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Literature summary extracted from

  • Pinuel, L.; Mazzaferro, L.; Breccia, J.D.
    Operational stabilization of fungal alpha-rhamnosyl-beta-glucosidase by immobilization on chitosan composites (2011), Process Biochem., 46, 2330-2335.
No PubMed abstract available

Application

EC Number Application Comment Organism
3.2.1.168 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

EC Number Inhibitors Comment Organism Structure
3.2.1.168 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.168 1.8
-
hesperidin free enzyme, pH 5.0, 60°C Acremonium sp.
3.2.1.168 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.
3.2.1.168 8.7
-
hesperidin methylchalcone free enzyme, pH 5.0, 60°C Acremonium sp.
3.2.1.168 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

EC Number Organism UniProt Comment Textmining
3.2.1.168 Acremonium sp.
-
enzyme is immobilized onto chitosan beads by adsorption and cross-linking
-

Storage Stability

EC Number Storage Stability Organism
3.2.1.168 8°C, immobilized enzyme, retains 100% activity during a long-term storage Acremonium sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.168 hesperidin + H2O
-
Acremonium sp. hesperetin + 6-O-alpha-L-rhamnopyranosyl-beta-D-glucopyranoside
-
?
3.2.1.168 hesperidin methylchalcone + H2O
-
Acremonium sp. hesperetin methylchalcone + 6-O-alpha-L-rhamnopyranosyl-beta-D-glucopyranoside
-
?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.168 alpha-rhamnosyl-beta-glucosidase a diglycosidase, catalyzing the transglycosylation and hydrolysis reactions Acremonium sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.168 additional information
-
study of the effect of temperature on the leakage of alpha-rhamnosyl-beta-glucosidase immoblized on chitosan-silica-polyethyleneimine beads Acremonium sp.
3.2.1.168 60
-
assay at Acremonium sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.168 5
-
assay at Acremonium sp.

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.2.1.168 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