Abstrait

Viscometric Studies on the Interaction of Anionic Surfactant with alpha Amylase

P. Arora and R. P. Singh

The viscometric studies on α–amylase-TEALS (triethanolamine lauryl sulphate) system were made and the effect of pH and temperature on viscosity behavior was investigated. The variation of viscosity with pH has been interpreted in terms of charged groups on the α–amylase surface. The intrinsic viscosity [η] of α-amylase in absence and presence of varying amounts of TEALS at different pH values was determined by plotting viscosity number vs. protein concentration in g/mL and then extrapolating to zero concentration of the α-amylase. With the help of intrinsic viscosity, molecular weight, hydrodynamic radius [Re], end to end root mean distance (r) and average molecular weight (M) of enzyme-surfactant system were also calculated at different temperatures and pH values.