Type your tag names separated by a space and hit enter

Temperature modulated solubility-activity alterations for poly(N-isopropylacrylamide)-lipase conjugates.


Chemical modification of proteins by use of functional polymers is expected to endow them with new properties without destroying their native functions, thus providing useful materials for application in different fields. We have synthesized poly(N-isopropylacrylamide) [poly(IPAAm)] co-oligomer with N,N-dimethylacrylamide (DMAAm) and reactive end groups by telomerization of IPAAm. This co-oligomer exhibits a lower critical solution temperature (LCST) at 37 degrees C. Using this temperature-responsive semitelechelic co-oligomer, we prepared polymer-enzyme conjugates of lipase by covalent coupling via carboxyl end-groups. This bioconjugate exhibits a LCST at 37 degrees C, having rapid, reversible hydration-dehydration changes due to highly mobile free polymer end groups. The conjugate retained its native enzymatic activity below this critical temperature, above which it precipitated and its catalytic function was shut off. This conjugate can be readily separated from reaction mixtures as a precipitate by simple temperature changes after reaction and reused in cycles without denaturation. Such a modulated system is attractive for application as a novel bioreactor system.


  • Publisher Full Text
  • FREE Publisher Full Text
  • Authors+Show Affiliations


    Department of Chemistry, Faculty of Science and Technology, Sophia University, Tokyo.

    , , , , ,


    Journal of biochemistry 116:3 1994 Sep pg 682-6


    Acrylic Resins
    Molecular Structure

    Pub Type(s)

    Journal Article



    PubMed ID