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Denaturation of Bacillus Amyloliquefaciens Α-Amylase With Urea Publisher Pubmed



Shareghi B1, 3 ; Arabi M1 ; Zargham M2
Authors
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Authors Affiliations
  1. 1. Department of Biology, Faculty of Basic Sciences, Shahrekord University, Iran
  2. 2. Isfahan University of Medical Sciences, Iran
  3. 3. Department of Biology, Faculty of Basic Sciences, Shahrekord University, Shahrekord-88186, P.O. Box 115, Iran

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.