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Related Experiment Videos

Bioaffinity based oriented immobilization of stem bromelain.

Pawan Gupta1, M Saleemuddin

  • 1Department of Biochemistry, Faculty of Life Sciences and Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, India. pawan_g75@hotmail.com

Biotechnology Letters
|June 21, 2006
PubMed
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Affinity-bound bromelain, an enzyme from pineapple stems, shows enhanced stability and broader pH activity compared to native or covalently immobilized forms. This immobilization method offers significant advantages for enzyme applications.

Area of Science:

  • Biochemistry
  • Enzyme Immobilization
  • Protein Chemistry

Background:

  • Bromelain is a thiol proteinase derived from pineapple stems.
  • Its unique oligosaccharide chain allows for specific binding interactions.
  • Enzyme immobilization is a key technique for enhancing enzyme properties.

Purpose of the Study:

  • To immobilize bromelain using affinity binding with concanavalin A (Con A).
  • To compare the properties of affinity-bound bromelain with native and covalently immobilized forms.
  • To evaluate the impact of immobilization on bromelain's thermal stability, pH profile, and kinetic parameters.

Main Methods:

  • Bromelain was affinity-bound to Sepharose pre-coupled with concanavalin A (Con A).
  • For comparison, bromelain was covalently coupled to CNBr-activated Sepharose.

Related Experiment Videos

  • Enzyme activity, thermal stability, pH profile, and kinetic parameters (Km, Vmax) were assessed for native and immobilized forms using casein as a substrate.

    • Main Results:

    • Affinity-bound bromelain demonstrated superior resistance to thermal inactivation, retaining over 50% activity after incubation at 60°C for 100 min.
    • The enzyme exhibited a broader pH-activity profile, maintaining over 60% activity at pH 11.
    • Apparent Km values were 1.1 mg/ml (native), 2 mg/ml (covalently coupled), and 0.54 mg/ml (affinity-bound), while Vmax remained unaffected by immobilization.

    Conclusions:

    • Affinity immobilization of bromelain using Con A-Sepharose significantly enhances its thermal stability and broadens its pH activity range.
    • This method provides a more favorable orientation and binding compared to covalent immobilization.
    • Affinity-bound bromelain exhibits improved kinetic properties, suggesting potential for optimized industrial applications.