تنقية و توصيف أنزيم الأنيولينيز من الفطر Aspergillus niger المعزول محليا

Abstract EN

Inulinase from a.

niger local isolate was purified.

the purification steps included precipitation with ethanol 70% ,Ion exchange chromatography with DEAE-cellulose and finaly ,gel filteration (two steps) using sephadex G-150.

two forms of inulinase (W and A) were obtained from the purification procedure used.

inulinase forms were purified with (6.8 and 9.4) fold and (9 and 13.5) % yield , respectively.

electrophoresis results confirmed the complete purity to the two enzyme forms since they gave a single band in polyacrylamide gel electrophoresis.

enzyme characterization revealed that the molecular weight of the W and A forms were 72.4 and 69.18 ,respectively.

the optimum pH activity was 4.5 for both enzyme forms .

the W form was stable within the range (3.5-7.0) while the A form was stable within the pH (4.5- 9.0).

the w form was stable with in temperature range (20-45) Cᵒ while the A form was stable within the range (20-50) Cᵒ.

Km value were (1.052 and 0.909) mM and V max values were (2.86 and 5) μM / ml / min for both enzyme forms W and A , respectively.