• Title, Summary, Keyword: mannan peptide

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Clinical Study on Mannan Peptide Combined with TP Regimen in Treating Patients with Non-small Cell Lung Cancer

  • Yan, Huai-An;Shen, Kang;Huang, Xin-En
    • Asian Pacific Journal of Cancer Prevention
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    • v.14 no.8
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    • pp.4801-4804
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    • 2013
  • Purpose: To investigate short-term response rate, quality of life and toxicities of mannan peptide combined with TP regimen in treating patients with non-small cell lung cancer (NSCLC). Patients and Methods: Forty one patients with NSCLC were divided into an experimental group treated with TP regimen combined with mannan peptide (21 patients) and a control group treated with TP alone (20 patients). Results: Response rates were 61.9% (13/21) for the experimental and 60% (12/20) for the control group (p>0.05). Regarding toxicity, white blood cell decreased more frequently in the control group (65%, 13/20) than in the experimental group (33.3%, 7/21) (p<0.05); nausea and vomiting also occurred more frequently in the control group (55%, 11/20 vs 23.8%, 5/21) (p<0.05). In terms of quality of life, this index was improved by 57.1% (12/21) and 25% (5/20) in experimental and control groups, respectively (p<0.05). Conclusions: Response rate of TP after combined with mannan peptide is mildly increased, while this combination alleviates bone marrow suppression as well as nausea and vomiting of TP, and improves quality of life when treating patients with NSCLC. However, this conclusion should be confirmed by randomized clinical trails.

Gene cloning of β-mannanase C from Cellulosimicrobium sp. YB-43 and characterization of the enzyme (Cellulosimicrobium sp. YB-43으로부터 mannanase C 유전자의 클로닝과 효소 특성)

  • Yoon, Ki-Hong
    • Korean Journal of Microbiology
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    • v.54 no.2
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    • pp.126-135
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    • 2018
  • The characteristics of enzyme and gene for mannanase B had been reported from Cellulosimicrobium sp. YB-43 producing some kind of mannanase. A gene coding for the enzyme, named mannanase C (ManC), was expected to be located downstream of the manB gene. The manC gene was cloned by polymerase chain reaction and sequenced completely. From this nucleotide sequence, ManC was identified to consist of 448 amino residues and contain a carbohydrate binding domain CBM2 besides a catalytic domain, which was homologous to mannanase belonging to the glycosyl hydrolase family 5. The catalytic domain of ManC showed the highest amino acid sequence similarity of 55% with the mannanases from Streptomyces sp. SirexAA-E (55.8%; 4FK9_A) and S. thermoluteus (57.6%; BAM62868). The His-tagged ManC (HtManC) lacking N-terminal signal peptide with hexahistidine at C-terminus was produced and purified from cell extract of recombinant Escherichia coli. The purified HtManC showed maximal activity at $65^{\circ}C$ and pH 7.5, with no significant change in its activity at pH range from 7.5 to 10. HtManC showed more active on konjac and locust bean gum (LBG) than guar gum and ivory nut mannan (ivory nut). Vmax and Km values of the HtManC for LBG were 68 U/mg and 0.45 mg/ml on the optimal condition, respectively. Mannobiose and mannotriose were observed on TLC as major products resulting from the HtManC hydrolysis of mannooligosacharides. In addition, mannobiose and mannose were commonly detected as the hydrolyzed products of LBG, konjac and ivory nut.

The Synergistic Action of the AL-Protease from Arthrobacter luteus on the Lysis of Yeast Cell Walls (Arthrobacter luteus가 생산하는 AL-Protease의 효모세포벽 용해 촉진작용)

  • Oh, Hong-Rock;Funatsu, Masaru
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.14 no.4
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    • pp.401-408
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    • 1985
  • The yeast cell wall lytic action of the alkaline AL-protease, which was found out of the crude Zymolyase that a kind of yeast cell wall lytic $endo-{\beta}-1$, 3-glucanase produced from Arthrobacter luteus, was investigated with the viable cells of S. sake and it's cell wall preparation. AL-protease on the lysis of the viable yeast cells showed very low activities with the alone, but the lytic activities were highly increased with the combination of AL-protease and Zymolyase. On the stepwise treatment of the viable yeast cells with AL-protease and Zymolyase, the cells were lysed highly only by the course having a treatment with Zymolyase after pretreatment with AL-protease. Thus synergistic action of AL-protease was not observed with any some commercial enzymes, known as a type of alkaline and serine protease such as AL-protease, and was also found to be affected greatly by the culture conditions and species of the yeast tested. AL-protease caused the release of some peptide and a lot of sugar from the cell wall preparation, but could not lysed the cell wall more than 66%. Whereas Zymolyase could lysed the cell walls almost completely with alone. On the basis of these results, the synergistic action of AL-protease on the lysis of S. sake cells is hypothesized that at first AL-protease bind to the yeast cell surface layer consisting of mannan and protein, and then changes their conformation to facilitate the penetration of Zymolyase from the outside to the inside framework layer constituted of alkali insoluble ${\beta}-1,\;3-glucan$.

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Cloning and Characterization of Xylanase 11B Gene from Paenibacillus woosongensis (Paenibacillus woosongensis의 Xylanase 11B 유전자 클로닝과 특성분석)

  • Yoon, Ki-Hong
    • 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.