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Global Journal of Pure and Applied Sciences

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Amylolytic studies of pleurotus tuber-regium

C.C. Monago, J. E. Okonkwo

Abstract


The alpha amylase of the sclerotium of Pleurotus tuber-regium was studied. The enzyme was purified from the fresh sclerotium through dialysis, ammonium sulphate fractionation and column chromatography of CM sephadex. The enzyme showed 70% of it's optimal activity between p.H 4.0 to 8.0. Acid and thermal stability was found at p.H 2.0 and temperature of 600c respectively. Michealis Menton constant (km) and maximum velocity (Vmax) of the enzyme with starch as substrate was 1.25mg/ml and 5.0ug/ml/min, respectively. The paper chromatography of the hydrolytic products in starch showed hydrolytic products like glucose, maltose and dextrin, suggesting an alpha-amylase type of activity. Maltose is not hydrolysed by this enzyme.

Keywords: Pleurotus tuber-regium, Amylase, Sclerotium, fungus.


(Global Journal of Pure and Applied Sciences: 2002 9(1): 53-58)



http://dx.doi.org/10.4314/gjpas.v9i1.15979
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