REVERSE MICELLES AS A VERSATILE MEDIUM FOR THE STUDY OF PORCINE PANCREATIC ALPHA-AMYLASE INVITRO

Abstract

Porcine pancreatic alpha amylase has been solubilized in cationic reverse micelles formed by cetyltrimethylammonium bromide (CTAB) and n-butanol. CTAB and n-butanol alone have been found to inhibit the alpha-amylase activity, whereas the enzyme activity is notably increased in reverse micelles formed by them. The activity is affected by change in water pool (Wo), pH, concentration of surfactant and temperature. There is 27% increase in control activity of alpha-amylase at Wo value of 24.7 at pH 7 in 66.66% n-butanol/0.75 mM CTAB and only 7% increase in enzyme activity is observed in 50% n-butanol/0.5 mM CTAB in comparison to the activity measured in aq. buffer system under optimal condition.