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Literature summary for 3.2.1.40 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

Application Comment Organism
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)

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

Inhibitors

Inhibitors Comment Organism Structure
Hg2+ 10 mM Aspergillus tubingensis

KM Value [mM]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Aspergillus tubingensis A0A1B2K4A7
-
-
Aspergillus tubingensis JMU-TS529 A0A1B2K4A7
-
-

Posttranslational Modification

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

Purification (Commentary)

Purification (Comment) Organism
-
Aspergillus tubingensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
?
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

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

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4
-
-
Aspergillus tubingensis