Application | Comment | Organism |
---|---|---|
food industry | with the enhanced thermostability, the mutant enzyme, K406R/K573R, has potentially broadened the applications of alpha-L-rhamnosidase in food processing industry | Aspergillus niger |
Protein Variants | Comment | Organism |
---|---|---|
K406R/K573R | to improve the thermostability of the enzyme multiple arginine residues are introduced into the r-Rha1 sequence to replace several lysine residues that located on the surface of the folded enzyme. Hinted by in silico analysis, five surface Lys residues (K134, K228, K406, K440, K573) are targeted to produce a list of 5 single-residue mutants and 4 multiple-residue mutants using site-directed mutagenesis. Among these mutants, K406R/K573R shows the best thermostability improvement. The half-life of this mutant's enzyme activity increased 3 h at 60°C, 23 min at 65°C, and 3.5 min at 70°C, when compared with the wild type. With the enhanced thermostability, the mutant enzyme, K406R/K573R, has potentially broadened the applications of alpha-L-rhamnosidase in food processing industry | Aspergillus niger |
Organism | UniProt | Comment | Textmining |
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Aspergillus niger | R9W5L0 | - |
- |
Aspergillus niger JMU-TS528 | R9W5L0 | - |
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