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Literature summary for 3.2.1.40 extracted from

  • Puri, M.; Kaur, A.; Singh, R.; Schwarz, W.; Kaur, A.
    One-step purification and immobilization of His-tagged rhamnosidase for naringin hydrolysis (2010), Process Biochem., 45, 451-456.
No PubMed abstract available

Application

Application Comment Organism
synthesis immobilization of recombinant enzyme on Ca2+ alginate beads. Immobilization enables its reutilization up to 9 hydrolysis batches without an appreciable loss in activity Thermoclostridium stercorarium

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Thermoclostridium stercorarium

Organism

Organism UniProt Comment Textmining
Thermoclostridium stercorarium Q9S3L0
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
naringin + H2O the free and immobilized enzymes achieve 76% and 67% hydrolysis of the naringin in Kinnow juice, respectively Thermoclostridium stercorarium ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
free enzyme Thermoclostridium stercorarium
60
-
enzyme immobilized in Ca2+ alginate beads Thermoclostridium stercorarium

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
free enzyme, less than 50% loss of activityafter 3 h Thermoclostridium stercorarium

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
free enzyme Thermoclostridium stercorarium
7.5
-
enzyme immobilized in Ca2+ alginate beads Thermoclostridium stercorarium