• DocumentCode
    1960372
  • Title

    Chemical modification and thermal stability study of β-cyclodextrin- and PAMAM-trypsin conjugates

  • Author

    Treetharnmathurot, B. ; Ovatlarnporn, C. ; Wungsinthaweekul, Juraithip ; Wiwattanapatapee, Ruedeekom

  • Author_Institution
    Dept. of Pharm. Technol., Prince of Songkla Univ., Songkhla
  • fYear
    2009
  • fDate
    5-8 Jan. 2009
  • Firstpage
    954
  • Lastpage
    959
  • Abstract
    Bovine pancreatic trypsin conjugates were first synthesized using succinoylated beta-cyclodextrin and succinoylated PAMAM dendrimer. Their conjugates had a trypsin content of 72 and 50 wt%, respectively. The trypsin activity of conjugates measured by using Nalpha-benzoyl-D, L-arginine-p-nitroanilide hydrochloride (BAPNA) as substrate was decreased by polymer conjugation. The kinetic parameters (KM, Vmax and Kcat) were also calculated. The beta-cyclodextrin-trypsin conjugate was more stable than native trypsin and PAMAM-trypsin conjugate at all temperatures between 30-70degC. It also exhibited better thermal stability in the autolysis assays at 40degC.
  • Keywords
    biomedical materials; enzymes; polymers; thermal stability; Bovine pancreatic trypsin conjugates; PAMAM-trypsin conjugates; beta-cyclodextrin conjugates; polymer conjugation; temperature 30 degC to 70 degC; thermal stability; Amino acids; Biochemistry; Chemical technology; Chemistry; Drugs; Immune system; Polymers; Proteins; Thermal resistance; Thermal stability; β-cyclodextrin; PAMAM dendrimer; polymer-protein conjugates; thermal stability;
  • fLanguage
    English
  • Publisher
    ieee
  • Conference_Titel
    Nano/Micro Engineered and Molecular Systems, 2009. NEMS 2009. 4th IEEE International Conference on
  • Conference_Location
    Shenzhen
  • Print_ISBN
    978-1-4244-4629-2
  • Electronic_ISBN
    978-1-4244-4630-8
  • Type

    conf

  • DOI
    10.1109/NEMS.2009.5068732
  • Filename
    5068732