Purification and characterization of two acetyl xylan esterases from Penicillium purpurogenum

Loreto Egaña, Rodrigo Gutiérrez, Valentina Caputo, Alessandra Peirano, Jeannette Steiner, Jaime Eyzaguirre

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51 Citations (Scopus)


Penicillium purpurogenum produces several enzymes active in xylan hydrolysis, of there, the acetyl xylan esterase (AXE) activity secreted by the fungus has now been studied. The amount of activity obtained in the culture is related to the degree of acetylation of the carbon source used, the best being chemically acetylated xylan. AXE was concentrated from culture supernatants by ultrafiltration and (NH4)2SO4 precipitation and fractionated by gel filtration in Bio-Gel P-300. Two peaks of activity (AXE I and AXE II) were obtained. These two enzymes were further purified separately to homogeneity by chromatography in CM-Sephadex C-50 and chromatofocusing. AXE I (M, 48,000) has a pI of 7.5, while AXE II (M(r) 23,000) has a pI of 7.8. Optimal enzyme activity was at pH 5.3 and 50°C for AXE I and pH 6.0 and 60°C for AXE II. Both enzymes are active towards several acetylated substrates. Antisera against the two enzymes do not cross-react, and the N-terminal sequences of AXE I and II do not show similarities. These results suggest that AXE I and AXE II are the products of different genes.

Original languageEnglish
Pages (from-to)33-39
Number of pages7
JournalBiotechnology and Applied Biochemistry
Issue number1
Publication statusPublished - 1996

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biotechnology


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