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Related Experiment Videos

Immobilized arylsulfotransferase.

D H Kim1, K Kobashi

  • 1Faculty of Pharmaceutical Science, Toyama Medical and Pharmaceutical University.

Journal of Biochemistry
|September 1, 1987
PubMed
Summary
This summary is machine-generated.

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Covalent immobilization enhanced arylsulfotransferase stability for storage. The immobilized enzyme maintained optimal activity and effectively sulfated tyrosine-containing peptides, showing promise for biotechnological applications.

Area of Science:

  • Biochemistry
  • Enzyme Engineering

Background:

  • Arylsulfotransferases (ATs) are crucial enzymes involved in sulfation reactions.
  • Stabilizing enzymes like ATs is essential for their practical application and storage.
  • Covalent immobilization is a common strategy to enhance enzyme stability.

Purpose of the Study:

  • To investigate the effect of covalent immobilization on arylsulfotransferase stability and activity.
  • To characterize the properties of immobilized arylsulfotransferase.
  • To evaluate the substrate specificity of the immobilized enzyme for tyrosine-containing peptides.

Main Methods:

  • Covalent immobilization of arylsulfotransferase onto DEAE-cellulose and DEAE-Sephadex.
  • Determination of optimal pH, Km for sulfate donor, and thermostability of free and immobilized enzymes.

Related Experiment Videos

  • Assay of sulfation activity using tyrosine-containing peptides as acceptor substrates.

    • Main Results:

    • Covalent immobilization significantly enhanced the storage stability of arylsulfotransferase.
    • The optimal pH, Km for sulfate donor, and thermostability of the immobilized enzyme were comparable to the free enzyme.
    • Immobilized arylsulfotransferase effectively catalyzed the sulfation of various tyrosine-containing peptides, including cholecystokinin-8-nonsulfate, tyrosine methylester, and (Leu)enkephalin.

    Conclusions:

    • Covalent immobilization is an effective method to stabilize arylsulfotransferase for improved storage and handling.
    • The immobilized enzyme retains its catalytic efficiency and substrate specificity.
    • Immobilized arylsulfotransferase holds potential for use in biotechnological processes requiring efficient sulfation of tyrosine-containing substrates.