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Literature summary extracted from

  • Li, L.; Yu, Y.; Zhang, X.; Jiang, Z.; Zhu, Y.; Xiao, A.; Ni, H.; Chen, F.
    Expression and biochemical characterization of recombinant alpha-L-rhamnosidase r-Rha1 from Aspergillus niger JMU-TS528 (2016), Int. J. Biol. Macromol., 85, 391-399 .
    View publication on PubMed

Application

EC Number Application Comment Organism
3.2.1.40 drug development the characteristics (good thermostability, wide range of pH-stability with the optimum pH of 5.0 and temperature of 60°C, not greatly affected by representative metal ions, excellent tolerance abilities against glucose and ethanol) of the enzyme suggest that it should be considered a potential new biocatalyst for food and drug industrial applications Aspergillus niger
3.2.1.40 food industry the characteristics (good thermostability, wide range of pH-stability with the optimum pH of 5.0 and temperature of 60°C, not greatly affected by representative metal ions, excellent tolerance abilities against glucose and ethanol) of the enzyme suggest that it should be considered a potential new biocatalyst for food and drug industrial applications Aspergillus niger

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.40 overexpression in Pichia pastoris GS115s Aspergillus niger

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.40 Fe2+ 100 mM, complete inactivation Aspergillus niger
3.2.1.40 Fe3+ 10 mM, 46% inhibition. 100 mM, 91% inhibition Aspergillus niger

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.40 Ca2+ 10 mM, 1.1fold activation. 100 mM, 1.4fold activation Aspergillus niger
3.2.1.40 Co2+ 10 mM, 1.1fold activation. 100 mM, 1.6fold activation Aspergillus niger
3.2.1.40 Cu2+ 10 mM, 1.2fold activation. 100 mM, 1.3fold activation Aspergillus niger
3.2.1.40 Fe2+ 10 mM, 1.1fold activation Aspergillus niger
3.2.1.40 Mg2+ 10 mM or 100 mM, 1.1fold activation Aspergillus niger
3.2.1.40 Mn2+ 100 mM, 1.5fold activation Aspergillus niger
3.2.1.40 Ni2+ 100 mM, 1.5fold activation Aspergillus niger
3.2.1.40 Zn2+ 10 mM, 1.1fold activation. 100 mM, 1.5fold activation Aspergillus niger

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.40 Aspergillus niger R9W5L0
-
-
3.2.1.40 Aspergillus niger JMU-TS528 R9W5L0
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.40 711.9
-
 activity of the recombinant overexpressed enzyme, pH and temperature not specified in the publication Aspergillus niger

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.40 4-nitrophenyl alpha-L-rhamnopyranoside + H2O 70.1% of the activity compared to naringin Aspergillus niger 4-nitrophenol + alpha-L-rhamnopyranose
-
 ?
3.2.1.40 4-nitrophenyl alpha-L-rhamnopyranoside + H2O 70.1% of the activity compared to naringin Aspergillus niger JMU-TS528 4-nitrophenol + alpha-L-rhamnopyranose
-
 ?
3.2.1.40 hesperidin + H2O 144.9% of the activity compared to naringin Aspergillus niger hesperetin 7-O-beta-D-glucoside + alpha-L-rhamnose
-
 ?
3.2.1.40 hesperidin + H2O 144.9% of the activity compared to naringin Aspergillus niger JMU-TS528 hesperetin 7-O-beta-D-glucoside + alpha-L-rhamnose
-
 ?
3.2.1.40 additional information the enzyme posseses broad substrate specificities by hydrolyzing alpha-1,2, alpha-1,3 alpha-1,4, and alpha-1,6 linkages to beta-D-glucosides Aspergillus niger ?
-
 ?
3.2.1.40 additional information the enzyme posseses broad substrate specificities by hydrolyzing alpha-1,2, alpha-1,3 alpha-1,4, and alpha-1,6 linkages to beta-D-glucosides Aspergillus niger JMU-TS528 ?
-
 ?
3.2.1.40 myricetrin + H2O 22.5% of the activity compared to naringin Aspergillus niger 3,5,7-trihydroxy-2-(3,4,5-trihydroxyphenyl)-4H-chromen-4-one + alpha-L-rhamnose
-
 ?
3.2.1.40 naringin + H2O
-
 Aspergillus niger beta-D-glucopyranosyl-2,3-dihydro-4',5,7-trihydroxyflavone + alpha-L-rhamnose
-
 ?
3.2.1.40 naringin + H2O
-
 Aspergillus niger JMU-TS528 beta-D-glucopyranosyl-2,3-dihydro-4',5,7-trihydroxyflavone + alpha-L-rhamnose
-
 ?
3.2.1.40 rutin + H2O 136.7% of the activity compared to naringin Aspergillus niger isoquercitrin + alpha-L-rhamnose
-
 ?
3.2.1.40 rutin + H2O 136.7% of the activity compared to naringin Aspergillus niger JMU-TS528 isoquercitrin + alpha-L-rhamnose
-
 ?
3.2.1.40 saikosaponin C + H2O 9.19% of the activity compared to naringin Aspergillus niger (3beta,16beta)-16-hydroxy-13,28-epoxyolean-11-en-3-yl) 6-O-beta-D-glucopyranosyl-beta-D-glucopyranoside + alpha-L-rhamnose
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.40 60
-
-
 Aspergillus niger

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.40 30 70 30°C: about 65% of maximal activity, 70°C: about 55% of maximal activity Aspergillus niger

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.40 50
-
 half-life time: 32.66 h Aspergillus niger
3.2.1.40 55
-
 half-life time: 15.44 h Aspergillus niger
3.2.1.40 60
-
 half-life time: 2.59 h Aspergillus niger
3.2.1.40 65
-
 half-life time: 18.7 min Aspergillus niger
3.2.1.40 70
-
 half-life time: 4.6 min Aspergillus niger

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.40 5
-
-
 Aspergillus niger

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.40 3 11 24 h, 4°C, more than 45% of its enzymatic activity is retained Aspergillus niger