Relationship between Secondary Structure and Surface Hydrophobicity of Soybean Protein Isolate Subjected to Heat Treatment

Wang, Zhongjiang; Li, Yang; Jiang, Lianzhou; Qi, Baokun; Zhou, Linyi

doi:10.1155/2014/475389

Cited by 192 publications

(124 citation statements)

References 42 publications

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“…Consistent with the results of our study, our previous research also showed that protein aggregate have higher β-sheet and β-turn content. [36] The α-helix content of MBPI-D-90 gradually increased and then decreased with treatment time, while the β-sheet content first decreased and then increased. The change in these structures of MBPI-D-90 was similar to that observed in MBPI-D-80.…”

Section: Discussionmentioning

confidence: 95%

“…We previously showed that protein denaturation increases the surface hydrophobicity, and that surface hydrophobicity decreases as aggregates are formed. [36] In general, the surface hydrophobicity of MBPI-D-90 was lower than that of MBPI-D-80, which suggested that more dextran grafting and aggregation formation decreased protein hydrophobicity to a large extent. …”

Section: Emulsifying Propertiesmentioning

confidence: 90%

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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: Discussionmentioning

confidence: 95%

Section: Emulsifying Propertiesmentioning

confidence: 90%

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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“…It has been suggested before that heating whilst grinding aqueous soy slurry causes proteinaceous material to aggregate due to denaturation (Nishinari et al, 2014). Thermal denaturation of the main storage proteins b-conglycinin and glycinin occurs in the ranges 74-77°C and 92-93.7°C respectively, which accounts for aggregation when soybeans were ground at 80°C (Kinsella, 1979;Wang et al, 2014). Aggregation of supernatant protein of a size less than 40 nm occurs upon heating of soymilk to increase the concentration of protein particles in the size range 40-110 nm (Ono et al, 1991).…”

Section: Resultsmentioning

confidence: 99%

“…Nonheat treated protein extraction was also carried out at ambient temperature as a control. After a total of 30 min grinding, the soy slurry increased to 41.4°C as no temperature control was performed, which is well below the denaturation temperatures for the main storage proteins, b-conglycinin and glycinin (74-77°C and 92-93.7°C, respectively; Kinsella, 1979;Wang et al, 2014).…”

Section: Sample Preparationmentioning

confidence: 99%

Confocal imaging to reveal the microstructure of soybean processing materials

Preece

Drost

Hooshyar

et al. 2015

Journal of Food Engineering

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Sustainable production of food products for human consumption is required to reduce negative impacts on the environment and to consumer’s health. Soybeans are an excellent source of nutritive plant proteins; aqueous extraction yields part of the available oil and protein from the legume. Many studies have been conducted which detail the various processing parameters and their effects on the extraction yields, yet there is little data on the localisation of nutritive components such as oil and protein in the fibrous unextracted by-product. Here we show a novel confocal laser scanning microscopy investigation of soybean processing materials and the physical effects of thermal treatment on the materials microstructure upon aqueous extraction. Various features, more specifically oil, protein (including protein aggregation) and cell wall structures, are visualised in the fibrous by-product, soy slurry and soy extract, with their presence both in the continuous phase and within intact cotyledon cells. Thermal treatment reduced the protein extraction yield; this is shown to be a result of aggregated protein bodies in the continuous phase and within intact cotyledons cells. Knowledge of the processing material microstructures can be applied to improve extraction yields and reduce waste production

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“…Moreover, defining and measuring protein functionality start at the level of protein structure (Wang, Li, Jiang, Qi & Zhou, 2014).…”

Section: Thermal and Xrd Propertiesmentioning

confidence: 99%

Effect of drying methods on physico-chemical and functional properties of chickpea protein concentrates

Ghribi

Gafsi

Blecker

et al. 2015

Journal of Food Engineering

188

117

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Relationship between Secondary Structure and Surface Hydrophobicity of Soybean Protein Isolate Subjected to Heat Treatment

Cited by 192 publications

References 42 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

Confocal imaging to reveal the microstructure of soybean processing materials

Effect of drying methods on physico-chemical and functional properties of chickpea protein concentrates

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