The Experts below are selected from a list of 102 Experts worldwide ranked by ideXlab platform
Wentong Xue - One of the best experts on this subject based on the ideXlab platform.
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effects of aot reverse micelle on properties of soy Globulins
Food Chemistry, 2008Co-Authors: Xiaoyan Zhao, Fusheng Chen, Junqi Chen, Guosheng Gai, Wentong XueAbstract:Abstract This study was focused on the influence of AOT reverse micelle on physical–chemical properties of 7S and 11S Globulins from soy proteins, and compared with aqueous buffer extraction. The results showed that the contents of the surface hydrophobicity and SH groups of 7S and 11S Globulins and SS bonds of 11S globulin, using AOT reverse micelle extraction, were augmented, and SS bonds of 7S globulin decreased. The thermal and rheological properties of 7S and 11S Globulins extracted using the two methods were studied by differential scanning calorimetry (DSC) and rheometery. It was found that the peak denaturation temperature and heat of transition of 7S and 11S Globulins with aqueous buffer extraction were different from that with AOT reverse micellar extraction. The AOT reverse micelle did not affect the gel properties of 11S globulin, while it influenced 7S globulin’s. Hardness, springiness, gumminess, adhesiveness and chewiness of 7S globulin from AOT reverse micelle were lower than that from aqueous buffer extraction, but gumminess was higher.
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ftir spectra studies on the secondary structures of 7s and 11s Globulins from soybean proteins using aot reverse micellar extraction
Food Hydrocolloids, 2008Co-Authors: Xiaoyan Zhao, Fusheng Chen, Wentong Xue, Lite LeeAbstract:Fourier transform infrared (FTIR) method was used to study the secondary structures of 7S and 11S Globulins from soybean proteins using aqueous buffer and reverse micelles extraction method for the first time. The Fourier second derivative was applied to all spectra, revealing that the amideband of 7S and 11S Globulins with two extraction methods consisted of eight bands. The I band frequencies were assigned to α-helix, β-sheet, unordered and turn structure. The second derivative spectra of 7S and 11S Globulins had been shifted with reverse micellar extraction method compared with their spectra with aqueous buffer extraction method. The relative amount of different structure of 7S and 11S Globulins could be estimated through accurate measurement of the band intensities. The results indicated that the percentage of 7S globulin α-helix and β-sheet, turn structures decreased with the reverse micelles extraction (7S globulin: 14.5% α-helix, 45.6% β-sheet, 14.4% unordered, 23.8% turn; 11S globulin: 17.0% α-helix, 47.3% β-sheet, 16.5% unordered, 19.3% turn), compared with 7S (16.5% α-helix, 47.6% β-sheet, 35.9% turn) and 11S (17.0% α-helix, 47.3% β-sheet, 35.8% turn) Globulins by the aqueous buffer extraction, while the percentage of 11S globulin α-helix and β-sheet structures did not change. The percentage of unordered structure was 14.4 and 16.5, respectively. The amount change of these substructures might affect functional properties of 7S and 11S Globulins.
Luiz G. Santoro - One of the best experts on this subject based on the ideXlab platform.
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Globulin and albumin proteins in dehulled seeds of three Phaseolus vulgaris cultivars
Plant Foods for Human Nutrition, 1997Co-Authors: Eliana P. Chagas, Luiz G. SantoroAbstract:Albumin and globulin fractions, obtained after modifications of the Osborne's fractionation scheme, were investigated in the seeds of three cultivars of Phaseolus vulgaris, after removal of the seed coats, to prevent interactions of tannins and phenols with the Globulins. Also, by using an appropriate buffer to separate the Globulins more efficiently, no cross-contaminations were observed in SDS-PAGE between these two fractions. The combination of these two procedures resulted in globulin to albumin ratios 70percnt higher than those published previously with the same cultivars. Amino acid compositions of total globulin, phaseolin and albumin fractions are presented. Whereas the albumins contained much more cysteine than the Globulins, the concentrations of methionine were evenly distributed in these two fractions. Also, the bulk of methionine was found in phaseolin; cysteine was found in non-phaseolin proteins. In addition, the Globulins contained unexpectedly high amounts of lysine.
H Orozco - One of the best experts on this subject based on the ideXlab platform.
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prophylactic effect of administration of human gamma Globulins in a mouse model of tuberculosis
Tuberculosis, 2009Co-Authors: Nesty Olivares, Alina Puig, Diana Aguilar, Aniel Moya, Armando Cadiz, Oscar Otero, Luis Izquierdo, Gustavo Falero, Rosa L Solis, H OrozcoAbstract:Summary The protective effect of human gamma Globulins on Mycobacterium tuberculosis infection was evaluated in a mouse model of intratracheal infection. Animals receiving human gamma Globulins intranasally, 2 h before intratracheal challenge showed a significant decrease in lung bacilli load compared to non-treated animals in different time intervals of up to 2 months after challenge. The same effect was obtained when M. tuberculosis was pre-incubated with the gamma globulin before challenge. The protective effect of the gamma-globulin formulation was abolished after pre-incubation with M. tuberculosis. These results suggest a potential role of specific antibodies in the defence against mycobacterial infections.
Xiaoyan Zhao - One of the best experts on this subject based on the ideXlab platform.
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determination of the domain structure of the 7s and 11s Globulins from soy proteins by xrd and ftir
Journal of the Science of Food and Agriculture, 2013Co-Authors: Jun Chen, Xiangyan Chen, Qingjun Zhu, Fengliang Chen, Xiaoyan ZhaoAbstract:BACKGROUND The 7S and 11S fractions from soybean proteins have interesting high nutritional and excellent functional properties. The aim of this research was to improve the functional properties of soy proteins by studying the effect of bis(2-ethylhexyl) sodium sulfosuccinate (AOT) reverse micelles on the conformation of the 7S and 11S Globulins using Fourier transform infrared and X-ray diffraction spectroscopy. RESULTS Fourier transform infrared revealed that the intensity of the 7S and 11S globulin bands from AOT reverse micelle extraction at 1600–1700, 1480–1575, 1220–1300, 3330, 1448 and 1395 cm−1 was higher than from aqueous buffer. X-ray diffraction data showed that the intensities of 7S globulin using two extraction methods at 2θ about 10° were significantly different (P < 0.05), about 22° slightly increased. The intensities of 11S globulin at 2θ about 10° and 22° were similar. The average distance between particles (dhkl) for 7S globulin with aqueous buffer extraction at 2θ about 10° was greater than AOT reverse micelle extraction. CONCLUSION This study showed the potential of reverse micelles as a protocol for extracting the 7S and 11S Globulins for analytical purposes. The results represent a new avenue for determining the structures of the 7S and 11S Globulins. © 2012 Society of Chemical Industry
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effects of aot reverse micelle on properties of soy Globulins
Food Chemistry, 2008Co-Authors: Xiaoyan Zhao, Fusheng Chen, Junqi Chen, Guosheng Gai, Wentong XueAbstract:Abstract This study was focused on the influence of AOT reverse micelle on physical–chemical properties of 7S and 11S Globulins from soy proteins, and compared with aqueous buffer extraction. The results showed that the contents of the surface hydrophobicity and SH groups of 7S and 11S Globulins and SS bonds of 11S globulin, using AOT reverse micelle extraction, were augmented, and SS bonds of 7S globulin decreased. The thermal and rheological properties of 7S and 11S Globulins extracted using the two methods were studied by differential scanning calorimetry (DSC) and rheometery. It was found that the peak denaturation temperature and heat of transition of 7S and 11S Globulins with aqueous buffer extraction were different from that with AOT reverse micellar extraction. The AOT reverse micelle did not affect the gel properties of 11S globulin, while it influenced 7S globulin’s. Hardness, springiness, gumminess, adhesiveness and chewiness of 7S globulin from AOT reverse micelle were lower than that from aqueous buffer extraction, but gumminess was higher.
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ftir spectra studies on the secondary structures of 7s and 11s Globulins from soybean proteins using aot reverse micellar extraction
Food Hydrocolloids, 2008Co-Authors: Xiaoyan Zhao, Fusheng Chen, Wentong Xue, Lite LeeAbstract:Fourier transform infrared (FTIR) method was used to study the secondary structures of 7S and 11S Globulins from soybean proteins using aqueous buffer and reverse micelles extraction method for the first time. The Fourier second derivative was applied to all spectra, revealing that the amideband of 7S and 11S Globulins with two extraction methods consisted of eight bands. The I band frequencies were assigned to α-helix, β-sheet, unordered and turn structure. The second derivative spectra of 7S and 11S Globulins had been shifted with reverse micellar extraction method compared with their spectra with aqueous buffer extraction method. The relative amount of different structure of 7S and 11S Globulins could be estimated through accurate measurement of the band intensities. The results indicated that the percentage of 7S globulin α-helix and β-sheet, turn structures decreased with the reverse micelles extraction (7S globulin: 14.5% α-helix, 45.6% β-sheet, 14.4% unordered, 23.8% turn; 11S globulin: 17.0% α-helix, 47.3% β-sheet, 16.5% unordered, 19.3% turn), compared with 7S (16.5% α-helix, 47.6% β-sheet, 35.9% turn) and 11S (17.0% α-helix, 47.3% β-sheet, 35.8% turn) Globulins by the aqueous buffer extraction, while the percentage of 11S globulin α-helix and β-sheet structures did not change. The percentage of unordered structure was 14.4 and 16.5, respectively. The amount change of these substructures might affect functional properties of 7S and 11S Globulins.
Eliana P. Chagas - One of the best experts on this subject based on the ideXlab platform.
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Globulin and albumin proteins in dehulled seeds of three Phaseolus vulgaris cultivars
Plant Foods for Human Nutrition, 1997Co-Authors: Eliana P. Chagas, Luiz G. SantoroAbstract:Albumin and globulin fractions, obtained after modifications of the Osborne's fractionation scheme, were investigated in the seeds of three cultivars of Phaseolus vulgaris, after removal of the seed coats, to prevent interactions of tannins and phenols with the Globulins. Also, by using an appropriate buffer to separate the Globulins more efficiently, no cross-contaminations were observed in SDS-PAGE between these two fractions. The combination of these two procedures resulted in globulin to albumin ratios 70percnt higher than those published previously with the same cultivars. Amino acid compositions of total globulin, phaseolin and albumin fractions are presented. Whereas the albumins contained much more cysteine than the Globulins, the concentrations of methionine were evenly distributed in these two fractions. Also, the bulk of methionine was found in phaseolin; cysteine was found in non-phaseolin proteins. In addition, the Globulins contained unexpectedly high amounts of lysine.