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Purification and Properties of -Galactosidase From A Thermophilic Fungus Rhizmmucor Pusillus IB8. | ||
| Iraqi Journal of Science | ||
| Article 1, Volume 54, Issue 2, 2013, Pages 307-315 | ||
| Authors | ||
| Mohammed Omer; Ghazi M Aziz; Khalid Jaber Alzwany | ||
| Abstract | ||
| An extracellular -galactosidase from the thermophilic fungus Rhizomucor Pusillus IB8 has been purified via several steps included precipitation by ammonium sulphate at 80 % saturation, DEAE- Cellulose Ion exchange chromatography and gel filteration on sepharose CL-6B column. The Final purification folds and the yield of the enzyme were 42.5 and 24.8 % respectively. The purified -galactosidase has an optimum pH for its activity between 4.5 to 5, while the optimum pH for enzyme stability was between 5 to 5.5. Futhermore, it was found that the optimum temperature for its activity was 60 C°. The purified enzyme retained approximatly 98% of its original activity when incubated at 60 C° for 60 min. However, 25 % of its activity was lost when incubated for 120 min at the same tmperaure. Activation energy for conversion of the substrate ONPG to products was 6.15 Kcal / mol, whereas, for enzyme denaturation it was 99.3 Kcal / mol. The molecular weight of the purified enzyme was 232000 dalton as determined by gel filtration on sepharose CL-6B. Kinetic studies showed that the Michaelis constant (Km) and maximum velocity (Vmax) values for the purified enzyme using ONPG as a substrate were 0.46 mM and 223 μM /min respectively. | ||
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