Cloning and characterization of an endo-β-1,3(4)glucanase and an aspartic protease from Phaffia rhodozyma CBS 6938
| Autor: | M. L. Bang, T. Sandal, I. Villadsen |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Signal peptide
DNA Complementary cDNA library Basidiomycota Genes Fungal Molecular Sequence Data Saccharomyces cerevisiae Sequence Analysis DNA General Medicine Glucanase Molecular cloning Biology Applied Microbiology and Biotechnology Molecular biology Isoelectric point Cellulase Biochemistry Complementary DNA Expression cloning Aspartic Acid Endopeptidases Amino Acid Sequence Cloning Molecular Peptide sequence Biotechnology |
| Zdroj: | Applied Microbiology and Biotechnology. 51:215-222 |
| ISSN: | 1432-0614 0175-7598 |
| DOI: | 10.1007/s002530051384 |
| Popis: | We describe the identification and expression cloning of two novel enzymes, a beta-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)-beta-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 degrees C. Both enzymes show only low sequence identity to other known enzymes. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full text from SpringerLink