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Production and characterization of extracellular α-amylases from the thermophilic fungus Thermomyces lanuginosus (wild and mutant strains)

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Abstract

α-Amylases from the thermophilic fungus, Thermomyces lanuginosus ATCC 34626 (wild and mutant strains), were purified to homogeneity by a simple procedure including, consecutively, precipitation with ice-cold 2-propanol, anion-exchange and molecular-sieve chromatographic methods. The molecular masses of the purified α-amylases (both with pI values of 3.0) were 58 kDa by SDS-PAGE. The optimal pH of α-amylase activity was 5.0 for the wild enzyme and 4.5 for the mutant one. 1-Cyclohexyl-3-(2-morpholinyl-4-ethyl)-carbodiimide (40–100 mM) and N-bromosuccinimide (0.1–1 mM) inhibited the enzymes, suggesting the involvement of carboxylic groups and tryptophan residues in the catalytic process.

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Authors and Affiliations

  1. Departments of Biochemistry, Bulgaria

    S.D. Petrova, N.G. Bakalova & D.N. Kolev

  2. Biotechnology, Faculty of Biology, University of Sofia `St. Kliment Ohridski', 1421 , Sofia, Bulgaria

    S.Z. Ilieva, A.P. Atev & M.K. Bhat

  3. Food Quality and Materials Science Department, Institute of Food Research, Norwich Laboratory, Colney, Norwich, NR4 7UA, UK

    S.Z. Ilieva, A.P. Atev & M.K. Bhat

Authors
  1. S.D. Petrova
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  2. S.Z. Ilieva
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  3. N.G. Bakalova
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  4. A.P. Atev
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  5. M.K. Bhat
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  6. D.N. Kolev
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Petrova, S., Ilieva, S., Bakalova, N. et al. Production and characterization of extracellular α-amylases from the thermophilic fungus Thermomyces lanuginosus (wild and mutant strains). Biotechnology Letters 22, 1619–1624 (2000). https://doi.org/10.1023/A:1005685226480

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  • DOI: https://doi.org/10.1023/A:1005685226480

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