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Purification of a heat-stable chitin deacetylase from Aspergillus nidulans and its role in cell wall degradation

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Abstract

An extracellular chitin deacetylase activity has been purified to homogeneity from autolyzed cultures of Aspergillus nidulans. This enzyme is an acidic glycoprotein with a pI of 2.75 and a 28% (wt/wt) carbohydrate content. The apparent M r of the enzyme estimated by SDS/PAGE and Superose 12 (f.p.l.c.) was around 27,000. The enzyme had an optimum pH at 7.0 and was stable in the pH range 4.0–7.5. Its optimum temperature of reaction was 50°C, and it was stable from 30° to 100°C after 1 h of preincubation. The enzyme hydrolyzed glycol chitin and oligomers of N-acetylgucosamine and to a lesser extent chitin, colloidal chitin, carboxymethylchitin, and an α-1 → 3,1 → 6-N-acetylgalactosamine-galactan among other substances with amido groups, but the enzyme did not hydrolyze peptide bonds. The role of this enzyme could be deacetylation of chitin oligosaccharides during autolysis, after action of endochitinase on cell walls.

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Authors and Affiliations

  1. Departamento de Microbiología Aplicada, Centro de Investigaciones Biológicas (C.S.I.C.), Velázquez 144, 28006, Madrid, Spain

    Carlos Alfonso, Oscar M. Nuero & Fuensanta Reyes

  2. Departamento de Biología Molecular, Universidad Autónoma de Madrid, Canto Blanco, 28049, Madrid, Spain

    Francisco Santamaría

Authors
  1. Carlos Alfonso
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  2. Oscar M. Nuero
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  3. Francisco Santamaría
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  4. Fuensanta Reyes
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Alfonso, C., Nuero, O.M., Santamaría, F. et al. Purification of a heat-stable chitin deacetylase from Aspergillus nidulans and its role in cell wall degradation. Current Microbiology 30, 49–54 (1995). https://doi.org/10.1007/BF00294524

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