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Huang L.,Guangzhou City Polytechnic | Peng S.,Guangzhou City Polytechnic | Li H.,Guangzhou City Polytechnic | Zhang Y.,Sericulture and Agri Food Research Institute GAAS | Chen L.,Guangzhou City Polytechnic
Journal of the Chinese Cereals and Oils Association | Year: 2013

In the storage conditions with normal room temperature and obturation for soybean protein isolated (SPI), SPI functional properties gradually decreased with the extension of storage time. High pressure microfluidization can improve SPI functional properties after long-term storage. The results showed that SPI solution protein content decreased with increase number of homogeneity under 3 times, while it is increased with increase pressure at 30, 60, 90 and 120 MPa, respectively. The soluble protein content decreased with increase storage time of 0, 120, 240 and 360 d. SPI soluble protein content has been significantly improved by microfluidization of 120 MPa and 2 times. SPI emulsification activity also significantly decreased with the storage time in different pH. Emulsifying activity and emulsion stability have been significantly improved by microfluidization. SPI foaming characteristic significantly decreased with prolonged storage time. Foaming and foaming stability have been significantly improved by microfluidization. Elastic modulus of 360 d SPI thermal gelation significantly increased from 563 Pa to 2527 Pa by microfluidization. Source


Huang L.-H.,Guangzhou City Polytechnic | Zhang Y.-H.,Sericulture and Agri Food Research Institute GAAS | Li H.-B.,Guangzhou City Polytechnic
Modern Food Science and Technology | Year: 2014

High-temperature soybean meal was hydrolyzed by Alcalase and papain, respectively. Six kinds of hydrolysates were obtained with the degrees of hydrolysis (DH) of 5%, 10%, and 15%. Effects of Alcalase and papain on physicochemical properties of these different hydrolysates were evaluated. The results showed that Alcalase and papain were all produced six kinds of hydrolysates with different ranges of molecular weight. The proportions of hydrolysates from different enzymes had significant differences (P<0.5), and the average molecular weight of hydrolysates was gradually decreased with increasing the DH. Alcalase included more peptides that less than 2562 Da compared with papain at the same DH. The significant difference of amount between exposed and destruct of hydrophobic groups in enzymatic reactions resulted in surface hydrophobicity decreased firstly with the increasing DH and then increased. Therefore, the hydrolysates with DH of 10% had the minimum surface hydrophobicity than the others. The absolute values of zeta potential increased with increasing DH, and the intermolecular repulsion of molecules increased synchronously. The effect of Alcalase and papain on zeta potential had no significant difference at the same DH. Moreover, at pH 3, 5, 7 and 9, the solubility of the hydrolysates increased gradually with increasing DH, and the emulsifying activity index and emulsion stability index exhibited decreasing trends with increasing DH. Source


Zhang Y.,Sericulture and Agri Food Research Institute GAAS | Huang L.,Guangzhou City Polytechnic | Ting S.,Sericulture and Agri Food Research Institute GAAS | Wang S.,Sericulture and Agri Food Research Institute GAAS | Lin Y.,Sericulture and Agri Food Research Institute GAAS
Digest Journal of Nanomaterials and Biostructures | Year: 2014

Self-assembly of globulin fibrils as nanoscale material exhibited unique properties. To gain insight into the effect of various electrostatic screening on the aggregates and gels structure of rice bran globulin(RBG), a kinetic process of rice bran globulin(RBG) turbidity and gelation were performed. The absorbance of solutions and required time of gelation are all reveal significant differences at various ionic strengths. AFM images showed the assembling morphology of RBG fibrils, a string beads transformed to branched cluster, when electrostatic repulsive forces attenuated gradually with increasing ionic strength. The gel strength increased with increasing ionic strength and protein concentration. A simulated phase diagram had been drawn, according to the actual state and color of solution and gel. A dense granular structure of gel network was observed, and a more intensive structure present at low ionic strength. A hypothetical pathway for possible RBG gel formation was promoted understanding of nano-structure. Source


Huang L.,Guangzhou City Polytechnic | Zhang Y.,Sericulture and Agri Food Research Institute GAAS | Li H.,Guangzhou City Polytechnic
Journal of Nanomaterials | Year: 2014

The effects of various ionic strengths and protein concentrations on the fibrils structure and gel properties of rice bran globulin (RBG) at pH 2.0 were investigated using atomic force microscopy (AFM), rheometer, and scanning electron microscope (SEM). AFM images showed the morphology of assembling RBG fibrils from strand beads to becoming branch clustered, when electrostatic repulsive forces attenuated gradually with increasing ionic strength. NaCl seems to accelerate the kinetics of fibrils formation, resulting in a significant increase in Th T fluorescence intensity. The increased ionic strengths promote particle size increasing and zeta potential decreasing synchronously. The percolation model G' (C - Cp)n be used to calculate theoretical RBG gels concentration at various ionic strengths (0-500 mM), which decreased from 15.17 ± 0.63 to 2.26 ± 0.27 wt%. SEM images exhibited a granular mesh-like gel structure. A more homogenous structure occurred in low ionic strength. This study elucidates properties of RBG fibrils and gels as a bioactive material. © 2014 Lihua Huang et al. Source


Li L.,Sericulture and Agri Food Research Institute GAAS | Xing D.-X.,Sericulture and Agri Food Research Institute GAAS | Li Q.-R.,Sericulture and Agri Food Research Institute GAAS | Xiao Y.,Sericulture and Agri Food Research Institute GAAS | And 2 more authors.
PLoS ONE | Year: 2014

Albendazole is a broad-spectrum parasiticide with high effectiveness and low host toxicity. No method is currently available for measuring albendazole and its metabolites in silkworm hemolymph. This study describes a rapid, selective, sensitive, synchronous and reliable detection method for albendazole and its metabolites in silkworm hemolymph using ultrafast liquid chromatography tandem triple quadrupole mass spectrometry (UFLC-MS/MS). The method is liquid-liquid extraction followed by UFLC separation and quantification in an MS/MS system with positive electrospray ionization in multiple reaction monitoring mode. Precursor-to-product ion transitions were monitored at 266.100 to 234.100 for albendazole (ABZ), 282.200 to 208.100 for albendazole sulfoxide (ABZSO), 298.200 to 159.100 for albendazole sulfone (ABZSO2) and 240.200 to 133.100 for albendazole amino sulfone (ABZSO2-NH2). Calibration curves had good linearities with R2of 0.9905-0.9972. Limits of quantitation (LOQs) were 1.32 ng/mL for ABZ, 16.67 ng/mL for ABZSO, 0.76 ng/mL for ABZSO2and 5.94 ng/mL for ABZSO2-NH2. Recoveries were 93.12%-103.83% for ABZ, 66.51%-108.51% for ABZSO, 96.85%-105.6% for ABZSO2and 96.46%-106.14% for ABZSO2-NH2, (RSDs ,8%). Accuracy, precision and stability tests showed acceptable variation in quality control (QC) samples. This analytical method successfully determined albendazole and its metabolites in silkworm hemolymph in a pharmacokinetic study. The results of single-dose treatment suggested that the concentrations of ABZ, ABZSO and ABZSO2increased and then fell, while ABZSO2-NH2level was low without obvious change. Different trends were observed for multi-dose treatment, with concentrations of ABZSO and ABZSO2rising over time. © 2014 Li et al. Source

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