Entity

Time filter

Source Type


Gu X.,Key Laboratory of Feed Biotechnology | Yao T.,Chinese Academy of Agricultural Sciences
Journal of Environmental Science and Health - Part B Pesticides, Food Contaminants, and Agricultural Wastes | Year: 2013

The bioconcentration and elimination of racemic benalaxyl (BX) in trout liver microsomes and in juvenile rainbow trout (Oncorhynchus mykiss) were investigated to determine whether the fish can bioconcentrate and degrade this fungicide enantioselectively. Both enantiomers of BX were extracted with organic solvents and evaluated using high-performance liquid chromatography. In the microsomes, BX degradation followed first-order kinetics, and the S-(+) enantiomer of BX was eliminated twice as rapidly as the R-(-) enantiomer, resulting in residues enriched for R-(-)-BX. In vivo experiment, chiral analysis showed an obvious selective bioconcentration of BX based on statistically altered enantiomer fractions (EFs) in the fish compared with the values in the water. The R-(-)-BX was initially preferentially bioconcentrated by rainbow trout and then dissipated more slowly than its antipode. The mean half-lives for individual enantiomers were calculated as 31.6 h for R-(-)-BX and 20.3 h for the S-(+)-form. The results of the study showed that the degradation of BX enantiomers was stereoselective in rainbow trout. © 2013 Copyright Taylor and Francis Group, LLC. Source


Wang J.,Key Laboratory of Feed Biotechnology | Wang J.,Chinese Academy of Agricultural Sciences | Tian Z.,Key Laboratory of Feed Biotechnology | Tian Z.,Chinese Academy of Agricultural Sciences
BioMetals | Year: 2010

This is a short preface of this Special Issue Lactoferrin, it described the major points of key reporters in 'The 9th International Conference on LF Structure, Function and Applications' in Beijing in late Autumn 2009, and the major articles published in this issue. A panaroma and the lastest advances of lactoferrin R&D during past two years (2007-2009) was tried to extract. © 2010 Springer Science+Business Media, LLC. Source


Liu B.,Key Laboratory of Feed Biotechnology | Liu B.,Chinese Academy of Agricultural Sciences | Teng D.,Key Laboratory of Feed Biotechnology | Teng D.,Chinese Academy of Agricultural Sciences | And 4 more authors.
Journal of Agricultural and Food Chemistry | Year: 2013

The full-length cDNA sequence of Gly m Bd 28K was chemically synthesized and expressed in Escherichia coli (E. coli) BL21 (DE3) as an inclusion body under the induction of 0.2 mmol/L of isopropyl β-d-1-thiogalactopyranoside (IPTG). The purity of the recombinant protein was over 90% following Ni-nitrilotriacetic acid (Ni-NTA) affinity chromatography, and its molecular weight was 29.71 kDa. The polyclonal antibody (pAB) against Gly m Bd 28K was prepared and referred to as pAB-28K, and it exhibited high specificity for the protein in soybean meal. We established an indirect enzyme-linked immunosorbent assay (iELISA) using the pAB-28K and the recombinant Gly m Bd 28K protein to determine the Gly m Bd 28K content in soybean products. The R2 value of the standard curve was 0.9910, the average relative standard deviation (RSD) was 16.93%, and the average recovery was 95.50%, which indicated that the iELISA was highly reproducible and accurate. Therefore, the pAB-28K and the iELISA provide valuable tools for the rapid and sensitive detection of Gly m Bd 28K in food and feed products from soybeans. This protocol meets the technical requirements for quality control and food safety as related to soybean. © 2013 American Chemical Society. Source


Wang X.,Key Laboratory of Feed Biotechnology | Wang X.,Chinese Academy of Agricultural Sciences | Teng D.,Key Laboratory of Feed Biotechnology | Teng D.,Chinese Academy of Agricultural Sciences | And 6 more authors.
Journal of Agricultural and Food Chemistry | Year: 2012

Three methods of DNA extraction from feed products and four detection methods for the 5′-junction fragment of genetically modified (GM) Roundup Ready soybean (RRS) were compared and evaluated. The DNA extraction methods, including cetyltrimethylammonium bromide (CTAB), sodium dodecyl sulfate (SDS), and guanidine hydrochloride (Kit), were assessed for their yields and purity of DNA, extraction time, and reagent cost. The DNA yields of CTAB, SDS, and Kit were 52-694, 164-1750 and 23-105 ng/mg sample, and their extraction time was 2.5-3, 2-2.5, and 1.5-2 h with reagent cost about US dollar 0.24, 0.13, and 1.9 per extraction, respectively. The SDS method was generally well suited to all kinds of feed matrices tested. The limits of detection for the four amplification protocols, including loop-mediated isothermal amplification (LAMP), hyperbranched rolling circle amplification (HRCA), conventional polymerase chain reaction (PCR), and real-time PCR, were 48.5, 4.85, 485, and 9 copies of the pTLH10 plasmid, respectively. The ranked results of the four detection methods were based on multiattribute utility theory as follows (from best to worse): HRCA, LAMP, PCR, and real-time PCR. This comparative evaluation was specifically useful for selection of a highly efficient DNA extraction or amplification method for detecting different GM ingredients. © 2012 American Chemical Society. Source


Liu B.,Key Laboratory of Feed Biotechnology | Liu B.,Chinese Academy of Agricultural Sciences | Teng D.,Key Laboratory of Feed Biotechnology | Teng D.,Chinese Academy of Agricultural Sciences | And 6 more authors.
Applied Microbiology and Biotechnology | Year: 2012

To detect the soybean allergen P34 (Gly m Bd 30K) from soybean products, the full-length cDNA sequence of P34 was synthesized and inserted into the prokaryotic expression vector pET-28a. The P34 protein was expressed in Escherichia coli BL21 (DE3) as an inclusion body under the induction of 0.8 mmol/L isopropyl β-D-1-thiogalactopyranoside. After purification with His-Bind affinity chromatography, the purity quotient of the recombinant protein was over 92%, and its molecular weight (approximately 33 kDa) was very close to that of the native soybean P34. The polyclonal antibody (pAB) against P34 was prepared with the purified recombinant P34. The generated pAB, named as pAB-P34, exhibited high specificity to the P34 protein of the soybean meal. The indirect enzyme-linked immunosorbent assay (iELISA) based on pAB-P34 was established to determine the P34 content of soybean products. The CVs of the recovery tests of P34 were less than 7.77%, which indicated that iELISA had high reproducibility and accuracy. Therefore, the recombinant P34 produced in the E. coli expression system, the prepared pAB-P34, and the developed iELISA could provide a valuable tool for sensitive detection of P34 in various soybean products and for future studies on allergies related to soybean P34. © Springer-Verlag 2012. Source

Discover hidden collaborations