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RISS 인기검색어
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- 저자 : Xu Jiaping (검색결과 3 건)
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Effects of Fermented Rapeseed Meal on Growth Performance and Serum Parameters in Ducks
Fazhi, Xu,Lvmu, Li,Jiaping, Xu,Kun, Qian,Zhide, Zhang,Zhangyi, Liang Asian Australasian Association of Animal Productio 2011 Animal Bioscience Vol.24 No.5
A trial was performed to study the effects of feeding a diet containing solid-state fermentation rapeseed meal (FRSM) replaced soybean meal (SBM) on growth performance and serum biochemistry parameters of ducks and then to determine the appropriate proportion of soybean meal replacement. The 75% rapeseed meal and 25% blood meal were mixed and inoculated with the Lactobacillus plantarum and Bacillus subtilis. Over the 21-day fermentation, isothiocyanates were reduced from 72.7 to 14.1 mmol/kg. A total of 1,280 fifteen-day-old Cherry Valley ducks were randomly allocated into 4 dietary treatments, 4 replicate groups of 80 ducks each for a 30-day feeding trial. In four treatment groups, fermentation rapeseed meal replaced soybean meal at 0, 33, 67 or 100%, respectively. Results showed that feed intake of ducks fed 100% FRSM was greater (p<0.05) than SBM and partial FRSM in both the finishing period (31-45 d) and entire feeding period (15-45 d). Daily gain increased gradually in the three treatment groups with augmenting FRSM over in the whole study period. In the growing period (15-30 d), compared with the SBM group, phosphorus and calcium content in serum from the FRSM group was improved (p<0.05). Total protein concentration was lower in ducks fed 100% FRSM than SBM and 33% FRSM (p<0.05). Concentrations of IgM were dramatically higher for animals fed 100% FRSM than in the SBM, 33% FRSM and 67% FRSM groups. In the finishing trail stage (31-45 d), only serum IgG content in 100% FRSM group was improved (p<0.05). Therefore, rapeseed meal fermented with Lactobacillus plantarum and Bacillus subtilis is a promising alternative protein source and fermented rapeseed meal can completely replace soybean meal in duck diet and potentially reduce the cost of duck production.
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Feng Xu,Tingting Tao,Qiangwen Chen,Xiangxiang Meng,Jiaping Yan,Jie Chang 한국유전학회 2016 Genes & Genomics Vol.38 No.12
3-Hydroxy-3-methylglutaryl-CoA synthase (HMGS) catalyzes the condensation of acetyl-CoA and acetoacetyl- CoA to form 3-hydroxy-3-methylglutaryl-CoA as the first committed enzyme in the mevalonate (MVA) pathway. HMGS plays an important role in the biosynthesis of the sesquiterpene, which is the main constituent of essential oil in Matricaria chamomilla. In this paper, a HMGS gene designated as McHMGS (GenBank Accession No. KU529970) was successfully cloned from M. chamomilla. The full-length cDNA of McHMGS was 1495-bp and contained a 1374-bp open reading frame. It encoded a 458-amino-acid protein with a calculated molecular weight of about 50.7 kDa and isoelectric point of 5.69. Sequence comparison revealed that McHMGS showed extensive homology with HMGSs from other plant species. Phylogenetic tree analysis indicated that McHMGS is clustered with the HMGS of Asteraceae in the dicotyledoneae clade. Further functional complementation of McHMGS in hmgsdeficient mutant yeast strain YSC6274 demonstrated that cloned McHMGS cDNA encodes a functional HMGS and mediates the MVA biosynthesis in yeasts. The tissue expression pattern analysis revealed that McHMGS expression level is highest in the flowers and lowest in the stems. Quantitative real-time PCR analysis showed that the expression of McHMGS was induced by MeJA, and the expression level is highest 24 h after induction. The characterization and expression of McHMGS can help in further studying the role of McHMGS gene in the biosynthesis of sesquiterpene in M. chamomilla.
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Yao Qin,Hu Zhigang,Xu Jiaping,Chen Keping Korean Society of Sericultural Science 2005 International Journal of Industrial Entomology Vol.10 No.2
Ribosome-associated membrane protein 4 (RAMP4) is a membrane protein that exposes its N-terminal hydrophilic portion on the cytoplasmic side and spans the membrane close to the C-terminal end. RAMP4 has previously been reported to belong to the set of proteins that remains associated with membrane-bound ribosomes, and controls the glycosylation of major histocompatbility complex class II-associated invariant chain. RAMP4 also may be relative to the stabilization of membrane proteins in response to stress, with other components of translocon, and molecular chaperons in ER. Application of 5'-RACE technique with specially designed primer, we cloned a 715 bp cDNA fragment which contains a 195 bp ORF, termed RAMP4. The deduced protein has 64 amino acid residues and contains a putative transmembrane-spanning domain at the COOH terminus.
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