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Literature summary for 3.2.1.7 extracted from

  • Yang, J.; Zhang, J.; Mao, L.; You, X.; Chen, G.
    Genetic modification and optimization of endo-inulinase for the enzymatic production of oligofructose from inulin (2016), J. Mol. Catal. B, 134, 225-232 .
No PubMed abstract available
Search for more literature for 3.2.1.7

Application

Application Comment Organism
synthesis enzymatic hydrolyzation of inulin by endo-inulinase to produce oligofructoses, a type of food additive and health product, a promising green and environmentally friendly technique Fusarium oxysporum

Cloned(Commentary)

Cloned (Comment) Organism
gene inu1, DNA and amino acid sequence determination and analysis, domain structure, phylogenetic analysis, recombinant expression of full-length and truncated enzymes in Pichia pastoris Fusarium oxysporum

Protein Variants

Protein Variants Comment Organism
additional information genetic modification and optimization of endo-inulinase for the enzymatic production of oligofructose from inulin, method optimization, overview. The activity of recombinant truncated enzyme TrINU reaches 148 U/ml which is significantly higher than that of recombinant full-length enzyme INU with 115 U/ml. Improvement of the stability of TrINU via mutation of protease cleavage sites. The optimal reaction conditions for Fusarium oxysporum endo-inulinase are: NaAc-HAc buffer, pH 5.0, 2 mM Mg2+, 8% substrate, and an incubation temperature of 55°C Fusarium oxysporum

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ activates Fusarium oxysporum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
inulin + H2O Fusarium oxysporum
-
 inulotriose + inulotetraose + inulopentaose
-
 ?
inulin + H2O Fusarium oxysporum ACCC31352
-
 inulotriose + inulotetraose + inulopentaose
-
 ?

Organism

Organism UniProt Comment Textmining
Fusarium oxysporum A0A1B2CX88
-
-
Fusarium oxysporum ACCC31352 A0A1B2CX88
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 the activity of recombinant truncated enzyme TrINU reaches 148 U/ml which is significantly higher than that of recombinant full-length enzyme INU with 115 U/ml, pH 5.0, 55°C Fusarium oxysporum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
inulin + H2O
-
 Fusarium oxysporum inulotriose + inulotetraose + inulopentaose
-
 ?
inulin + H2O
-
 Fusarium oxysporum ACCC31352 inulotriose + inulotetraose + inulopentaose
-
 ?

Subunits

Subunits Comment Organism
More analysis of domains within the full-length endo-inulinase and its truncated derivatives, overview Fusarium oxysporum

Synonyms

Synonyms Comment Organism
endo-inulinase
-
 Fusarium oxysporum
inu1
-
 Fusarium oxysporum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
-
-
 Fusarium oxysporum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
-
 Fusarium oxysporum

General Information

General Information Comment Organism
physiological function Inulinases are a group of enzymes that catalyze the hydrolysis of the (2-1)-beta-D-fructosidic linkages in inulin. Inulinases can be further classified into the following two types of enzymes: exo-inulinases (EC 3.2.1.80) and endo-inulinases (EC 3.2.1.7). Endo-inulinases hydrolyze the internal linkages in inulin, yielding an oligofructose mixture with inulotriose, inulotetraose, and inulopentaose as the main components Fusarium oxysporum