Purification and Properties of Aspergillus 3cuum exoinulinase

Aspergillus ficuum 조효소액으로부터 Exoinulinase의 정제 및 특성

- An exoinulinase (EC 3.2.1.80) was purified from a commercial inulinase preparation from Aspergillus ficuum using ion exchange chromatography on CM-Sephadex C-50 and DEAESepharose 6B and HPLC gel filtration on a Protein Pak 125 column. Native exoinulinase had a molecular weight of 83, 000$\pm$ 1, 000 and was glycoprotein. Optimal pHs of the enzyme were ranged from 4.4 to 4.7. About ninety five percent of the whole activity was maintained even after incubation of 8 hours at $55^{\circ}C$.The enzyme was a typical non-specific P-fructofuranosidase, of which I/S ratio appears to be 0.35.

Aspergillus ficuum이 생산하는 exoniulinase가 CM-Sephadex, DEAE-Sepharose 6B, 및 HPLC gel filtration을 통해 단백질 mg당 약 2,800U의 specific activity로 정제되었다. 이 효소는 native 상태에서 약 83,000+1,000의 분자량을 나타냈으며 당을 함유하고 있었다. 이 효소는 최적 pH가 4.4-4.7이었고, 55'C에서 8시간 노출 후에도 그 활성을 95 유지하였다. 이 효소의 I/S ratio는 약 0.35이고 전형적인 non-speific Beta-fructofuranosidase의 특성을 나타내었으며 raffinose와 stachyose를 분해할 수 있었다.