@article{MAKHILLJAVA20111022527,
    title = {Some Properties of a New Thermostable Xylanase from Alkaliphilic and Thermophilic <I>Bacillus</I> sp. Isolate DM-15},
    journal = {Journal of Animal and Veterinary Advances},
    volume = {10},
    number = {2},
    pages = {138-143},
    year = {2011},
    issn = {1680-5593},
    doi = {javaa.2011.138.143},
    url = {https://makhillpublications.co/view-article.php?issn=1680-5593&doi=javaa.2011.138.143},
    author = {Bahri Devrim,Ali,Numan and},
    keywords = {molecular weight,Bacillus sp,characterization,Thermostable xylanase,optimum,thermal spring},
    abstract = {Alkaliphilic and thermophilic <I>Bacillus</I> sp. DM-15 was isolated from ciftehan thermal spring, Turkey, produced thermostable xylanase at 55&deg;C at pH 9. The molecular weight of the enzyme was estimated to be 95.6 kDa by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The enzyme showed broad working pH range of 4.5-10.0 with an optimum pH of 6.5. The temperature optimum of the enzyme was found to be 60-70&deg;C. Xylanase production by thermophilic <I>Bacillus</I> sp. strain cultivated in liquid media reached a maximum at 36 h, with levels of 192.8 &#956;mol mg<SUP>-1</SUP> protein/min. The enzyme was stable for 15 min at 60&deg;C while 13, 86, 95 and 96% of the original activities were lost at 70, 80, 90 and 100&deg;C, respectively. Enzyme activity was increased in the presence of 5 mM CaCl<SUB>2</SUB> (137%), CoCl<SUB>2</SUB> (133%), CuSO<SUB>4</SUB> (112%), MgCl<SUB>2</SUB> (106%) and KCl (105%) and inhibited in the presence of 5 mM EDTA, HgCl<SUB>2</SUB>, FeSO<SUB>4</SUB>, SDS (1%), MnCl<SUB>2</SUB>, Triton X-100 (1%) up to 93, 89, 73, 41, 29 and 8%, respectively. The DM-15 thermostable xylanase may be suitable for several industrial applications, such as food, agricultural and biofuel.}
    }