@article{MAKHILLRJBS20105111067,
    title = {Characterization of Thermostable &#945;-amylase from Thermophilic</B> <B>andAlkaliphilic <I>Bacillus</I> sp. Isolate DM-15},
    journal = {Research Journal of Biological Sciences},
    volume = {5},
    number = {1},
    pages = {118-124},
    year = {2010},
    issn = {1815-8846},
    doi = {rjbsci.2010.118.124},
    url = {https://makhillpublications.co/view-article.php?issn=1815-8846&doi=rjbsci.2010.118.124},
    author = {Bahri,Makbule,Numan and},
    keywords = {isolation,characterization,Thermostable ±-amylase,thermophilic Bacillus,molecular mass,Turkey},
    abstract = {<I> Bacillus</I> sp. DM-15 was isolated from &Ccedil;iftehan Thermal Spring, Turkey produced thermostable &#945;-amylase at 55&deg;C at pH 9. Analysis of the enzyme for molecular mass and amylolytic activity carried out by SDS-Starch-PAGE electrophoresis revealed a single band with high molecular mass 126 kDa. After extraction, the enzyme remained stable in a range of temperature and pH between 40-100&deg;C and 4.5-10, respectively. The optimum enzyme activity was displayed at 60&deg;C and pH 5.5-6.0. &#945;-amylase production by thermophilic <I>Bacillus</I> sp. strain cultivated in liquid media reached a maximum at 12 h with levels of 27.5 &#956;mol mg<SUP>-1</SUP> protein min<SUP>-1</SUP>. The enzyme was stable for 15 min at 60&deg;C  while 24% of the original activity was lost at 100&deg;C. Enzyme activity was increased in the presence of 5 mM CaCl<SUB>2</SUB>, Na<SUB>2</SUB>SO<SUB>3</SUB> and KCl (105%) and inhibited in the presence of 5 mM EDTA, CuSO<SUB>4</SUB>, FeSO<SUB>4</SUB>, SDS (1%), Urea (8 M), Co up to 98, 79, 57, 36, 33 and 10%, respectively. The DM-15 &#945;-amylase may be suitable for in liquefaction of starch in detergent and textile industries and in other industrial applications.}
    }