Purification and Characterization of an $\alpha$ -L-Arabinofuranosidase from Bacillus sp. DSNC 101

Bacillus sp. DSNC 101이 생산하는 $\alpha$-L-Arabinofuranosidase의 정제 및 특성

  • Published : 2001.02.01

Abstract

${\alpha}$-L-Arabinofuranosidase was purified from the culture supernatant of Bacillus sp. DSNC 101. The enzyme had a molecular weight of 56 kDa. Optimum temperature and pH for ${\alpha}$-L-arabinofuranosidase activity were 55$^{\circ}C$ and 7.0 respectively. The Michaelis constant(Km) and maximal reaction velo-city(Vmax) for p-nitrophenyl-${\alpha}$-L-arabinofuranoside were 1.0 mM and 113.6 U/mg protein, respe-ctively. ${\alpha}$-L-Arabinofuranosidase was completely inhibited by HgCl$_2$ and CuSO$_4$. The enzyme was spe-cific for the ${\alpha}$-linked arabinoside in the furanoside configuration. The enzyme was produced during growth on agricultural residue such as rice straw, but not during growth on spelt xylan, glucose or cellobiose.

Bacillus sp. DSNC 101의 배양 상징액으로부터 $\alpha$-L-arabinofuranosidase를 정제하여 그 특성을 조사하였다. 정제된 효소의 분자량을 SDS-PAGE를 이용하여 측정한 결과 56kDa로 나타났으며 효소 활성도에 대한 최적 온도와 최적 pH는 각각 55$^{\circ}C$와 7.0이었다. p-nitrophenyl-alpha-L-arabinofuranoside에 대한 Km 값과 Vmax는 1.0mM과 113.6U/mg이었으며 Hg$^{2+}$과 Cu$^{2+}$의 첨가는 효소 반응을 완전히 저해하였다. Ba-cillus sp. DSNC 101은 탄소원으로 볏짚을 사용할 때 $\alpha$-L-arabinofuranosidase를 생산하였으나 xylan이나 glucose, cellulose를 탄소원으로 배양할 때는 생산되지 않았다.

Keywords