with 0.4% κ-carrageenan had the lowest proportion of T22 (7.85%) and the shortest T21 relaxation time (252.81 ms). The paraffin section showed that the phase separation behavior of the composite gel transformed from single-phase behavior to dispersed phase behavior to bi-continuous phase behavior, and the ratio of CG/MP phase area significantly increased from 0.06 to 1.73. The SEM showed that the three-dimensional network of myofibrillar protein transformed from a loose structure to a compact structure to an unaggregated structure with κ-carrageenan addition. The myofibrillar protein network of the treatment with 0.4% κ-carrageenan had the highest DF value (1.7858) and lowest lacunary value (0.452). The principal component analysis was performed on the data of microstructure and textural properties, and the results showed that the dispersed phase behavior and moisture stabilization promoted the aggregation of myofibrillar protein and the composite gel had better water holding capacity and textural properties, while bi-continuous phase behavior hindered the aggregation of myofibrillar protein and the composite gel had worse water holding capacity and textural properties.

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Soy protein isolate–guar gum–goose liver oil O/W Pickering emulsions that remain stable under accelerated oxidation at high temperatures

Fan,

Li,

Shi

et al. 2023

J Sci Food Agric

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BackgroundGoose liver oil (GLO) is a solid‐liquid mixture, rich in polyunsaturated fatty acids and high in nutritional value, but poor in fluidity and easily oxidized. Therefore, O/W Pickering emulsions of three polysaccharides and soy protein isolate (SPI) with GLO were prepared to improve the stability of it.ResultsSDS‐PAGE, Fourier transform infrared spectroscopy, and zeta potential revealed that the SPI and complexes with konjac glucomannan, pectin, and guar gum (GG) ranged from 17‐75 KDa, with the site of action being the ‐OH stretch and the amide group, and bound by hydrogen bonding. Adding konjac glucomannan and GG significantly increased the water contact angle of the SPI to 74.1° and 59.0°, respectively. Therefore, the polysaccharide‐protein complexes could enhance the emulsion stability. In addition, the oil‐in‐water (O/W) Pickering emulsions with GLO had near‐Newtonian fluid rheological properties with a significant increase in apparent viscosity and viscoelasticity, forming a dual network structure consisting of a ductile and flexible protein network and a rigid and brittle polysaccharide network. The microstructure observation indicated that the O/W emulsions were spherical and homogeneous. The highest emulsification activity was observed for the GG‐SPI‐GLO emulsions, without significant delamination or flocculation and high oxidative stability after 7 days in storage.ConclusionThese results demonstrate that the construction of SPI‐GG‐GLO O/W Pickering emulsions can stabilize GLO even at high temperatures that promote oxidation.This article is protected by copyright. All rights reserved.

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Interaction between Kidney-Bean Polysaccharides and Duck Myofibrillar Protein as Affected by Ultrasonication: Effects on Gel Properties and Structure

Cited by 17 publications

References 46 publications

Effect of lentinan on gelling properties and structural changes of goose myofibrillar protein under oxidative stress

Effect of lentinan on gelling properties and structural changes of goose myofibrillar protein under oxidative stress

Insight into the Mechanism of Porcine Myofibrillar Protein Gel Properties Modulated by κ-Carrageenan

Soy protein isolate–guar gum–goose liver oil O/W Pickering emulsions that remain stable under accelerated oxidation at high temperatures

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