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Literature summary for 3.2.1.40 extracted from

  • Kaur, A.; Singh, S.; Singh, R.; Schwarz, W.; Puri, M.
    Hydrolysis of citrus peel naringin by recombinant alpha-L-rhamnosidase from Clostridium stercorarium (2010), J. Chem. Technol. Biotechnol., 85, 1419-1422.
No PubMed abstract available
Search for more literature for 3.2.1.40

Application

Application Comment Organism
degradation recombinant rhamnosidase is thermostable and highly active for naringin hydrolysis up to more than 77%, thus producing L-rhamnose and prunin from citrus peel waste 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.
4-nitrophenyl-alpha-L-rhamnopyranoside + H2O
-
 Thermoclostridium stercorarium alpha-L-rhamnose + 4-nitrophenol
-
 ?
naringin + H2O citrus peel naringin Thermoclostridium stercorarium ?
-
 ?

Synonyms

Synonyms Comment Organism
RamA
-
 Thermoclostridium stercorarium

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
-
 Thermoclostridium stercorarium

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
70
-
 74% of maximum activity Thermoclostridium stercorarium
80
-
 36% of maximum activity Thermoclostridium stercorarium

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
 stable up to Thermoclostridium stercorarium

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
-
 Thermoclostridium stercorarium