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Literature summary for 3.2.1.40 extracted from

  • Spohner, S.; Zahn, D.; Schaum, V.; Quitmann, H.; Czermak, P.
    Recombinant alpha-L-rhamnosidase from Aspergillus terreus in selective trimming of alpha-L-rhamnose from steviol glycosides (2015), J. Mol. Catal. B, 122, 248-254 .
No PubMed abstract available
Search for more literature for 3.2.1.40

Application

Application Comment Organism
food industry Aspergillus terreus alpha-L-rhamnosidase specifically hydrolyses the glycosidic linkage of dulcoside A (the bitterest compounds in steviol glycoside mixtures), and converts it to rubusoside. During a 12 h biotransformation, the dulcoside A from crude leaf extracts is completely converted by recombinant alpha-L-rhamnosidase from Aspergillus terreus into rubusoside. This process offers a promising approach for reducing the bitterness of steviol glycoside mixtures Aspergillus terreus

Cloned(Commentary)

Cloned (Comment) Organism
expression of alpha-L-rhamnosidase in Pichia pastoris and Kluyveromyces lactis achieves high protein yields of up to 17.6 U/ml and 30.6 U/ml Aspergillus terreus

Organism

Organism UniProt Comment Textmining
Aspergillus terreus I0AZ41
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dulcoside A + H2O no hydrolytic activity against dulcoside A analogues. No transrhamnosylation activity is observed Aspergillus terreus rubusoside + alpha-L-rhamnose
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 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
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 enzyme produced by Pichia pastoris Aspergillus terreus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
 half-life: more than 30 h Aspergillus terreus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 8 recombinant enzymes Aspergillus terreus