Denaturation of Bacillus amyloliquefaciens alpha-amylase with urea.
The urea induced denaturation of the Bacillus amyoliqefaciens alpha-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 degrees 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). alpha-amylase lost 80% of its activity in the concentrated solution of urea. alpha-amylase was more thermostable than other mesophilic enzymes.
Shareghi
B
B
Department of Biology, Faculty of Basic Sciences, Shahrekord University, Iran
Arabi
M
M
Zargham
M
M
D001407:Bacillus / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D008320:Maltose / Q000737:chemistry; D008956:Models, Chemical; D011489:Protein Denaturation; D013053:Spectrophotometry / Q000379:methods; D013056:Spectrophotometry, Ultraviolet / Q000379:methods; D013696:Temperature; D013816:Thermodynamics; D014508:Urea / Q000737:chemistry*; D000516:alpha-Amylases / Q000737:chemistry*
D008320:Maltose; D014508:Urea; D000516:alpha-Amylases