Penicillium purpurogenum produces several xylanases: Purification and properties of two of the enzymes

Andrea Belancic, Juan Scarpa, Alessandra Peirano, René Díaz, Jeannette Steiner, Jaime Eyzaguirre

Research output: Contribution to journalArticlepeer-review

103 Citations (Scopus)

Abstract

The fungus Penicillium purpurogenum produces several extracellular xylanases. The two major forms (xylanases A and B) have been purified and characterized. After ammonium sulfate precipitation and chromatography in Bio-Gel P 100, xylanase A was further purified by means of DEAE-cellulose, hydroxylapatite and CM-Sephadex, and xylanase B by DEAE-cellulose and CM-Sephadex. Both xylanases showed apparent homogeneity in SDS-polyacrylamide gel electrophoresis. Xylanase A (33 kDa) has an isoelectric point of 8.6, while xylanase B (23 kDa) is isoelectric at pH 5.9. Antisera against both enzymes do not cross-react. The amino terminal sequences of xylanases A and B show no homology. The results obtained suggest that the enzymes are produced by separate genes and they may perform different functions in xylan degradation.

Original languageEnglish
Pages (from-to)71-79
Number of pages9
JournalJournal of Biotechnology
Volume41
Issue number1
DOIs
Publication statusPublished - 15 Jul 1995

Keywords

  • Amino acid sequence, similarity
  • Enzyme purification
  • P. purpurogenum
  • Xylanase

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology

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