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Literature summary for 3.2.1.26 extracted from

  • Azodi, M.; Falamaki, C.; Mohsenifar, A.
    Sucrose hydrolysis by invertase immobilized on functionalized porous silicon (2011), J. Mol. Catal. B, 69, 154-160.
No PubMed abstract available
Search for more literature for 3.2.1.26

Application

Application Comment Organism
synthesis immobilization of invertase on a porous silicon layer with appropriate catalytic behavior for the sucrose hydrolysis. The procedure is based on support surface chemical oxidation, silanization, activation with glutaraldehyde and finally covalent bonding of the free enzyme to the functionalized surface. Vmax undergoes a substantial increase of about 30% upon immobilization. The value of Km increases by a factor of 1.53 upon immobilization. The initial activity is still preserved up to 28 days while the free enzyme undergoes a 26% loss of activity after the same period Cyberlindnera jadinii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
24.5
-
 sucrose free enzyme, pH 4.5, 57°C Cyberlindnera jadinii
37.6
-
 sucrose immobilized enzyme, pH 4.5, 57°C Cyberlindnera jadinii

Organism

Organism UniProt Comment Textmining
Cyberlindnera jadinii
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
 Cyberlindnera jadinii
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sucrose + H2O
-
 Cyberlindnera jadinii alpha-D-glucose + D-fructose
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
57
-
 free enzyme, no significant change upon immobilization Cyberlindnera jadinii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5 5.5 immobilized enzyme Cyberlindnera jadinii
7 8 broad, free enzyme Cyberlindnera jadinii

pH Range

pH Minimum pH Maximum Comment Organism
4 8 free enzyme Cyberlindnera jadinii