• Title/Summary/Keyword: feed bin

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Gene Cloning, Expression, and Characterization of a Novel ${\beta}$-Mannanase from Bacillus circulans CGMCC 1416

  • Li, Yanan;Yang, Peilong;Meng, Kun;Wang, Yaru;Luo, Huiying;Wu, Ningfeng;Fan, Yuliu;Yao, Bin
    • Journal of Microbiology and Biotechnology
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    • v.18 no.1
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    • pp.160-166
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    • 2008
  • A DNA fragment containing 2,079 base pairs from Bacillus circulans CGMCC 1416 was cloned using degenerate PCR and inverse PCR. An open reading frame containing 981 bp was identified that encoding 326 amino acids residues, including a putative signal peptide of 31 residues. The deduced amino acid sequence showed the highest identity (68.1%) with $endo-{\beta}-1,4-D-mannanase$ from Bacillus circulans strain K-1 of the glycoside hydrolase family 5 (GH5). The sequence encoding the mature protein was cloned into the pET-22b(+) vector and expressed in Escherichia coli as a recombinant fusion protein containing an N-terminal hexahistidine sequence. The fusion protein was purified by $Ni^{2+}$ affinity chromatography and its hexahistidine tag cleaved to yield a 31-kDa ${\beta}$-mannanase having a specific activity of 481.55U/mg. The optimal activity of the purified protein, MANB48, was at $58^{\circ}C$ and pH 7.6. The hydrolysis product on substrate locust bean gum included a monosaccharide and mainly oligosaccharides. The recombinant MANB48 may be of potential use in the feed industry.

Field evaluation of Enterotoxigenic Escherichia coli-specific bacteriophage (ΦCJ19) as a feed additive (Enterotoxigenic Escherichia coli 특이 박테리오파지 (ΦCJ19)의 사료 첨가제로서의 사양 평가)

  • Yoo, Anna;Cha, Seung Bin;Shin, Min Kyoung;Park, Hong Tae;Seo, Hyo Sil;Kim, Jae Won;Yoo, Han Sang
    • Korean Journal of Veterinary Research
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    • v.53 no.2
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    • pp.83-88
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    • 2013
  • Field efficacy of enterotoxigenic Escherichia coli-specific phage (${\Phi}CJ19$) as a feed additive was evaluated in weaning piglets. Fifty-four piglets at 3-4 weeks old were allocated in three different groups and two of them were fed with bacteriophage at different concentrations ($10^6PFU/kg$ feed and $10^8PFU/kg$ feed, respectively) for 30 days. Body weight and feed intake were measured at 10 days interval and body condition and fecal score were inspected every day. Based on the measurement, feed conversion rate (FCR) and average daily gain (ADG) of each group during 30 days were analyzed. The analysis suggests that the bacteriophage may help the improvement of FCR and ADG at $10^8PFU/kg$ of bacteriophage feeding group in 30 days. A result from analysis of fecal score indicates that the bacteriophage also may help to relieve the intermittent diarrhea in post-weaning stage. Those results suggest that bacteriophage might help the growth of piglets in post-weaning stage.

Cloning, Expression, and Characterization of a New Phytase from the Phytopathogenic Bacterium Pectobacterium wasabiae DSMZ 18074

  • Shao, Na;Huang, Huoqing;Meng, Kun;Luo, Huiying;Wang, Yaru;Yang, Peilong;Yao, Bin
    • Journal of Microbiology and Biotechnology
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    • v.18 no.7
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    • pp.1221-1226
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    • 2008
  • The soft rot bacterium Pectobacterium wasabiae is an economically important pathogen of many crops. A new phytase gene, appA, was cloned from P. wasabiae by degenerate PCR and TAIL-PCR. The open reading frame of appA consisted of 1,302 bp encoding 433 amino acid residues, including 27 residues of a putative signal peptide. The mature protein had a molecular mass of 45 kDa and a theoretical pI of 5.5. The amino acid sequence contained the conserved active site residues RHGXRXP and HDTN of typical histidine acid phosphatases, and showed the highest identity of 48.5% to PhyM from Pseudomonas syringae. The gene fragment encoding the mature phytase was expressed in Escherichia coli BL21 (DE3), and the purified recombinant phytase had a specific activity of 1,072$\pm$47 U/mg for phytate substrate. The optimum pH and temperature for the purified phytase were pH 5.0 and 50$^{\circ}C$, respectively. The $K_m$ value was 0.17 mM, with a $V_{max}$ of 1,714 $\mu$mol/min/mg. This is the first report of the identification and isolation of phytase from Pectobacterium.

Mixed and separate gender feeding influenced the growth performance for two lines of Korean native chickens when compared to a white semi-broiler and a commercial broiler from day 1 to 35 post-hatch

  • Ogola, Oketch Elijah;Cho, Hyun Min;Hong, Jun Seon;Kim, Yu Bin;Nawarathne, Shan Randima;Yu, Myunghwan;Heo, Jung Min;Yi, Young-Joo
    • Korean Journal of Agricultural Science
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    • v.48 no.1
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    • pp.171-178
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    • 2021
  • A comparative study was conducted to examine the effects of mixed and separate gender feeding on growth performance of Korean native chickens (KNC) against a white semi-broiler (WSB) and a commercial broiler (CB) over five weeks. 576 chicks were used with eight birds per cage in a randomized complete block design with 18 replicates per breed. For the KNC lines, three groups of male (M), female (F) and mixed-gender (FM) were used. Fresh water and feed were supplied on an ad-libitum basis. Birds were fed a standard starter (d 1 - 22) and grower diet (d 23 - 35). Body weight (BW), feed intake, and shank length (SL) were measured weekly. From the BW and feed consumed data, the average daily feed intake (ADFI), average daily gain (ADG), and feed conversion ratio (FCR) were calculated. The commercial broiler showed higher performance (p < 0.05) for all the indices measured for the entire period. The CB group consumed more feed and were more feed-efficient thus grew faster. This group was followed by the white semi-broiler and the KNC, in order. An intra-breed comparison for KNCs revealed that the males showed better growth performance with longer SL (p < 0.05) compared to the female and mixed-gender groups. The results showed that other than the breed type, mixed and separate gender feeding impacted on the growth performance of the two lines of Korean native chickens. Males for both lines of KNC generally performed better for the parameters measured, as determined by a greater BW and reduced FCR.

Effects of Charcoal Application on Ammonia Emission and Nitrogen Use Efficiency of Pig Slurry in the Vegetative Growth of Maize (Zea Mays L.)

  • Lee, Seung Bin;Park, Sang Hyun;Kim, Tae Hwan
    • Journal of The Korean Society of Grassland and Forage Science
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    • v.41 no.4
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    • pp.280-286
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    • 2021
  • The objective of this study was to prove the effect of pig slurry application with charcoal on nitrogen use efficiency (NUE), feed value and ammonia (NH3) emission from maize forage. The four treatments were applied: 1) non-pig slurry (only water as a control), 2) only pig slurry application (PS), 3) pig slurry application with large particle charcoal (LC), 4) pig slurry application with small particle charcoal (SC). The pig slurry was applied at a rate of 150 kg N ha-1, and the charcoal was applied at a rate of 300 kg ha-1 regardless of the size. To determine the feed value of maize, crude protein, dry matter intake, digestible dry matter, total digestible nutrient, and relative feed value were investigated. All feed value was increased by charcoal treatment compared to water and PS treatment. Also, the NUE for plant N was significantly higher in charcoal treatments (LC and SC) compared to PS treatment. On the other hand, there is no significant difference for feed value and NUE between LC and SC. The NH3 emission was significantly reduced 15.2% and 27.9% by LC and SC, respectively, compared to PS. Especially, SC significantly decreased NH3 emission by 15% compared to LC. The present study clearly showed that charcoal application exhibited positive potential in nitrogen use efficiency, feed value and reducing N losses through NH3 emission.

Cloning, Expression, and Characterization of a New Xylanase from Alkalophilic Paenibacillus sp. 12-11

  • Zhao, Yanyu;Meng, Kun;Luo, Huiying;Yang, Peilong;Shi, Pengjun;Huang, Huoqing;Bai, Yingguo;Yao, Bin
    • Journal of Microbiology and Biotechnology
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    • v.21 no.8
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    • pp.861-868
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    • 2011
  • A xylanase gene, xyn7c, was cloned from Paenibacillus sp. 12-11, an alkalophilic strain isolated from the alkaline wastewater sludge of a paper mill, and expressed in Escherichia coli. The full-length gene consists of 1,296 bp and encodes a mature protein of 400 residues (excluding the putative signal peptide) that belongs to the glycoside hydrolase family 10. The optimal pH of the purified recombinant XYN7C was found to be 8.0, and the enzyme had good pH adaptability at 6.5-8.5 and stability over a broad pH range of 5.0-11.0. XYN7C exhibited maximum activity at $55^{\circ}C$ and was thermostable at $50^{\circ}C$ and below. Using wheat arabinoxylan as the substrate, XYN7C had a high specific activity of 1,886 U/mg, and the apparent $K_m$ and $V_{max}$ values were 1.18 mg/ml and 1,961 ${\mu}mol$/mg/min, respectively. XYN7C also had substrate specificity towards various xylans, and was highly resistant to neutral proteases. The main hydrolysis products of xylans were xylose and xylobiose. These properties make XYN7C a promising candidate to be used in biobleaching, baking, and cotton scouring processes.

Molecular Cloning and Expression of a Novel Protease-resistant GH-36 $\alpha$-Galactosidase from Rhizopus sp. F78 ACCC 30795

  • Yanan, Cao;Wang, Yaru;Luo, Huiying;Shi, Pengjun;Meng, Kun;Zhou, Zhigang;Zhang, Zhifang;Yao, Bin
    • Journal of Microbiology and Biotechnology
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    • v.19 no.11
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    • pp.1295-1300
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    • 2009
  • A 2,172-bp full-length gene (aga-F78), encoding a protease-resistant $\alpha$-galactosidase, was cloned from Rhizopus sp. F78 and expressed in Escherichia coli. The deduced amino acid sequence shared highest identity (45.0%) with an $\alpha$-galactosidase of glycoside hydrolase family 36 from Absidia corymbifera. After one-step purification with a Ni-NTA chelating column, the recombinant Aga-F78 migrated as a single band of ~82 and ~210 kDa on SDS-PAGE and nondenaturing gradient PAGE, respectively, indicating that the native structure of the recombinant Aga-F78 was a trimer. Exhibiting the similar properties as the authentic protein, purified recombinant Aga-F78 was optimally active at $50^{\circ}C$ and pH 4.8, highly pH stable over the pH range 5.0-10.0, more resistant to some cations and proteases, and had wide substrate specificity (pNPG, melidiose, raffinose, and stachyose). The recombinant enzyme also showed good hydrolytic ability to soybean meal, releasing galactose of $415.58\;{\mu}g/g$ soybean meal. When combined with trypsin, the enzyme retained over 90% degradability to soybean meal. These favorable properties make Aga-F78 a potential candidate for applications in the food and feed industries.

Cloning, Expression, and Characterization of Protease-resistant Xylanase from Streptomyces fradiae var. k11

  • Li, Ning;Yang, Peilong;Wang, Yaru;Luo, Huiying;Meng, Kun;Wu, Nigfeng;Fan, Yunliu;Yao, Bin
    • Journal of Microbiology and Biotechnology
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    • v.18 no.3
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    • pp.410-416
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    • 2008
  • The gene SfXyn10, which encodes a protease-resistant xylanase, was isolated using colony PCR screening from a genomic library of a feather-degrading bacterial strain Streptomyces fradiae var. k11. The full-length gene consists of 1,437bp and encodes 479 amino acids, which includes 41 residues of a putative signal peptide at its N terminus. The amino acid sequence shares the highest similarity (80%) to the endo-1,4-${\beta}$-xylanase from Streptomyces coelicolor A3, which belongs to the glycoside hydrolase family 10. The gene fragment encoding the mature xylanase was expressed in Escherichia coli BL21 (DE3). The recombinant protein was purified to homogeneity by acetone precipitation and anion-exchange chromatography, and subsequently characterized. The optimal pH and temperature for the purified recombinant enzyme were 7.8 and $60^{\circ}C$, respectively. The enzyme showed stability over a pH range of 4.0-10.0. The kinetic values on oat spelt xylan and birchwood xylan substrates were also determined. The enzyme activity was enhanced by $Fe^{2+}$ and strongly inhibited by $Hg^{2+}$ and SDS. The enzyme also showed resistance to neutral and alkaline proteases. Therefore, these characteristics suggest that SfXyn10 could be an important candidate for protease-resistant mechanistic research and has potential applications in the food industry, cotton scouring, and improving animal nutrition.

In vitro stability evaluation of coated lipase

  • Liu, Lu Jie;Zhu, Jia;Wang, Bin;Cheng, Chu;Du, Yong Jie;Wang, Min Qi
    • Asian-Australasian Journal of Animal Sciences
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    • v.30 no.2
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    • pp.192-197
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    • 2017
  • Objective: The study was conducted to evaluate the stability of commercial coated lipase (CT-LIP) in vitro. Methods: The capsules were tested under different conditions with a range of temperature, pH, dry heat treatment and steaming treatment, simulated gastric fluid (SGF) and simulated intestinal fluid (SIF) in this work, respectively. Free lipase (uncoated lipase, UC-LIP) was the control group. Lipase relative activities measured in various treatments were used as a reference frame to characterize the stability. Results: The lipase activities were decreased with increasing temperatures (p<0.05), and there was a markedly decline (p<0.01) in lipase comparative activities of UC-LIP at $80^{\circ}C$ compared with CT-LIP group. Higher relative activities of lipase were observed in CT-LIP group compared with the free one under acidic ambient (pH 3 to 7) and an alkaline medium (pH 8 to 12). Residual lipase activities of CT-LIP group were increased (p<0.05) by 5.67% and 35.60% in dry heat and hydrothermal treatments, respectively. The lipase relative activity profile of CT-LIP was raised at first and dropped subsequently (p<0.05) compared with constantly reduced tendency of UC-LIP exposed to both SGF and SIF. Conclusion: The results suggest that the CT-LIP possesses relatively higher stability in comparison with the UC-LIP in vitro. The CT-LIP could retain the potential property to provide sustained release of lipase and thus improved its bioavailability in the gastrointestinal tract.

A study on the Optimum Wheel Characteristics Using Grinding Machine (연삭 장비를 이용한 최적의 휠 특성분석)

  • Ko, Jun-Bin;Kim, Woo-Kang;Jeon, Tek-Jong
    • Journal of the Korean Society of Manufacturing Process Engineers
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    • v.7 no.4
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    • pp.142-148
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    • 2008
  • This study aims to find the optimal cutting conditions, which are obtained by grinding condition, and the grinding characteristics and condition of constant velocity joint were investigated with respect to wheel velocity, depth of cut, feed speed. Grinding machine has been widely used in manufacturing optical reflects of metal. Such as steel are easy to be machined because of their proper material. As a result I obtained the data of grinding conditions makes good surface roughness and the optimal condition of grinding and get the mesh condition. The purpose of this study is to find the optimum grinding wheel characteristics for cutting constant velocity joint.

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