Literature summary for 3.2.1.40 extracted from

Magario, I.; Neumann, A.; Oliveros, E.; Syldatk, C.
Deactivation kinetics and response surface analysis of the stability of alpha-L-rhamnosidase from Penicillium decumbens (2009), Appl. Biochem. Biotechnol., 152, 29-41.

Search for more literature for 3.2.1.40

General Stability

General Stability	Organism
addition of bovine serum albumine or increasing enzyme concentration up to 0.1 g/l renders the enzyme stable for 5 h without initial losses of activity	Penicillium decumbens

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
6.1	-	4-nitrophenyl alpha-L-rhamnopyranoside	60°C, pH 5.5	Penicillium decumbens

Organism

Organism	UniProt	Comment	Textmining
Penicillium decumbens	-	naringinase: complex of beta-D-glucosidase and alpha-L-rhamnosidase	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
13.3	-	60°C, pH 5.5	Penicillium decumbens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
4-nitrophenyl alpha-L-rhamnopyranoside + H2O	-	Penicillium decumbens	4-nitrophenol + alpha-L-rhamnose	-	?

Synonyms

Synonyms	Comment	Organism
naringinase	complex of beta-D-glucosidase and alpha-L-rhamnosidase	Penicillium decumbens

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
40	60	at low enzyme concentration, activity rapidly decreases within the first 30 min incubation time but afterwards remains stable at about 45% of the initial value for 5 h. Addition of bovine serum albumine or increasing enzyme concentration up to 0.1 g/l renders the enzyme stable for 5 h without initial losses of activity	Penicillium decumbens

pH Stability

pH Stability	pH Stability Maximum	Comment	Organism
3.5	-	naringinase complex, unstable below	Penicillium decumbens
4.5	5	naringinase complex, most stable within this range	Penicillium decumbens

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Release 2023.1 (January 2023)