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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
이보미;김주원;박제권

  • Received : 2015.06.15
  • Accepted : 2015.06.30
  • Published : 2015.06.30

Abstract

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.

Keywords

Bacillus safensis;${\alpha}$--D-Mannosidase;16S rDNA sequence;Membrane protein;p-nitrophenyl-${\alpha}$-D-mannopyranoside

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Acknowledgement

Supported by : 해양수산부