Abstract
Bovine serum albumin (BSA) as a modifier was used with glutaraldehyde as a binder to study the activity and thermal stability of α-amylase. The optimum temperature of the enzyme was found to be 50C ± 2C. Further increase in temperature resulted in irreversible thermal inactivation of the enzyme. On modification of the enzyme with BSA, the rate of thermal inactivation was found to be significantly reduced. BSA modified α-amylase was found to retain its activity at 80C even after 3 h of incubation. The apparent thermal inactivation energy (Ed) of α-amylase was found to be significantly increased on modification with BSA. The half-life of BSA modified α-amylase at both 70C and 80C was found to be 2.5 times higher than the native α-amylase. Thermodynamic parameters, ΔH, ΔS and ΔG, were determined as a function of temperature. The kinetic constants Km and Vmax, using starch as substrate, were determined to study the effect of BSA conjugation on α-amylase.
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