@article{MAKHILLJAVA201312194289,
    title = {Cloning of a Gene Encoding Xylanase B from <I>Aspergillus niger</I> and 
  its Expression in <I>Escherichia coli},
    journal = {Journal of Animal and Veterinary Advances},
    volume = {12},
    number = {19},
    pages = {1489-1494},
    year = {2013},
    issn = {1680-5593},
    doi = {javaa.2013.1489.1494},
    url = {https://makhillpublications.co/view-article.php?issn=1680-5593&doi=javaa.2013.1489.1494},
    author = {Yinglei,Renjie and},
    keywords = {Xylanase,xynB gene,Aspergillus niger,Escherichia coli,enzyme},
    abstract = {In this study, the gene <I>xynB</I> encoding xylanase B, obtained from <I>Aspergillus 
  niger</I> AN-1 was cloned and efficiently expresed in <I>E. coli</I> BL21. The 
  full-length gene contained 658 bp and encoded a mature protein containing 225 
  amino acids. The purified, recombinant xylanase XYNB showed one band at about 
  25 kDa. The maximum yeild of the recombinant xylamase was 4.09x10<SUP>5</SUP> 
  U g<SUP>-1</SUP> which was higher than that obtained when <I>Aspergillus niger</I> 
  was solid state fermented. The optimal temperature of XYNB was 50&deg;C and 
  recombinant enzyme displayed about 75% of peak activity in the temperature range 
  found in the body of animals to which the enzyme might be fed. The optimum pH 
  of XYNB was about pH 5.0 and the recombinant enzyme retained &gt;80% enzyme 
  activity in the pH range found in the animal gastrointestinal tract where the 
  enzyme might take effect. These enzyme properties suggested that this enzyme 
  could be potentially useful in feed industry.}
    }