Cloning and expression of the gene encoding Streptomyces coelicolor A3(2) alpha-galactosidase belonging to family 36
| Autor: | Wook-Dong Kim, Kenji Kondoh, Satoshi Kaneko, Kohei Morisaki, Gwi-Gun Park, Hideyuki Kobayashi |
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| Rok vydání: | 2004 |
| Předmět: |
Molecular Sequence Data
Oligosaccharides Bioengineering Streptomyces coelicolor medicine.disease_cause Applied Microbiology and Biotechnology Homology (biology) Stachyose Substrate Specificity chemistry.chemical_compound medicine Escherichia coli Amino Acid Sequence Raffinose Cloning Molecular Thermus Melibiose N-Glycosyl Hydrolases chemistry.chemical_classification biology Sequence Homology Amino Acid Hydrolysis Thermus thermophilus Temperature Galactose General Medicine Hydrogen-Ion Concentration biology.organism_classification Molecular biology Amino acid Protein Structure Tertiary Biochemistry chemistry alpha-Galactosidase Electrophoresis Polyacrylamide Gel Biotechnology Plasmids |
| Zdroj: | Biotechnology letters. 27(9) |
| ISSN: | 0141-5492 |
| Popis: | The alpha-galactosidase gene of Streptomyces coelicolor A3(2) was cloned, expressed in Escherichia coli and characterized. It consisted of 1497 nucleotides encoding a protein of 499 amino acids with a predicted molecular weight of 57,385. The observed homology between the deduced amino acid sequences of the enzyme and alpha-galactosidase from Thermus thermophilus was over 40%. The alpha-galactosidase gene was assigned to family 36 of the glycosyl hydrolases. The enzyme purified from recombinant E. coli showed optimal activity at 40 degrees C and pH 7. The enzyme hydrolyzed p-nitrophenyl-alpha-D -galactopyroside, raffinose, stachyose but not melibiose and galactomanno-oligosaccharides, indicating that this enzyme recognizes not only the galactose moiety but also other substrates. |
| Databáze: | OpenAIRE |
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