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Related Experiment Videos

Some properties of a cyclomaltodextrin-glucanotransferase from Bacillus circulans DF 9 R type

L R Maréchal1, A M Rosso, M A Maréchal

  • 1Instituto de Investigaciones Bioquímicas Luis F. Leloir Fundación Campomar, Buenos Aires, Argentina.

Cellular and Molecular Biology (Noisy-Le-Grand, France)
|July 1, 1996
PubMed
Summary

Cyclomaltodextrin-glucanotransferase (CGTase) from Bacillus circulans was purified and characterized. Its stability significantly increased with calcium ions or alpha-cyclodextrins, enhancing cyclodextrin production.

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Area of Science:

  • Enzymology
  • Biochemistry
  • Microbiology

Background:

  • Cyclomaltodextrin-glucanotransferase (CGTase) is an enzyme crucial for cyclodextrin production.
  • Bacillus circulans is a known source of industrially relevant enzymes.
  • Understanding CGTase properties is key to optimizing its applications.

Purpose of the Study:

  • To purify and characterize CGTase from Bacillus circulans strain DF 9, R type.
  • To investigate factors influencing the enzyme's thermal stability and activity.
  • To determine the cyclodextrin product profile and conversion efficiency.

Main Methods:

  • Enzyme purification to homogeneity.
  • Isoelectric focusing (IEF) for pI determination.
  • SDS-PAGE for molecular weight estimation.

Related Experiment Videos

  • Enzyme activity assays across a range of pH and temperatures.
  • High-Performance Liquid Chromatography (HPLC) for cyclodextrin analysis.

    • Main Results:

    • Purified CGTase exhibited a pI of 5.3 and a molecular weight of 78 kDa.
    • Optimal enzymatic activity was observed over a broad pH range (4.5-7.5).
    • Thermal stability at 55°C increased 4-5 fold with calcium ions (10-100 mM) or 10 mM alpha-cyclodextrins.
    • HPLC analysis revealed an alpha:beta:gamma cyclodextrin ratio of approximately 1:0.9:0.4.
    • Maximal conversion of 5% soluble starch to cyclodextrins reached approximately 36%.

    Conclusions:

    • The purified Bacillus circulans CGTase is a robust enzyme with broad pH activity.
    • Calcium ions and alpha-cyclodextrins are effective stabilizers, enhancing enzyme performance.
    • The enzyme efficiently produces a mixture of cyclodextrins, with potential for industrial applications in carbohydrate modification.