Denaturation of Bacillus Amyloliquefaciens Α-Amylase With Urea Publisher Pubmed



Shareghi B^{1, 3} ; Arabi M¹ ; Zargham M²
Source: Pakistan Journal of Biological Sciences Published:2007

Abstract

The urea induced denaturation of the Bacillus amyoliqefaciens α-amylase (E.C. 3.2.1.1) was studied by absorption measurements in the near ultra-violet region and specific activity measurements. Spectral measurements were made at pH 6.9 and over the temperature range 20-80°C. It has been observed that urea induced a cooperative transition. In the absence of denaturant, the Gibs energy changes were in the range of 8-15 kcal mol -1, α-amylase lost 80% of its activity in the concentrated solution of urea, α-amylase was more thermostable than other mesophilic enzymes. © 2007 Asian Network for Scientific Information.