• Journal of Microbiology and Biotechnology
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• v.14 no.6
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• pp.1295-1302
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• 2004

A gene encoding the mannanase of Bacillus subtilis WL-7, which had been isolated from Korean soybean paste, was cloned into Escherichia coli, and the gene product was purified from the culture filtrate of the recombinant E. coli. This mannanase gene, designated manA, consisted of 1,086 nucleotides, encoding a polypeptide of 362 amino acid residues. The deduced amino acid sequence was highly homologous to those of mannanases belonging to the glycosyl hydrolase family 26. The molecular mass of the purified mannanase was 38 kDa as estimated by SDS-PAGE. The enzyme had a pH optimum at 6.0 and a temperature optimum at $55^{\circ}C$. The enzyme was active on locust bean gum, konjak, guar gum, and lichenan, while it did not exhibit activity towards yeast mannan, laminarin, carboxymethylcellulose, $\beta$­glucan, xylan, and para-nitrophenyl-$\beta$-mannopyranoside.

• Korean Journal of Pharmacognosy
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• v.28 no.2
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• pp.65-71
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• 1997

This study was carried out to purify and to characterize various bioactive material acemannan from Aloe vera. Purified acemannan was mannose (67%) and acetyl group (23%), and the rest of glucose was galactose that consists of long chain polydispered beta-(1, 4) linked mannan polymers. The sugar and acetyl group in the molecule were linked by molar ratio of 3 : 1. This polysaccharide from Aloe vera may provide functional flood and potential drug source with antiviral and immunomodulating properties.

• Journal of Microbiology and Biotechnology
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• v.15 no.6
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• pp.1250-1257
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• 2005

Two groups of exopolysaccharides (designated as Fr-I EPS and Fr-II EPS) were isolated from the culture filtrate of new fungal strain Trichoderma erinaceum DG-312 by Sepharose CL-6B chromatography. The structures of the exopolysaccharides were investigated using gas chromatography (GC), Fourier transform-infrared (FT-IR) spectroscopy, GCMS analysis, and NMR. GC analysis indicated that Fr-I EPS was composed of mainly mannose ($78.9\%$) and galactose ($21.1\%$), whereas Fr-II EPS contained mannose ($68.4\%$), galactose ($26.2\%$), and glucose ($5.4\%$). In the anomeric region ($950-700cm_{-1}$) of the FT-IR spectrum, both EPSs exhibited obvious characteristic absorption of $810\;cm_{-1}$, indicating the existence of mannose. The spectra of $\alpha-and\;\beta$-configurations were assigned at 880 and $914\;cm_{-1}$, respectively. The results of GC-MS analyses confirmed that both EPSs were complex heteropolysaccharides with a ($1{\rightarrow}3$)-linked mannan backbone. The C-1 region that appeared in the $^{13}C-NMR$ spectra of these EPSs indicated a typical anomeric carbon signal. The Fr-I EPS showed two anomeric carbon signals at 102.6 and 99.6 ppm, whereas the Fr-II EPS displayed four anomeric carbon signals at 102.5, 99.6, 98.5, and 94.3 ppm. The molecular characteristics of the EPSs were further investigated using a size exclusion chromatography/multi-angle laser light scattering (SEC/MALLS) system. The SEC/MALLS system revealed that the average molar masses of the EPSs were $6.592{\times}10^{4}$ (Fr-I EPS) and $1.920{\times}10^{4}$ (Fr-II EPS) g/mol, and the molecular conformation of both EPSs in aqueous solution was random coils.

• Korean Journal of Food Science and Technology
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• v.29 no.6
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• pp.1269-1274
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• 1997

This study was researched to purify and characterize variety bioactive material acethylmannan from Aloe vera. Purified acethylmannan was mannose (67%), acetyl group (23%) and the rest glucose, galactose that consisting of long chain polydispered ${\beta}-1,4$ linked mannan polymers. The sugar and acetyl group in molecular were linked molar ration one third. $IC_{50}$ value (i.e that concentration which exhibits 50% more enzyme inhibition than control) on angiotensin converting enzyme were 0.58 mM. This compound were found to be a competitive inhibition of Angiotensin Converting Enzyme with apparent Ki values of 0.068 mM.

• Microbiology and Biotechnology Letters
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• v.45 no.2
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• pp.155-161
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• 2017

A gene coding for the xylanase predicted from the partial genomic sequence of Paenibacillus woosongensis was cloned by PCR amplification and sequenced completely. This xylanase gene, designated xyn11B, consisted of 1,071 nucleotides encoding a polypeptide of 356 amino acid residues. Based on the deduced amino acid sequence, Xyn11B was identified to be a modular enzyme, including a single carbohydrate-binding module besides the catalytic domain, and was highly homologous to xylanases belonging to glycosyl hydrolase family 11. The SignalP4.1 server predicted a stretch of 26 residues in the N-terminus to be the signal peptide. Using DEAE-Sepharose and Phenyl-Sepharose column chromatography, Xyn11B was partially purified from the cell-free extract of recombinant Escherichia coli carrying a copy of the P. woosongensis xyn11B gene. The partially purified Xyn11B protein showed maximal activity at $50^{\circ}C$ and pH 6.5. The enzyme was more active on arabinoxylan than on oat spelt xylan and birchwood xylan, whereas it did not exhibit activity towards carboxymethylcellulose, mannan, and para-nitrophenyl-${\beta}$-xylopyranoside. The activity of Xyn11B was slightly increased by $Ca^{2+}$ and $Mg^{2+}$, but was significantly inhibited by $Cu^{2+}$, $Ni^{2+}$, $Fe^{3+}$, and $Mn^{2+}$, and completely inhibited by SDS.

• Korean Journal of Poultry Science
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• v.33 no.2
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• pp.151-158
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• 2006

In order to study the effects of supplementary $Safmannan^(R)$(Beta-glucan & MOS complex) and $World-Labs^(R)$ (multiple probiotics) on the performance, nutrient availability, small intestinal microflora and immune response in broiler chicks, one thousand hatched broilers ($Ross^(R)$ were assigned to 4 treatments: control(basal diet), $BMD^(R),\;Safmannan^(R)\;and\;World-Labs^(R)$. There were no significant differences in the performance and in serum IgG, ND titre. However parameters of leukocytes and erythrocytes were significantly different among treatments (p<0.05). Leukocytes and RBC of $World-Labs^(R)\;and\;Safmannan^(R)$ were mostly lower than $BMD^(R)$ and control whereby MCH and MCHC of $World-Labs^(R)\;and\;Safmannan^(R)$ were higher than other treatments. The cfu of intestinal microflora had no significant differences among treatments. The $BMD^(R)$ treatment was higher than others in amino acid and crude fat availability and $World-Labs^(R)$ was higher than others in crude fiber availability. It was concluded that supplements used in the present experiment did not significantly affect the production parameters. However, significant impact on blood parameters, especially on leucocytes, may need further investigation.