Arthrobacter globiformis S14-3 produced a novel type of inulin decomposing enzyme in the culture broth. The enzyme converted inulin into di-D-fructofuranose-l, 2';2, 1'-dianhydride (DFA I) and a small amount of oligosaccharides. The enzyme was purified 63-fold by DEAE-Toyopearl chromatographies. The optimal pH for the enzyme reaction was 6.0, and the optimal temperature was 40°C. The enzyme was stable up to 70°C in 8 HIM phosphate buffer, pH 6.0. Hg²⁺ and Fe³⁺ (1 MM) strongly inhibited the enzyme activity. By SDS-PAGE, the molecular weight of the enzyme was estimated to be 39, 000.
The NH₂-terminal amino acid sequence of the enzyme was determined to be
H₂N-Ala¹-Asn²Thr³-Val⁴-Tyr⁵-Asp⁶-Val⁷-Thr⁸-Thr⁹-Trp¹⁰-Ser¹¹-Gly¹²-Ala¹³-Thr¹⁴-Ile¹⁵-Ser¹⁶-Pro¹⁷-Tyr¹⁸-Val¹⁹-Asp²⁰.

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