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A thermostable maltose-tolerant alpha-amylase from Aspergillus tamarii

Fabiana Guillen Moreira1, Veridiana Lenartovicz, Rosane Marina Peralta

  • 1Departamento de Bioquímica, Universidade Estadual de Maringá, 87020-900, Maringá, PR. Brazil.

Journal of Basic Microbiology
|February 10, 2004
PubMed

Insights

A purified alpha-amylase from Aspergillus tamarii is a stable glycoprotein enzyme. It efficiently hydrolyzes starch, producing maltose and maltotriose with minimal end-product inhibition.

Area of Science:

  • Biochemistry
  • Enzymology
  • Microbial Biotechnology

Background:

  • Alpha-amylase enzymes are crucial for carbohydrate metabolism.
  • Aspergillus tamarii is a fungal source with potential for enzyme production.
  • Efficient purification of enzymes is key for industrial applications.

Purpose of the Study:

  • To purify and characterize alpha-amylase from Aspergillus tamarii.
  • To determine the enzyme's properties, including optimal conditions and stability.
  • To assess the enzyme's substrate specificity and inhibition profile.

Main Methods:

  • Homogeneous purification of alpha-amylase from Aspergillus tamarii.
  • Characterization of enzyme properties: pH optimum, temperature optimum, thermal stability.
  • Substrate specificity analysis and determination of kinetic parameters (K(M), V(max)).
  • Assessment of end-product inhibition by maltose and glucose.

Main Results:

  • A homogeneous alpha-amylase fraction was obtained with a molecular weight of 37.5 kDa.
  • Optimal activity was observed at pH 4.5-6.5 and temperatures of 50-55°C.
  • The enzyme demonstrated stability up to 65°C and preferentially hydrolyzed starch, amylose, and amylopectin.
  • Main hydrolysis products were maltose and maltotriose, with low sensitivity to end-product inhibition.

Conclusions:

  • The purified Aspergillus tamarii alpha-amylase is a robust and efficient enzyme.
  • Its properties make it suitable for applications requiring starch hydrolysis under specific conditions.
  • The enzyme's resistance to end-product inhibition is advantageous for industrial processes.

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