Enzyme and Microbial Technology, Vol.36, No.7, 855-861, 2005
Purification and characterization of thermo-labile alkaline phosphatase from an Antarctic psychrotolerant Bacillus sp P9
A psychrotolerant Bacillus sp. from Antarctica produced an alkaline phosphatase in the culture supernatant. The strain showed 98.4% 16s rDNA sequence identity with Bacillus sphaericus. The 76 kDa protein was purified 11.1-fold showing alkaline phosphomonoesterase activity. Enzyme was optimally produced at 25 degrees C and pH 7.0. This cold active alkaline phosphatase is heat labile and gets completely inactivated at 60 degrees C in 50 min and is active in broad pH range. (c) 2005 Elsevier Inc. All rights reserved.