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Literature summary for 3.2.1.40 extracted from

  • Soria, F.; Ellenrieder, G.
    Thermal inactivation and product inhibition of Aspergillus terreus CECT 2663 alpha-L-rhamnosidase and their role on hydrolysis of naringin solutions (2002), Biosci. Biotechnol. Biochem., 66, 1442-1449.
    View publication on PubMed
Search for more literature for 3.2.1.40

Inhibitors

Inhibitors Comment Organism Structure
L-rhamnose
-
 Aspergillus terreus
prunin
-
 Aspergillus terreus

Organism

Organism UniProt Comment Textmining
Aspergillus terreus
-
 CECT 2663
-
Aspergillus terreus CECT 2663
-
 CECT 2663
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
-
 Aspergillus terreus p-nitrophenol + alpha-L-rhamnopyranose
-
 ?
p-nitrophenyl-alpha-L-rhamnopyranoside + H2O
-
 Aspergillus terreus CECT 2663 p-nitrophenol + alpha-L-rhamnopyranose
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 2 h, 85% residual activity, inactivation is completely reversible, rhamnose and naringin protect Aspergillus terreus
60
-
 2 h, 70% residual activity, inactivation is completely reversible, rhamnose and naringin protect Aspergillus terreus
65
-
 2 h, 55% residual activity Aspergillus terreus
70
-
 2 h, 10% residual activity Aspergillus terreus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.1
-
 L-rhamnose pH 5.5, 40°C Aspergillus terreus
2.6
-
 prunin pH 5.5, 40°C Aspergillus terreus