• DocumentCode
    534748
  • Title

    Study on the characterization of a potential thermostable β-galactosidase from thermus thermophilus HB27

  • Author

    Li, Yan ; Yao, Tianran ; Wei, Miao ; Yan, Ming ; Hao, Ning ; Xu, Lin

  • Author_Institution
    State Key Lab. of Mater.-Oriented Chem. Eng., Nanjing Univ. of Technol., Nanjing, China
  • Volume
    5
  • fYear
    2010
  • fDate
    16-18 Oct. 2010
  • Firstpage
    2118
  • Lastpage
    2121
  • Abstract
    A β-galactosidase gene bgal from Thermus thermophilus was cloned and expressed in Escherichia coli. The optimum temperature for this β-galactosidase activity was 70 °C, at which it maintained stable. The optimal pH for enzyme activity is 6.5. The Km value for ONPG was 3.5 mM, while in the presence of cysteine it decreased to 1.4 mM. Cysteine, β-mercaptoethanol, Fe2+ or Mn2+ promoted the enzymatic activity.
  • Keywords
    biochemistry; enzymes; microorganisms; molecular biophysics; pH; Escherichia coli; Thermus thermophilus HB27; beta-galactosidase activity; beta-galactosidase gene; beta-mercaptoethanol; cysteine; enzyme activity pH; iron dication; manganese dication; pH 6.5; temperature 70 degC; thermostable beta-galactosidase; Biotechnology; Dairy products; Kinetic theory; Proteins; Substrates; β-galactosidase; Thermus thermophilus; lactose;
  • fLanguage
    English
  • Publisher
    ieee
  • Conference_Titel
    Biomedical Engineering and Informatics (BMEI), 2010 3rd International Conference on
  • Conference_Location
    Yantai
  • Print_ISBN
    978-1-4244-6495-1
  • Type

    conf

  • DOI
    10.1109/BMEI.2010.5639979
  • Filename
    5639979
    • Link To Document
    https://search.isc.ac/dl/search/defaultta.aspx?DTC=49&DC=534748