Study on the thermal stability of alpha-amylase modified by maleic anhydride copolymer.

Brissová M, Augustín J, Simonetti M
Int J Biol Macromol. 1994 16 (3): 131-5

PMID: 7981159 · DOI:10.1016/0141-8130(94)90039-6

The thermal inactivation of mesophilic Bacillus subtilis alpha-amylase modified by maleic anhydride/vinyl acetate copolymer has been studied at different polymer/enzyme ratios in the pH range of relevance to enzymatic catalysis. Enzymatic activity measurements combined with circular dichroism measurements were used to determine the enzyme thermostability. The apparent first-order rate constants and activation energies of thermo-inactivation affected by addition of Ca2+ ions as well as by modification have been calculated. The modified alpha-amylase exhibited sufficiently high catalytic activity with enhanced resistance to the thermal unfolding process.

MeSH Terms (10)

alpha-Amylases Bacillus subtilis Bacterial Proteins Circular Dichroism Hot Temperature Kinetics Maleates Maleic Anhydrides Polyvinyls Protein Denaturation

Connections (1)

This publication is referenced by other Labnodes entities: