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α-glucosidase from grape berries: Partial purification and characterization.

A D Peruffo1, F Renosto, C Pallavicini

  • 1Istituto di Chimica Agraria, Via Gradenigo, 6, I-35100, Padova, Italy.

Planta
|January 11, 2014
PubMed
Summary

Grape berry α-glucosidase was purified and characterized. This enzyme, important for carbohydrate breakdown, shows stability and specific inhibition patterns, suggesting potential applications.

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Area of Science:

  • Biochemistry
  • Enzymology

Background:

  • α-Glucosidase (EC 3.2.1.20) plays a key role in carbohydrate metabolism.
  • Understanding grape berry enzymes is crucial for food science and biotechnology.

Purpose of the Study:

  • To purify and characterize α-glucosidase from Vitis vinifera var. Riesling.
  • To investigate the enzyme's substrate specificity, kinetics, and inhibition patterns.

Main Methods:

  • Enzyme purification using chromatography.
  • Enzyme activity assays at varying pH.
  • Kinetic analysis and inhibition studies.

Main Results:

  • α-Glucosidase purified ~30-fold from grape berries.
  • Optimal activity at pH 5.1, molecular weight ~100,000 Da.
  • Inhibition studies suggest a Ping-Pong kinetic mechanism, treatable as a Uni Bi system.

Conclusions:

  • The purified grape berry α-glucosidase is stable and exhibits specific kinetic properties.
  • The enzyme may exist in multiple forms (pI 7.2, 8.2) and does not require ions.
  • Findings provide insights into grape berry carbohydrate processing and enzyme behavior.