Protein Variants | Comment | Organism |
---|---|---|
additional information | bioinspired production of antibacterial sucrose isomerase-sponge for the synthesis of isomaltulose, enzyme immobilization, method development, optimization, and evaluation, overview. The enzyme is immobilized on a epsilon-poly-L-lysine (epsilons-PL)-gelatin sponge as matrix is produced by the lyophilizing method, using water as a porogen. The carboxyl groups of gelatin are activated by 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide (EDC) and N-hydroxysuccinimide (NHS) to form reactive NHS esters, which can promote the rate of the synthesis reaction to form a stable amide bond. Then the esters react with amine groups of epsilon-PL to form peptide bonds. Through a series of cross-linking reactions, gelatin and epsilon-PL form a sponge. The affinity of immobilized enzyme SIase to substrate is basically unchanged. Immobilized SIase still exhibits more than 90% sucrose conversion after 13 consecutive cycles, which indicates that it has a good operational stability. Furthermore, the immobilized SIase has the potential for isomaltulose production, with 200 g/l sucrose solution as its substrate in the food industry. Isomaltulose is isolated in 83.58% yield and high purity (97.3%). epsilon-Poly-L-lysine (epsilon-PL), is an ideal carrier for enzyme immobilization and has attracted considerable attention because of its good biocompatibility, antimicrobial activity, and non-toxic characteristic. The loose and porous structures of epsilon-PL-gelatin sponge are critical for ensuring relatively high catalytic efficiency | Erwinia rhapontici |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.246 | - |
sucrose | immobilized recombinant enzyme, pH 6.0, 30°C | Erwinia rhapontici | |
0.26 | - |
sucrose | free recombinant enzyme, pH 6.0, 30°C | Erwinia rhapontici |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
sucrose | Erwinia rhapontici | - |
6-O-alpha-D-Glucopyranosyl-D-fructofuranose | - |
r | |
sucrose | Erwinia rhapontici NX-5 | - |
6-O-alpha-D-Glucopyranosyl-D-fructofuranose | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Erwinia rhapontici | - |
- |
- |
Erwinia rhapontici NX-5 | - |
- |
- |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
6 | - |
free recombinant enzyme, pH 6.0, 30°C | Erwinia rhapontici |
71.58 | - |
immobilized recombinant enzyme, pH 6.0, 30°C | Erwinia rhapontici |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
sucrose | - |
Erwinia rhapontici | 6-O-alpha-D-Glucopyranosyl-D-fructofuranose | - |
r | |
sucrose | - |
Erwinia rhapontici NX-5 | 6-O-alpha-D-Glucopyranosyl-D-fructofuranose | - |
r |
Synonyms | Comment | Organism |
---|---|---|
SIase | - |
Erwinia rhapontici |
sucrose isomerase | - |
Erwinia rhapontici |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
free recombinant enzyme | Erwinia rhapontici |
40 | - |
immobilized recombinant enzyme | Erwinia rhapontici |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.5 | - |
immobilized recombinant enzyme | Erwinia rhapontici |
6 | - |
free recombinant enzyme | Erwinia rhapontici |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
4 | 8 | and above, the immobilized enzyme retains over 50% of its relative activity | Erwinia rhapontici |
5 | 8 | the free enzyme retains over 50% of its relative activity | Erwinia rhapontici |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
4.5 | 8 | the immobilized enzyme retains more than 80% of its relative activity at pH 4.5-8.0 | Erwinia rhapontici |
5 | 7.5 | the free enzyme retains more than 80% of its relative activity at pH 5.0-7.5 | Erwinia rhapontici |