Cloned (Comment) | Organism |
---|---|
gene PTO0069, functional recombinant expression of the gene, fused to the YlPir1 anchor gene, in Yarrowia lipolytica strain CLIB724, the enzyme is displayed on the cell surface | Picrophilus torridus |
Protein Variants | Comment | Organism |
---|---|---|
additional information | the trehalose synthase gene is fused to the YlPir1 anchor gene and then inserted into the genome of Yarrowia lipolytica strain CLIB724 leading to functional enzyme expression and a trehalose yield reaching 73% under optimal conditions. Thermal and pH stabilities of the cell surface-displayed recombinant enzyme are improved compared to those of its free form purified from recombinant Escherichia coli. After biotransformation, the glucose byproduct and residual maltose are directly fermented to ethanol by a Saccharomyces cerevisiae strain. Ethanol can be separated by distillation, and high-purity trehalose can easily be obtained from the fermentation broth. The results show that this one-pot procedure is an efficient approach to the economical production of trehalose from maltose. Method optimization and evaluation, overview. The optimal reaction temperature is 5°C higher than that of the free purified enzyme reported previously. As the temperature increases from 20°C to 60°C, the final concentrations of glucose increases from approximately 3 to 12.4 g/l. At 70°C the glucose production is approximately 4.4 g/l, and it is clear that the high temperature inhibits the production of trehalose as well as the hydrolysis reaction. The lyophilized engineered Y. lipolytica cells retain their original activity for 15 days at room temperature and lose only 15% activity after storage for 40 days | Picrophilus torridus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
maltose | Picrophilus torridus | - |
alpha,alpha-trehalose | - |
r | |
maltose | Picrophilus torridus ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 | - |
alpha,alpha-trehalose | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Picrophilus torridus | Q6L2Z7 | - |
- |
Picrophilus torridus ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 | Q6L2Z7 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
maltose | - |
Picrophilus torridus | alpha,alpha-trehalose | - |
r | |
maltose | - |
Picrophilus torridus ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 | alpha,alpha-trehalose | - |
r | |
additional information | the wild-type and the mutant enzymes show a hydrolytic side activity producing D-glucose from maltose | Picrophilus torridus | ? | - |
? | |
additional information | the wild-type and the mutant enzymes show a hydrolytic side activity producing D-glucose from maltose | Picrophilus torridus ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Trehalose synthase | - |
Picrophilus torridus |
TreS | - |
Picrophilus torridus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | - |
recombinant surface-displayed TreS | Picrophilus torridus |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | 80 | activity range. The optimal reaction temperature for the intramolecular transglucosylation of the recombinant surface-displayed TreS is 50°C, and 90% of the activity remains at 45°C and 55°C, over 50% of maximal activity at 30-65°C, profile overview | Picrophilus torridus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
recombinant surface-displayed TreS | Picrophilus torridus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
4 | 8 | activity range. Approximately 25% activity of the displayed TreS remains when at pH 4.0 and pH 8.0, maximal activity at pH 6.0, over 80% of maximal activity at pH 4.5-7.5, profile overview | Picrophilus torridus |