• Title/Summary/Keyword: 알파바이오

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업계소식

  • Korea Far Infrared Association
    • Journal of Korea Far Infrared Association
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    • s.20
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    • pp.20-29
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    • 2004
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업계소식

  • Korea Far Infrared Association
    • Journal of Korea Far Infrared Association
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    • s.19
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    • pp.22-31
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    • 2003
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협회소식

  • Korea Far Infrared Association
    • Journal of Korea Far Infrared Association
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    • s.19
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    • pp.7-20
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    • 2003
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업계소식

  • Korea Far Infrared Association
    • Journal of Korea Far Infrared Association
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    • s.15
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    • pp.16-25
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    • 2002
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업계소식

  • Korea Far Infrared Association
    • Journal of Korea Far Infrared Association
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    • s.18
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    • pp.18-27
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    • 2003
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업계소식

  • Korea Far Infrared Association
    • Journal of Korea Far Infrared Association
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    • s.16
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    • pp.21-30
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    • 2003
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업계소식

  • Korea Far Infrared Association
    • Journal of Korea Far Infrared Association
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    • s.17
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    • pp.17-24
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    • 2003
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Experimental Evaluation of Far Infrared Characteristic for Bio Liquid Ceramics used in Bulding finishing Materials (액상세라믹의 원적외선 특성의 실험적평가)

  • 지철근;최태섭;장성일
    • Journal of the Korean Institute of Illuminating and Electrical Installation Engineers
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    • v.16 no.6
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    • pp.7-12
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    • 2002
  • This paper presents the Experimental Evaluation for the physical, chemical property and Far Infrared Characteristic, the effects to the living body of liquid ceramics which was made by the a Bio ceramic(co).

Characterization of α-D-manosidase activity from Bacillus safensis MA-01 (Bacillus safensis MA-01 유래 알파-만노사이데이즈의 효소학적 특성)

  • Lee, Bo Mi;Kim, Joo Won;Park, Jae Kweon
    • Journal of Marine Bioscience and Biotechnology
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    • v.7 no.1
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    • pp.11-18
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    • 2015
  • An extracellular alkaline ${\alpha}$-D-mannosidase produced by a strain named as MA-01 was produced and its preliminary enzyme activity was characterized. Upon determining the 16S rDNA sequence and its homology search, the strain was identified to be one of species of the Bacillus safensis. Localization of enzyme was elucidated that ${\alpha}$-D-mannosidase can be found in culture medium as an extracellular enzyme. In addition, partial enzyme activity of 63% compared with the extracellular enzyme activity was observed in membrane protein. The optimal pH and temperature of the ${\alpha}$-D-mannosidase were pH 7.5 and $37^{\circ}C$, respectively. The $K_m$ and $V_{max}$ values of the ${\alpha}$-D-mannosidase in crude enzyme toward p-nitrophenyl-${\alpha}$-D-mannopyranoside were determined to be $455.6{\mu}M$ and $10.8{\mu}mole/min/mg$ of protein, respectively. To the best of our knowledge, this is the first report described the alkaline ${\alpha}$-D-mannosidase from the family of B. safensis.