• English
    • العربية
  • العربية
  • Login
  • QU
  • QU Library
  •  Home
  • Communities & Collections
  • Help
    • Item Submission
    • Publisher policies
    • User guides
    • FAQs
  • About QSpace
    • Vision & Mission
View Item 
  •   Qatar University Digital Hub
  • Qatar University Institutional Repository
  • Academic
  • University Publications
  • QU Ceased Journals
  • Qatar University Science Journal - [From 1981 TO 2007]
  • View Item
  • Qatar University Digital Hub
  • Qatar University Institutional Repository
  • Academic
  • University Publications
  • QU Ceased Journals
  • Qatar University Science Journal - [From 1981 TO 2007]
  • View Item
  •      
  •  
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Partial characterization Of an alkalophilic extracellular Crude pectinases from a bacillus Polymyxa strain

    Thumbnail
    View/Open
    079918-0009-fulltext.pdf (550.4Kb)
    Date
    1999
    Author
    Al Rajabi, Ihab. I. [ايهاب الرجبي وعادل محاسنه]
    Mahasneh, Adel M.
    Metadata
    Show full item record
    Abstract
    A mesophilic spore forming isolate from the soil of Um-Qais region, which could produce extracellular pectinases was tentatively identified as Bacillus polymyxa. This bacterium grew best at 37°C and pH 7.0 and was able to produce extracellular enzymes other than pectinases, e.g.: protease, amylases, and cellulases. The production of two pectolytic enzymes, pectin lyase and pectate lyase, by this organism was investigated. Pectin lyase production reached its maximum in 12h cultures, while pectate lyase reached its maximum production in 15h cultures. The optimum pH and optimum temperature for pectin lyase activity were 8.5 and 30°C, respectively, while for pectate lyase the optima were 9 and 30°C repectively. Chelating agents such as lmM EDTA caused a decrease in pectate lyase activity by about 48%, nitrilotriacetate (NTA) also caused a decrease in activity of pectin lyase and pectate lyase by about 35% and 53% respectively. Divalent ions such as, Co , Hg , Cu , and Fe inhibited pectin lyase activity at the concentration of lmM, while Mg+2, and Mn+2 stimulated the enzyme activity to about 105% and 140% respectively at the same concentration. Pectate lyase, was inhibited by Co+2, Hg+2, Cu+2 and Fe+3 at the concentration of lmM, while Mg+2, Zn+2, and Mn+2 stimulated its activity to about 106%, 186%, and 230%, respectively at the same concentration.
    DOI/handle
    http://hdl.handle.net/10576/9901
    Collections
    • Qatar University Science Journal - [From 1981 TO 2007] [‎770‎ items ]

    entitlement


    Qatar University Digital Hub is a digital collection operated and maintained by the Qatar University Library and supported by the ITS department

    Contact Us | Send Feedback
    Contact Us | Send Feedback | QU

     

     

    Home

    Submit your QU affiliated work

    Browse

    All of Digital Hub
      Communities & Collections Publication Date Author Title Subject Type Language Publisher
    This Collection
      Publication Date Author Title Subject Type Language Publisher

    My Account

    Login

    Statistics

    View Usage Statistics

    About QSpace

    Vision & Mission

    Help

    Item Submission Publisher policiesUser guides FAQs

    Qatar University Digital Hub is a digital collection operated and maintained by the Qatar University Library and supported by the ITS department

    Contact Us | Send Feedback
    Contact Us | Send Feedback | QU

     

     

    Video