Production of Aspergillus niger β-mannosidase in Pichia pastoris
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
22884703
DOI
10.1016/j.pep.2012.07.012
PII: S1046-5928(12)00208-2
Knihovny.cz E-resources
- MeSH
- Aspergillus niger enzymology genetics MeSH
- beta-Mannosidase biosynthesis chemistry genetics isolation & purification MeSH
- Electrophoresis, Polyacrylamide Gel MeSH
- Fungal Proteins biosynthesis chemistry genetics isolation & purification MeSH
- Cloning, Molecular MeSH
- Hydrogen-Ion Concentration MeSH
- Culture Media MeSH
- Pichia enzymology genetics MeSH
- Recombinant Proteins biosynthesis chemistry genetics isolation & purification MeSH
- Enzyme Stability MeSH
- Temperature MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- beta-Mannosidase MeSH
- Fungal Proteins MeSH
- Culture Media MeSH
- Recombinant Proteins MeSH
β-Mannosidase (EC 3.2.1.25) is an exoglycosidase specific for the hydrolysis of terminal β-linked mannoside in various sugar chains. cDNA corresponding to the β-mannosidase gene was cloned from Aspergillus niger, sequenced, and expressed in the yeast Pichia pastoris. The β-mannosidase gene contains an open reading frame which encodes the protein with 933 amino acid residues. The wild type and recombinant proteins were purified to apparent homogeneity and biochemically characterized (K(M) 0.28 and 0.44 mmol/l for p-nitrophenyl β-d-mannopyranoside, pI 4.2 and 4.0, and their pH optima were at pH 4.5 and 5.5 and 65°C, respectively).
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