Cloning and characterization of an endo-β-1,3(4)glucanase and an aspartic protease from Phaffia rhodozyma cbs 6938

M. L. Bang, I. Villadsen, T. Sandal

Research output: Contribution to journalArticlepeer-review

Abstract

We describe the identification and expression cloning of two novel enzymes, a β-glucanase and an aspartic protease, secreted from the basidiomycetous yeast Phaffia rhodozyma. A cDNA library from P. rhodozyma CBS 6938 was constructed, and full-length cDNA encoding an endo-1,3(4)-β- glucanase (bg1) and an aspartic protease (pr1) were cloned by expression cloning in Saccharomyces cerevisiae W3124. The bg1 cDNA encodes a 424- residue precursor protein with a putative signal peptide. The pr1 cDNA encodes a 405-residue prepropolypeptide with an 81-residue leader peptide. The aspartic protease was purified and characterized. It has a molecular mass of 36 kDa, an isoelectric point of pH 7.5, a pH activity optimum at 4.0-6.0, and a temperature activity optimum around 40 °C. Both enzymes show only low sequence identity to other known enzymes.

Original languageEnglish
Pages (from-to)215-222
Number of pages8
JournalApplied Microbiology and Biotechnology
Volume51
Issue number2
DOIs
Publication statusPublished - 1999

ASJC Scopus subject areas

  • Biotechnology
  • Microbiology
  • Bioengineering

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