Springer Iranian Journal of Science and Technology (Sciences) 1028-6276 32 2 2008 06 01 THERMAL DENATURATION OF α-AMYLASE FROM BACILLUS AMYLOLIQUEFACIENS IN THE PRESENCE OF SODIUM DODECYL SULPHATE* 135 140 2251 10.22099/ijsts.2008.2251 EN B. SHAREGHI Department of Biology, University of Shahrekord, P.O. Box: 115, Shahrekord, I. R. of Iran M. ARABI Department of Biology, University of Shahrekord, P.O. Box: 115, Shahrekord, I. R. of Iran Journal Article 2006 11 25 The thermal denaturation of α-Amylase from Bacillus amyloliquefaciens has been investigated in the presence and absence of sodium dodecyl sulphate (SDS) over the temperature range (293-373) K in 20 mM sodium phosphate buffer, pH 6.9, using temperature scanning spectroscopy. The presence of SDS caused the destabilization of α-Amylase resulting in a decrease in the temperature of unfolding with an increase in SDS concentration. The thermodynamic parameters for unfolding of α-Amylase were determined in terms of the two-state model, using the temperature dependence of the spectroscopic behaviour of the enzyme at 280 nm. The result from specific activity measurements in the presence of SDS is in conformity with the results from thermal studies. https://ijsts.shirazu.ac.ir/article_2251_e17cf601786b621fea6bd684e14f86bb.pdf