Enhancement of the aspartame precursor synthetic activity of an organic solvent-stable protease
| Autor: | Hiroyasu Ogino, Masahiro Yasuda, Noriyuki Doukyu, Shotaro Tsuchiyama |
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| Rok vydání: | 2010 |
| Předmět: |
Models
Molecular Proteases Protein Conformation medicine.medical_treatment Thermolysin Bioengineering Phenylalanine Protein Engineering Biochemistry Substrate Specificity chemistry.chemical_compound Residue (chemistry) Enzyme Stability medicine Amino Acid Sequence Organic Chemicals Aspartame Molecular Biology chemistry.chemical_classification Protease Binding Sites fungi food and beverages Amino acid Kinetics Enzyme chemistry Mutation Mutagenesis Site-Directed Solvents Biotechnology Peptide Hydrolases |
| Zdroj: | Protein engineering, designselection : PEDS. 23(3) |
| ISSN: | 1741-0134 |
| Popis: | The PST-01 protease is highly stable and catalyzes the synthesis of the aspartame precursor with high reaction yields in the presence of organic solvents. However, the synthesis rate using the PST-01 protease was slower than that observed when thermolysin was used. Structural comparison of both enzymes showed particular amino acid differences near the active center. These few residue differences in the PST-01 protease were mutated to match those amino acid types found in thermolysin. The mutated PST-01 proteases at the 114th residue from tyrosine to phenylalanine showed enhancement of synthetic activity. This activity was found to be similar to thermolysin. In addition, mutating the residue in the PST-01 protease with arginine and serine showed more improvement of the activity. The mutant PST-01 protease should be more useful than thermolysin for the synthesis of the aspartame precursor, because this enzyme has higher stability and activity in the presence of organic solvents. The results show the potential of organic solvent-stable enzymes as industrial catalysts. |
| Databáze: | OpenAIRE |
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