Key Laboratory of Feed Biotechnology

Beijing, China

Key Laboratory of Feed Biotechnology

Beijing, China
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Wang X.,Key Laboratory of Feed Biotechnology | Hao Y.,Key Laboratory of Feed Biotechnology | Teng D.,Chinese Academy of Agricultural Sciences | Wang J.,Key Laboratory of Feed Biotechnology
Biochemistry and Cell Biology | Year: 2017

Lactoferrin (Lf), a multifunctional glycoprotein, is an important antimicrobial and immune regulatory protein present in neutrophils and most exocrine secretions of mammals. Lactoferricin (Lfcin) is located in the N-terminal region of this protein. In this review, the current state of research into Lf and Lfcin in China is described. Searching with HistCite software in Web Sci located 118 papers published by Chinese researchers from 2011-2015, making China one of the top 3 producers of Lf research and development in the world. The biological functions of Lf and Lfcin are discussed, including antibacterial, antiviral, antifungal, anticarcinogenic, and anti-inflammatory activities; targeted drug delivery, induction of neurocyte, osteoblast, and tenocyte growth, and possible mechanisms of action. The preparation and heterologous expression of Lf in animals, bacteria, and yeast are discussed in detail. Five Lf-related food additive factories and 9 Lf-related health food production companies are certified by the China Food and Drug Administration (CFDA). The latest progress in the generation of transgenic livestock in China, the safety of the use of transgenic animals, and future prospects for the uses of Lf and Lfcin are also covered. © 2017 Published by NRC Research Press.

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.

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.
Food Control | Year: 2013

LAMP-LFD, loop-mediated isothermal amplification (LAMP) combined with a lateral-flow dipstick (LFD), was developed and evaluated as a new method for the detection of Roundup Ready soybean (RRS). Biotinylated LAMP amplicons were produced by two sets of six designed primers that specifically recognized the endogenous gene (Lec1) and the event-specific 5' -junction region (G35S) of RRS followed by hybridization with FITC-labeled probes and LFD detection. The following optimized conditions for the LAMP assay were used: deoxynucleotide triphosphate (dNTP) concentrations ranging from 0.6 to 3.2 mM, 6 mM Mg 2+, 4 U Bst DNA polymerase and a 1:6 ratio of outer to inner primers. The LAMP-LFD results were generated within 50 min. The detection limit of LAMP-LFD was 2.4 copies of the linearized plasmid pTLH10 and was 20 times more sensitive than conventional PCR. We demonstrated the high specificity of LAMP-LFD by testing processed soybean products, genetically modified (GM) maize and Bt-cotton meal. The novel LAMP-LFD setup presented here is simple, rapid, and has the potential for future use in the detection of GM ingredients in feed and food products. © 2012 Elsevier Ltd.

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.

Zhang Y.,Key Laboratory of Feed Biotechnology | Zhang Y.,Chinese Academy of Agricultural Sciences | Teng D.,Key Laboratory of Feed Biotechnology | Teng D.,Chinese Academy of Agricultural Sciences | And 10 more authors.
Applied Microbiology and Biotechnology | Year: 2014

NZ2114, a new variant of plectasin, was overexpressed in Pichia pastoris X-33 via pPICZαA for the first time. The total secreted protein of fermentation supernatant reached 2,390 mg/l (29 C) and 2,310 mg/l (25 C), and the recombinant NZ2114 (rNZ2114) reached 860 mg/l (29 C) and 1,309 mg/l (25 C) at 96 h induction in a 5-l fermentor, respectively.The rNZ2114 was purified by cation exchange chromatography, and its yield was 583 mg/l with 94.8 % purity. The minimal inhibitory concentration (MIC) of rNZ2114 to four ATCC strains of Staphyloccocus aureus was evaluated from 0.028 to 0.90 μM. Meanwhile, it showed potent activity (0.11-0.90 μM) to 20 clinical isolates of MRSA. The rNZ2114 killed over 99.9 % of tested S. aureus (ATCC 25923 and ATCC 43300) in Mueller-Hinton medium within 6 h when treated with 4 × MIC. The postantibiotic effect of rNZ2114 to S. aureus ATCC 25923 and ATCC 43300 was 18.6-45.6 and 1.7-3.5 h under 1×, 2×, and 4× MIC, respectively. The fractional inhibitory concentration index (FICI) indicated a synergistic effect between rNZ2114 and kanamycin, streptomycin, and vancomycin against S. aureus ATCC 25923 (FICI = 0.125), and additivity between rNZ2114 and ampicillin, spectinomycin (FICI = 0.625), respectively. To S. aureus ATCC 43300 [methicillin-resistant S. aureus (MRSA)], rNZ2114 showed a synergistic effect (FICI = 0.125-0.3125) with kanamycin, ampicillin, streptomycin, and vancomycin, and antagonism with spectinomycin (FICI = 8.0625). The rNZ2114 caused only less than 0.1 % hemolytic activity in the concentration of 128 μg/ml, and showed a good thermostability from 20 to 80 C. In addition, it exhibited the highest activity at pH 8.0. These results suggested that large-scale production of NZ2114 is feasible using the P. pastoris expression system, and it could be a new potential antimicrobial agent for the prevention and treatment of S. aureus especially for MRSA infections. © 2013 Springer-Verlag Berlin Heidelberg.

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.

PubMed | Key Laboratory of Feed Biotechnology
Type: Journal Article | Journal: Applied microbiology and biotechnology | Year: 2016

Colibacillosis, caused by pathogenic Escherichia coli, is a common disease in animals and human worldwide with extensive losses in breeding industry and with millions of people death annually. There is thus an urgent need for the development of universal vaccines against colibacillosis. In this study, the BamA protein was analyzed in silico for sequence homology, physicochemical properties, allergenic prediction, and epitopes prediction. The BamA protein (containing 286 amino acids) clusters in E. coli were retrieved in UniProtKB database, in which 81.7% sequences were identical (Uniref entry A7ZHR7), and sequences with 94.82% identity were above 93.4%. Moreover, BamA was highly conserved among Salmonella and Shigella and has no allergenicity to mice and human. The epitopes of BamA were located principally in periplasm and extracellular domain. Surf_Ag_VNR domain (at position 448-810 aa) of BamA was expressed, purified, and then used for immunization of mice. Titers of the rBamA sera were 1:736,000 and 1:152,000 against rBamA and E. coli and over 1:27,000 against Salmonella and Shigella. Opsonophagocytosis result revealed that the rBamA sera strengthened the phagocytic activity of neutrophils against E. coli. The survival rate of mice vaccinated with rBamA and PBS was 80 and 20%, respectively. These data indicated that BamA could serve as a promising universal vaccine candidate for the development of a protective subunit vaccine against bacterial infection. Thus, the above protocol would provide more feasible technical clues and choices for available control of pathogenic E. coli, Salmonella, and Shigella.

PubMed | Key Laboratory of Feed Biotechnology
Type: Journal Article | Journal: Applied biochemistry and biotechnology | Year: 2016

Peanut meal (PM) is limited in practical use (feed or food) from imbalance of amino acid profile and denaturation of protein. Fermentation was used to promote its nutritional and functional properties by single-factor experiments and orthogonal experiments. Results showed that the nutritional properties of fermented peanut meal (crude protein content, dry matter content, ash content, acid soluble oligopeptides content, in vitro digestibility, and content of organic acids) had a significant increase (P<0.05 or P<0.01) and more importantly, the content of amino acids was balanced by fermentation. In addition, fermented peanut meal possessed better antioxidant activities in the areas of reducing power, 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging activity, hydroxyl radical scavenging activity, and metal chelating activity (P<0.05 or P<0.01). These results implied that the nutritional and antioxidant properties of peanut meal were improved effectively by biological modification, which could be valuable in terms of nutrition and protein resources. It is great of importance to meet requirement of raw materials for husbandry in China when facing a huge lacking of feedstuff, especially for protein feed with an over 80% import amount depending from other countries yearly.

A marine arenicin-3 derivative, N4, displayed potent antibacterial activity against Gram-negative bacteria, but its antibacterial mode of action remains elusive. The mechanism of action of N4 against pathogenic Escherichia coli was first researched by combined cytological and transcriptomic techniques in this study. The N4 peptide permeabilized the outer membrane within 1 min, disrupted the plasma membrane after 0.5 h, and localized in the cytoplasm within 5 min. Gel retardation and circular dichroism (CD) spectrum analyses demonstrated that N4 bound specifically to DNA and disrupted the DNA conformation from the B type to the C type. N4 inhibited 21.1% of the DNA and 20.6% of the RNA synthesis within 15 min. Several hallmarks of apoptosis-like cell death were exhibited by N4-induced E. coli, such as cell cycle arrest in the replication (R) and division(D) phases, reactive oxygen species production, depolarization of the plasma membrane potential, and chromatin condensation within 0.5 h. Deformed cell morphology, disappearance of the plasma membrane, leakage of the contents, and ghost cell formation were demonstrated by transmission electron microscopy, and nearly 100% of the bacteria were killed by N4. A total of 428 to 663 differentially expressed genes are involved in the response to N4, which are associated mainly with membrane biogenesis (53.9% to 56.7%) and DNA binding (13.3% to 14.9%). N4-protected mice that were lethally challenged with lipopolysaccharide (LPS) exhibited reduced levels of interleukin-6 (IL-6), IL-1, and tumor necrosis factor alpha (TNF-) in serum and protected the lungs from LPS-induced injury. These data facilitate an enhanced understanding of the mechanisms of marine antimicrobial peptides (AMPs) against Gram-negative bacteria and provide guidelines in developing and applying novel multitarget AMPs in the field of unlimited marine resources as therapeutics.

PubMed | Key Laboratory of Feed Biotechnology
Type: Journal Article | Journal: Applied microbiology and biotechnology | Year: 2016

This work is the first to report the antibacterial characteristics and antibacterial mechanisms of MP1102, which is a variant of NZ2114, against pathogenic Clostridium perfringens. MP1102 exhibited strong antimicrobial activity against C. perfringens strains CVCC 61, CVCC 1163, and CVCC 2032 at a low minimal inhibitory concentration (MIC) of 0.91M. MP1102 showed anti-C. perfringens activity over a wide pH range of 2.0 and 10.0, high thermal stability from 20 to 80C, and remarkable resistance to pepsin. The fractional inhibitory concentration index (FICI) indicated an additive or synergic effect between MP1102 and bacitracin zinc, nisin, vancomycin, virginiamycin, aureomycin, and ampicillin against C. perfringens (FICI=0.3125-1.0). To further elucidate the antibacterial mechanism of MP1102, its effect on the C. perfringens CVCC 61 cell membrane and intracellular DNA was studied. Flow cytometry and scanning electron microscopy (SEM) indicated that MP1102 treatment resulted in the release of cellular contents by damaging the membrane. A DNA gel retardation and circular dichroism analysis demonstrated that MP1102 interacted with DNA and intercalated into the DNA base pairs. A cell cycle assay demonstrated that MP1102 affected cellular functions, such as DNA synthesis. These results suggested that MP1102 exhibited potential as a new antimicrobial agent against C. perfringens infections.

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