Partial purification of some properties of -Glucosidase from the gut of the giant African snail, Achatina achatina

Abstract

b-glucosidase was partially purified from animal source (Achatina achatina) by extraction with acetate buffer, separate fractional precipitation with ammonium sulphate and acetone followed by heat treatment.  The activity and specific activity of the crude enzyme were 1.6U/ml and 2.35U/mg protein.  The partially enzyme has activity of 4.70U/ml (for ammonium sulphate fraction) and 3.80U/ml (for acetone precipitate) with specific activity of 6.18U/mg protein and 6.03U/mg protein in the order above.  Mathematical treatment of the data from the degradation of linamarin by the partially purified enzyme generated HCN values that were used to construct Lineweaver-Burk plot which gave apparent Km and Vmax values of 0.34mM and 0.25mmol HCN/min/ml of enzyme or 8.46mg HCN/min/mg protein respectively.  The temperature and pH optima obtained for both the crude and partially purified enzyme were 55 – 60°C and 6.0 – 6.5.  Both the crude and partially purified enzyme showed high degree of hydrolysis towards standard linamarin, the cynogenic glycosides of cassava and lima beans but did not significantly hydrolyse the cyanogenic glycoside of sorghum species.