Glycohydrolase contamination of commercial enzymes frequently used in the preparation of fungal cell walls

Thomas E. Davis, Judith E. Domer

Research output: Contribution to journalArticle

5 Scopus citations

Abstract

Commercial enzyme preparations frequently used in the preparation of fungal cell walls, viz., proteases, a lipase, and a phosphatase, were examined for the presence of contaminating glycohydrolase activity, since such activity could result not only in the removal of cytoplasmic constituents but also in the removal of portions of the wall itself. Glucosidase activities were detected in a protease of fungal origin, in a lipase from wheat germ, and in a phosphatase from potatoes. Additionally, two commercial protease preparations from Streptomyces griseus contained β-1,3-glucanase activity in significant amounts, a third contained trace amounts of the glucanase, but a fourth was totally free of glycohydrolase activity. The protease preparations from S. griseus released laminaribiose from yeast-phase cell walls of Histoplasma capsulatum chemotypes I and II, but only trace amounts of glucose were released. One protease was examined more closely and was found to be optimally active on laminarin at pH 5.5 and 50°C. It was also highly active on the same substrate at pH 8.0 and 37°C, however. A protease preparation from Aspergillus oryzae released glucose from the yeast-phase cell walls of H. capsulatum chemotypes I and II as well as from cell walls of Blastomyces dermatitidis, suggesting that the preparation contained both α- and β-glucanases.

Original languageEnglish (US)
Pages (from-to)593-600
Number of pages8
JournalAnalytical biochemistry
Volume80
Issue number2
DOIs
StatePublished - Jun 1977
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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