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Literature summary for 3.2.1.168 extracted from
- Operational stabilization of fungal alpha-rhamnosyl-beta-glucosidase by immobilization on chitosan composites (2011), Process Biochem., 46, 2330-2335.
No PubMed abstract available
Application
| Application | Comment | Organism |
|---|---|---|
| biotechnology | bulk biotransformations, the hydrolytic and transglycosidic activity of alpha-rhamnosyl-beta-glucosidase has potential use for industrial processing of plant-based food and the products of the transglycosylation products could play a role as starting materials for the development of new drugs. The immobilization allows the kinetic control of the process | Acremonium sp. |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| DMSO | 1 h incubation at 60°C, no loss of activity at 10% v/v DSMO, 40% loss at 20% v/v DSMO, and no activity at 50% v/v DSMO of the free enzyme. The immobilized enzyme retains 82% of the activity, independently of DSMO concentration after the exposure at high temperature | Acremonium sp. |  |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.8 | - |
hesperidin | free enzyme, pH 5.0, 60°C | Acremonium sp. | |
| 8 | - |
hesperidin | immobilized enzyme, pH 5.0, 60°C, the change in the affinity of the enzyme to its substrate compared to the free enzyme is probably caused by structural changes introduced by the immobilization process and by the lower accessibility to the active site | Acremonium sp. | |
| 8.7 | - |
hesperidin methylchalcone | free enzyme, pH 5.0, 60°C | Acremonium sp. | |
| 38.7 | - |
hesperidin methylchalcone | immobilized enzyme, pH 5.0, 60°C, the change in the affinity of the enzyme to its substrate compared to the free enzyme is probably caused by structural changes introduced by the immobilization process and by the lower accessibility to the active site | Acremonium sp. | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Acremonium sp. | - |
enzyme is immobilized onto chitosan beads by adsorption and cross-linking | - |
Storage Stability
| Storage Stability | Organism |
|---|---|
| 8°C, immobilized enzyme, retains 100% activity during a long-term storage | Acremonium sp. |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| hesperidin + H2O | - |
Acremonium sp. | hesperetin + 6-O-alpha-L-rhamnopyranosyl-beta-D-glucopyranoside | - |
? | |
| hesperidin methylchalcone + H2O | - |
Acremonium sp. | hesperetin methylchalcone + 6-O-alpha-L-rhamnopyranosyl-beta-D-glucopyranoside | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| alpha-rhamnosyl-beta-glucosidase | a diglycosidase, catalyzing the transglycosylation and hydrolysis reactions | Acremonium sp. |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
study of the effect of temperature on the leakage of alpha-rhamnosyl-beta-glucosidase immoblized on chitosan-silica-polyethyleneimine beads | Acremonium sp. |
| 60 | - |
assay at | Acremonium sp. |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | - |
assay at | Acremonium sp. |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Acremonium sp. | since the isoelectric point of the enzyme is acidic, it is expected to interact with polyethyleneimine under the conditions of the immobilzation procedure | - |
5.7 |
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