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Literature summary extracted from

  • Li, L.; Gong, J.; Wang, S.; Li, G.; Gao, T.; Jiang, Z.; Cheng, Y.S.; Ni, H.; Li, Q.
    Heterologous expression and characterization of a new clade of Aspergillus alpha-L-rhamnosidase suitable for citrus juice processing (2019), J. Agric. Food Chem., 67, 2926-2935 .
    View publication on PubMed

Application

EC Number Application Comment Organism
3.2.1.40 food industry the enzyme can efficiently remove naringin from pomelo juice without changing its aroma. It is desirable for debittering citrus juice thereby improving the quality of juice Aspergillus tubingensis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.40 expression in Pichia pastoris GS115 Aspergillus tubingensis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.40 Hg2+ 10 mM Aspergillus tubingensis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.40 0.47
-
 naringin pH 4.0, 60°C Aspergillus tubingensis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.40 110000
-
 gel filtration Aspergillus tubingensis

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.40 Aspergillus tubingensis A0A1B2K4A7
-
-
3.2.1.40 Aspergillus tubingensis JMU-TS529 A0A1B2K4A7
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.2.1.40 glycoprotein the enzyme is secreted in the glycosylated form, which contains approximately 14 kDa of glycosidic chain Aspergillus tubingensis

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.40
-
 Aspergillus tubingensis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.40 naringin + H2O the enzyme shows a strong ability to hydrolyze naringin but scarcely acts on other substrates. It shows negligible activities on rutin, hesperidin, quercitrin, ginsenoside Rg2, myricitrin, saikosaponin C and 4-nitrophenyl-alpha-L-rhamnoside Aspergillus tubingensis beta-D-glucopyranosyl-2,3-dihydro-4',5,7-trihydroxyflavone + alpha-L-rhamnose
-
 ?
3.2.1.40 naringin + H2O the enzyme shows a strong ability to hydrolyze naringin but scarcely acts on other substrates. It shows negligible activities on rutin, hesperidin, quercitrin, ginsenoside Rg2, myricitrin, saikosaponin C and 4-nitrophenyl-alpha-L-rhamnoside Aspergillus tubingensis JMU-TS529 beta-D-glucopyranosyl-2,3-dihydro-4',5,7-trihydroxyflavone + alpha-L-rhamnose
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.40 monomer 1 * 110000, SDS-PAGE Aspergillus tubingensis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.40 50 60
-
 Aspergillus tubingensis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.40 48900
-
 naringin pH 4.0, 60°C Aspergillus tubingensis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.40 4
-
-
 Aspergillus tubingensis