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Literature summary for 5.4.99.11 extracted from

  • Wu, L.; Qiu, J.; Wu, S.; Liu, X.; Liu, C.; Xu, Z.; Li, S.; Xu, H.
    Bioinspired production of antibacterial sucrose isomerase-sponge for the synthesis of isomaltulose (2016), Adv. Synth. Catal., 358, 4030-4040 .
No PubMed abstract available
Search for more literature for 5.4.99.11

Protein Variants

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 [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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Erwinia rhapontici
-
-
-
Erwinia rhapontici NX-5
-
-
-

Specific Activity [micromol/min/mg]

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 and Products (Substrate)

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

Synonyms Comment Organism
SIase
-
 Erwinia rhapontici
sucrose isomerase
-
 Erwinia rhapontici

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 free recombinant enzyme Erwinia rhapontici
40
-
 immobilized recombinant enzyme Erwinia rhapontici

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
 immobilized recombinant enzyme Erwinia rhapontici
6
-
 free recombinant enzyme Erwinia rhapontici

pH Range

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 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