Enzymes
| UniProtKB help_outline | 2 proteins |
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- Name help_outline keto-L-tagatose Identifier CHEBI:134275 (CAS: 17598-82-2) help_outline Charge 0 Formula C6H12O6 InChIKeyhelp_outline BJHIKXHVCXFQLS-LFRDXLMFSA-N SMILEShelp_outline [C@H](O)(C(CO)=O)[C@@H]([C@H](CO)O)O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline keto-L-sorbose Identifier CHEBI:13172 (Beilstein: 1724554,3588863) help_outline Charge 0 Formula C6H12O6 InChIKeyhelp_outline BJHIKXHVCXFQLS-OTWZMJIISA-N SMILEShelp_outline OC[C@H](O)[C@@H](O)[C@H](O)C(=O)CO 2D coordinates Mol file for the small molecule Search links Involved in 8 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:61780 | RHEA:61781 | RHEA:61782 | RHEA:61783 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Purification and characterization of D-allulose 3-epimerase derived from Arthrobacter globiformis M30, a GRAS microorganism.
Yoshihara A., Kozakai T., Shintani T., Matsutani R., Ohtani K., Iida T., Akimitsu K., Izumori K., Gullapalli P.K.
An enzyme that catalyzes C-3 epimerization between d-fructose and d-allulose was found in Arthrobacter globiformis strain M30. Arthrobacter species have long been used in the food industry and are well-known for their high degree of safety. The enzyme was purified by ion exchange and hydrophobic i ... >> More
An enzyme that catalyzes C-3 epimerization between d-fructose and d-allulose was found in Arthrobacter globiformis strain M30. Arthrobacter species have long been used in the food industry and are well-known for their high degree of safety. The enzyme was purified by ion exchange and hydrophobic interaction chromatographies and characterized as a d-allulose 3-epimerase (d-AE). The molecular weight of the purified enzyme was estimated to be 128 kDa with four identical subunits. The enzyme showed maximal activity and thermostability in the presence of Mg<sup>2+</sup>. The optimal pH and temperature for enzymatic activity were 7.0-8.0 and 70°C, respectively. The enzyme was immobilized to ion exchange resin whereupon it was stable for longer periods than the free enzyme when stored at below 10°C. In the column reaction, the enzyme activity also maintained stability for more than 4 months. Under these conditions, 215 kg of d-allulose produced per liter immobilized enzyme, and this was the highest production yield of d-allulose reported so far. These highly stable properties suggest that this enzyme represents an ideal candidate for the industrial production of d-allulose. << Less
J. Biosci. Bioeng. 123:170-176(2017) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.