• Title/Summary/Keyword: Animal activity

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Molecular cloning, expression and characterization of a novel feruloyl esterase enzyme from the symbionts of termite (Coptotermes formosanus) gut

  • Chandrasekharaiah, Matam;Thulasi, Appoothy;Bagath, M.;Kumar, Duvvuri Prasanna;Santosh, Sunil Singh;Palanivel, Chenniappan;Jose, Vazhakkala Lyju;Sampath, K.T.
    • BMB Reports
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    • v.44 no.1
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    • pp.52-57
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    • 2011
  • Termites play an important role in the degradation of dead plant materials and have acquired endogenous and symbiotic cellulose digestion capabilities. The feruloyl esterase enzyme (FAE) gene amplified from the metagenomic DNA of Coptotermes formosanus gut was cloned in the TA cloning vector and subcloned into a pET32a expression vector. The Ft3-7 gene has 84% sequence identity with Clostridium saccharolyticum and shows amino acid sequence identity with predicted xylanase/chitin deacetylase and endo-1,4-beta-xylanase. The sequence analysis reveals that probably Ft3-7 could be a new gene and that its molecular mass was 18.5 kDa. The activity of the recombinant enzyme (Ft3-7) produced in Escherichia coli (E.coli) was 21.4 U with substrate ethyl ferulate and its specific activity was 24.6 U/mg protein. The optimum pH and temperature for enzyme activity were 7.0 and $37^{\circ}C$, respectively. The substrate utilization preferences and sequence similarity of the Ft3-7 place it in the type-D sub-class of FAE.

Effects of Chromium Yeast on Performance, Insulin Activity, and Lipid Metabolism in Lambs Fed Different Dietary Protein Levels

  • Yan, Xiaogang;Zhang, Wei;Cheng, Jianbo;Wang, Runlian;Kleemann, David O.;Zhu, Xiaoping;Jia, Zhihai
    • Asian-Australasian Journal of Animal Sciences
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    • v.21 no.6
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    • pp.853-860
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    • 2008
  • This experiment was conducted to study the effects of chromium (Cr), dietary crude protein (CP) level and potential interactions between these two factors on growth rate and carcass response, insulin activity and lipid metabolism in lambs. Forty-eight, 9-week-old weaned lambs (Dorper$\times$Small-tail Han sheep, mean initial body weight = $22.96kg{\pm}2.60kg$) were used in a $2{\times}3$ factorial arrangement of supplemental Cr (0 ppb, Cr0; 400 ppb, Cr1; or 800 ppb, Cr2 from chromium yeast) and CP levels (157 g/d to 171 g/d for each animal, LP; or 189 g/d to 209 g/d for each animal, HP). Growth data and blood samples were collected at the beginning and end of the feed trial, after which the lambs were killed. Both Cr additive groups and the HP group increased final weight and average daily gain, especially the Cr1 and HP group (p<0.01). HP increased pelvic fat weight (p<0.05), fat thickness of the 10th rib (p<0.05), longissimus muscle area (p<0.01) and rate of deposition of intramuscular fat (p<0.01). Supplemental Cr decreased the rate of deposition of intramuscular fat (p<0.05). Fasting insulin level and the ratio of insulin to glucose were lower with Cr1 than other groups, but with no significant difference. Glucose concentration was not affected by any treatment. Nonesterified fatty acids increased in the Cr1 (p<0.05) and HP (p<0.05) conditions and there was a significant $Cr{\times}CP$ interaction (p<0.05). Cr1 decreased triglycerides (p<0.05) and total cholesterol (p = 0.151) and HP increased high-density lipoprotein cholesterol (p<0.05). Cr1 decreased lipoprotein lipase activity in subcutaneous adipose tissue (aLPL, p<0.05) and the ratio of aLPL to lipoprotein lipase activity in skeletal muscle (mLPL, p = 0.079). mLPL and hepatic lipase (hHL) were not affected by any treatment. In the present study, Cr had limited effects on growth rate and carcass response, whereas Cr and CP had some notable effects on plasma metabolites and enzyme activities. Cr has a potential effect on energy modulation between lipid and muscle tissue. In addition, few $Cr{\times}CP$ interactions were observed.

Degradation of Phytate Pentamagnesium Salt by Bacillus sp. T4 Phytase as a Potential Eco-friendly Feed Additive

  • Park, In-Kyung;Lee, Jae-Koo;Cho, Jaie-Soon
    • Asian-Australasian Journal of Animal Sciences
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    • v.25 no.10
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    • pp.1466-1472
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    • 2012
  • A bacterial isolate derived from soil samples near a cattle farm was found to display extracellular phytase activity. Based on 16S rRNA sequence analysis, the strain was named Bacillus sp. T4. The optimum temperature for the phytase activity toward magnesium phytate (Mg-$InsP_6$) was $40^{\circ}C$ without 5 mM $Ca^{2+}$ and $50^{\circ}C$ with 5 mM $Ca^{2+}$. T4 phytase had a characteristic bi-hump two pH optima of 6.0 to 6.5 and 7.4 for Mg-$InsP_6$. The enzyme showed higher specificity for Mg-$InsP_6$ than sodium phytate (Na-$InsP_6$). Its activity was fairly inhibited by EDTA, $Cu^{2+}$, $Mn^{2+}$, $Co^{2+}$, $Ba^{2+}$ and $Zn^{2+}$. T4 phytase may have great potential for use as an eco-friendly feed additive to enhance the nutritive quality of phytate and reduce phosphorus pollution.

Characterization of Novel Amylase-Sensitive, Anti-Listerial Class IId Bacteriocin, Agilicin C7 Produced by Ligilactobacillus agilis C7

  • Jeong Min Yoo;Ji Hoon Song;Robie Vasquez;In-Chan Hwang;Jae Seung Lee;Dae-Kyung Kang
    • Food Science of Animal Resources
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    • v.43 no.4
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    • pp.625-638
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    • 2023
  • Among various biological agents, bacteriocins are important candidates to control Listeria monocytogenes which is a foodborne pathogen. In this study, a novel bacteriocin, named agilicin C7, was isolated from Ligilactobacillus agilis C7 showing inhibitory activity against L. monocytogenes. Agilicin C7 biosynthesis gene was characterized by bioinformatics analyses and heterologously expressed in Escherichia coli for further study. The anti-listeria activity of recombinant agilicin C7 (r-agilicin C7) was lost by proteases and α-amylase, suggesting that agilicin C7 is a glycoprotein. r-Agilicin C7 has wide pH and thermal stability and is also stable in various organic solvents. It destroyed L. monocytogenes by damaging the integrity of the cell envelope. These properties of r-agilicin C7 indicate that agilicin C7 is a novel amylase-sensitive anti-listerial Class IId bacteriocin. Physicochemical stability and inhibitory activity against L. monocytogenes of r-agilicin C7 suggest that it can be applied to control L. monocytogenes in the food industry, including dairy and meat products.

Peroxide Status in Tissues of Heat-Stressed Broilers

  • Lin, H.;Du, R.;Zhang, Z.Y.
    • Asian-Australasian Journal of Animal Sciences
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    • v.13 no.10
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    • pp.1373-1376
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    • 2000
  • The peroxidation status of tissues was estimated in broilers under acute or chronic heat stress ($32^{\circ}C$, 24 h, $5{\times}24h$) in the present study. The results showed that the lipid peroxide (LPO) concentrations in plasma and liver were elevated (p<0.05) by acute heat stress, and were not influenced in kidney (p>0.05). At the same time, no significant change of superoxide dismutase (SOD) activity in the liver, kidney or plasma was observed. Under chronic heat exposure, the SOD activity in liver was increased (p<0.05) and the LPO concentrations in the liver and plasma were restored to the normal levels. The LPO level in kidney was not affected by chronic heat stress (p>0.05), but SOD activity was significantly decreased (p<0.01). The results suggested that the peroxidation was induced by acute heat stress and disappeared along with the time of heat exposure, and the peroxidation reactions were different among tissues.

Comparative Activity of Medicinal Herbs Between Hollow Fiber Assay and Xenographic Animal Assay (Hollow Fiber 검색법과 Xenographic Animal Assay를 이용한 생약재의 암세포 저해활성 비교)

  • Cho, Choa-Hyung;Yoon, Won-Ho;Lee, Keyong-Ho
    • Korean Journal of Pharmacognosy
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    • v.34 no.4 s.135
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    • pp.288-292
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    • 2003
  • We compared the antitumor activity between hollow fiber assay and xenographic animal assay on thirty herbal plants. It is evaluated that the antitumor activity of above 30% is regarded as 'positive response', and its of below 30% is regarded as 'negative response'. The two herbal plants extracts (Ulmus davidiana Hedyotis diffusa) among thirty herbal plants show to be positive in xenographic animal assay and they were also correctly identified as positive by the hollow fiber assay. The correlation of the hollow fiber assay data with xenographic animal assay would suggest that hollow fiber assay presents a potentially unique tool to develop the herbal medicine for cancer.

PURIFICATION AND PROPERTIES OF EXTRACELLULAR NUCLEASE(S) FROM RUMEN CONTENTS OF BUBALUS BUBALIS

  • Sinha, P.R.;Dutta, S.M.
    • Asian-Australasian Journal of Animal Sciences
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    • v.3 no.2
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    • pp.115-120
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    • 1990
  • Extracellular nuclease(s) in buffalo rumen fluid were purified from strained rumen fluid by a procedure involving Seitz filtration, acetone fractionation and gel filtration on Sephadex G-100. The enzyme resolved into two peaks exhibiting both DNase and RNase activities. The molecular weight of enzyme corresponding to peaks I and II were approximately 30,000 and 12,000 respectively. The properties of enzymes from the two peaks, however, were same. Optimum temperature for both DNase and RNase activities was at $50^{\circ}C$. Whereas DNase activity was stable upto $60^{\circ}C$, RNase activity was stable only up to $50^{\circ}C$. DNase activity recorded two pH optima, one at pH 5.5 and the other at pH 7.0. RNase activity recorded a broad pH optimum between pH 6.0-8.0. pH stability of the enzyme coincided with pH optima for both the activities. DNase activity was stimulated by $Mg^{2+}$ and $Mn^{2+}$ and inhibited by $Fe^{2+}$, $Zn^{2+}$, $Hg^{2+}$ and $Ag^+$. RNase activity was also stimulated by $Mg^{2+}$ and $Mn^{2+}$ and inhibited by $Cu^{2+}$, $Fe^{2+}$, $Zn^{2+}$, $Hg^{2+}$ and $Ag^+$. Reducing agents stimulated both the activities.

Purification and Characterization of α-Galactosidase from Lactobacillus salivarius subsp. salivarius Nam27

  • Bae, Hyoung-Cchurl;Choi, Jong-Woo;Nam, Myoung-Soo
    • Food Science of Animal Resources
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    • v.27 no.1
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    • pp.102-109
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    • 2007
  • Lactobacillus salivarius subsp. salivarius CNU27 possessed a high level of ${\alpha}$-galactosidase activity. Purified ${\alpha}$-galactosidase was obtained after sonication of harvested cell pellet followed by DEAE-Sephadex A-50 and Mono Q anion exchange chromatography. The specific activity of the purified enzyme was 8,994 units/mg protein which is 17.09 times higher than that in crude extract. The native enzyme was a monomer with a molecular mass of 56,397.1 dalton. The optimum temperature and pH for the enzyme were $40^{\circ}C$ and 6.0, respectively. The enzyme was stable between 25 and $50^{\circ}C$. However, ${\alpha}$-galactosidase activity was lost rapidly below pH 4.5 and above pH 8.5. The enzyme activity decreased to 6.73% and 4.30% of the original activity by addition of $Cu^{2+}$ and $Hg^{2+}$, respectively. Other metal compounds did not affect the enzyme activity significantly. The enzyme liberated galactose from melibiose, raffinose, and stachyose. The rate of substrates hydrolysis was measured by HPLC. Raffinose, stachyose and melibiose were completely decomposed after 24 hr at $40^{\circ}C$.

Optimal Condition and Interspecific Cross-Reaction of H-Y Antibody Activity (H-Y항체활성의 최적조건과 종간교차반응)

  • ;H.S.Shim;J.B.Kim;H.Y.Park;K.S.Chung
    • Korean Journal of Animal Reproduction
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    • v.10 no.2
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    • pp.168-174
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    • 1986
  • These experiments were carried out to clarify the optimalconditions and interspecific cross reaction of H-Y antibody activity. H-Y antiserum was prepared in inbred SD female rats and Balb/c female mice by repeated immunization of rat newborn testis homogemate, rat and mouse spleen cells obtained from males of same strain. The activity of H-Y antibody in antiserum was tested by ELISA and biological tests. The cross reactivity of H-Y antibody was confirmed by culturing mouse and rabbit embryos in medium containing H-Y antibody and complement obtained from rat and guinea pig, respectively. The optimal condition for the activity of H-Y antibody was also investigated by culturing embryos in medium with different pH and complement concentration. The results obtained in these experiments were summarized as follows: 1. The formation rates of H-Y antibody in rats immunized with newborn testis and spleen cell were 40.0 and 50.0% respectively, and that in mouse immunized with spleen cell was 48.4%. 2. The activity of H-Y antibody was not affected by pH in range of 6.5 to 8.0, and the same was true for the relative concentration of complement to the H-Y antibody. 3. Minimum time needed for the activity of H-Y antibody was confirmed to be 0.5 to 1 hour and 24 to 48 hours respectively for the zona free embryos and intact embryos. 4. When mouse and rabbit embryos were treated with H-Y antibody obtained from rat, 46.4 and 54.8% of embryos were retarded or destroyed. From these results it could be said that H-Y antibody had strong interspecific cross reactivity.

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