Bacillus sp. DSNC 101의 배양 상징액으로부터 α-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℃와 7.0이었다. p-nitrophenyl-alpha-L-arabinofuranoside에 대한 Km 값과 Vmax는 1.0mM과 113.6U/㎎이었으며 Hg^2+과 Cu^2+의 첨가는 효소 반응을 완전히 저해하였다. Ba-cillus sp. DSNC 101은 탄소원으로 볏짚을 사용할 때 α-L-arabinofuranosidase를 생산하였으나 xylan이나 glucose, Cellulose를 탄소원으로 배양할 때는 생산되지 않았다.

α-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 α-L-arabinofuranosidase activity were 55℃ and 7.0 respectively. The Michaelis constant(Km) and maximal reaction velocity(Vmax) for p-nitrophenyl-α-L-arabinofuranoside were 1.0 mM and 113.6 U/㎎ protein, respectively. α-L-Arabinofuranosidase was completely inhibited by HgCl_2 and CuSO_4. The enzyme was specific for the α-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.

• 김소자 | So Ja Kim
• 김욱한 | Uk Han Kim