@article {10.3844/ojbsci.2009.67.74,
article_type = {journal},
title = {Characteristics of a Novel Highly Thermostable and Extremely Thermophilic Alkalitolerant Amylase from Hyperthermophilic Bacillus Strain HUTBS71},
author = {Al-Quadan, Farouk and Akel, Hazem and Natshi, Rasha},
volume = {9},
number = {3},
year = {2009},
month = {Sep},
pages = {67-74},
doi = {10.3844/ojbsci.2009.67.74},
url = {https://thescipub.com/abstract/ojbsci.2009.67.74},
abstract = {Problem statement: This study reported the purification and characterization of a novel highly thermostable alkaline amylase from a newly isolated Bacillus strain HUTBS71. Approach: The enzyme was purified using ammonium sulfate precipitation, ion exchange and gel filtration chromatography. Results: Maximum amylase activity (72 U mL-1) was obtained at 100°C after 10 min of incubation. The enzyme was purified 24 fold with 12.5% yield and showed a monomer band with a molecular weight of 58.8 kDa by SDS-PAGE. This enzyme exhibited maximum activity at pH and temperature, 7.8 and 100°C, respectively. It performed stability over a broad range of pH and temperature, 5.2-10.0 and 80-115°C, respectively. The half-life of the enzyme at 90 and 100°C was estimated to be 3 h. The activation energy of denaturation of purified enzyme was 2.53 kJ moL-1. The enzyme was activated by 5 mM of CoCl2, MgSO4, MnCl2, ZnSO4 and MnSO4 (relative activity was 133, 126, 133, 106.6 and 103%, respectively). It was strongly inhibited by CuSO4 and CdCl2 but less affected by NaCl, CaCl2, FeCl3, ZnCl2 and EDTA. Conclusion: The present purified amylase therefore could be defined as a highly thermostable, extremely hyperthermophilic and alkalitolerant with new properties make the present enzyme applicable for many starch processing and food industries.},
journal = {OnLine Journal of Biological Sciences},
publisher = {Science Publications}
}