A novel thermostable, acidophilic α-amylase from a new thermophilic "Bacillus sp Ferdowsicous" isolated from Ferdows hot mineral spring in Iran: Purification and biochemical characterization

This paper describes the purification and characterization of a novel acidophile alpha-amylase from newly Isolated Bacillus sp Ferdowsicous The enzyme displayed a molecular weight of 53 kDa and it was stable over a range of pH from 35 to 7 with an optimum around 45 The optimum temperature for activity was found to be around 70 degrees C and the enzyme remained active to more than 75% up to 75 degrees C for 45 min The enzyme activity was decreased by Zn2+ and EDTA but inhibited by Hg2+, whereas the activity was increased by approximately 15% by Ba2+ and Fe2+ Na+, Mg2+, Ca2+. PMSF, Triton X-100 and beta-mercaptoethanol had any considerable effect on its activity. The enzyme activity on the amylose as substrate was 1 98 times greater than amylopectin. Partial N-terminal sequencing demonstrated no significant similarity with other known alpha-amylases, indicating that the presented enzyme was new Considering its promising properties, this enzyme can find potential applications in the food industry as well as in laundry detergents (C) 2010 Elsevier B V All rights reserved