3.2.1.7: inulinase
This is an abbreviated version!
For detailed information about inulinase, go to the full flat file.
Word Map on EC 3.2.1.7
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3.2.1.7
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fructose
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kluyveromyces
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aspergillus
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marxianus
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niger
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jerusalem
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artichoke
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invertase
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syrup
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fructans
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fructooligosaccharides
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nutrition
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food industry
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chicory
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ficuum
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saccharification
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beta-fructofuranosidase
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guilliermondii
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plackett-burman
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synthesis
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levanase
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high-fructose
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agave
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industry
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beta-fructosidase
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tuberosus
- 3.2.1.7
- fructose
- kluyveromyces
- aspergillus
- marxianus
- niger
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jerusalem
- artichoke
- invertase
- syrup
- fructans
- fructooligosaccharides
- nutrition
- food industry
- chicory
- ficuum
-
saccharification
- beta-fructofuranosidase
- guilliermondii
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plackett-burman
- synthesis
- levanase
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high-fructose
- agave
- industry
- beta-fructosidase
- tuberosus
Reaction
Synonyms
2,1-beta-D-fructanfructanohydrolase, AARAC_000847, An11g03200, AUD_0597, beta-2,1-D-fructan fructanohydrolase, beta-D-fructan fructanohydrolase, Endo I, Endo-I, Endo-II, endo-inulinase, endoinulinase, EnIA, extracellular endo-inulinase, fructofuranosyl hydrolase, Fructozyme L, Insulinase, inu1, Inu2, InuA, inuB, inuC, inuE, inulase, inulinase, P-III, PENSUB_1400, PENSUB_5768, PENSUB_5772, TCE0_044r16122, TSTA_051680, Xcp KM 24
ECTree
3.2.1.7 inulinaseAdvanced search results
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results (Engineering
Engineering on EC 3.2.1.7 - inulinase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D460E
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active to some extent. pKa of the acid/base catalyst decreases from 9.2 for the wild-type enzyme to 7.0 for the mutant
E323A
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enzyme efficiency (kcat/Km) is significantly lower than that of the wild-type due to a substantial decrease in kcat, but not due to variations in Km consistent with its putative role as nucleophile catalyst
E519A
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enzyme efficiency (kcat/Km) is significantly lower than that of the wild-type due to a substantial decrease in kcat, but not due to variations in Km consistent with its putative role as acid/base catalyst
D298A
mutation within the enlarged cavity formed by the conserved motif W-M(I)-N-D(E)-P-N-G, the so-called loop 1 and the loop 4. 59.7% of wild-typ activity
E43D
mutation within the enlarged cavity formed by the conserved motif W-M(I)-N-D(E)-P-N-G, the so-called loop 1 and the loop 4. 5.4% of wild-typ activity
F99A
mutation within the enlarged cavity formed by the conserved motif W-M(I)-N-D(E)-P-N-G, the so-called loop 1 and the loop 4. 6.1% of wild-typ activity
I70A
mutation within the enlarged cavity formed by the conserved motif W-M(I)-N-D(E)-P-N-G, the so-called loop 1 and the loop 4. 38.9% of wild-typ activity
M41A
mutation within the enlarged cavity formed by the conserved motif W-M(I)-N-D(E)-P-N-G, the so-called loop 1 and the loop 4. 56.2% of wild-typ activity
N265A
mutation within the enlarged cavity formed by the conserved motif W-M(I)-N-D(E)-P-N-G, the so-called loop 1 and the loop 4. 72.9% of wild-typ activity
N42G
mutation within the enlarged cavity formed by the conserved motif W-M(I)-N-D(E)-P-N-G, the so-called loop 1 and the loop 4. 7.1% of wild-typ activity
P62G
mutation within the enlarged cavity formed by the conserved motif W-M(I)-N-D(E)-P-N-G, the so-called loop 1 and the loop 4. 0.2% of wild-typ activity
Q59A
mutation within the enlarged cavity formed by the conserved motif W-M(I)-N-D(E)-P-N-G, the so-called loop 1 and the loop 4. 2.2% of wild-typ activity
R175A
mutation within the enlarged cavity formed by the conserved motif W-M(I)-N-D(E)-P-N-G, the so-called loop 1 and the loop 4. 0.1% of wild-typ activity
R295A
mutation within the enlarged cavity formed by the conserved motif W-M(I)-N-D(E)-P-N-G, the so-called loop 1 and the loop 4. 84.6% of wild-typ activity
W67A
mutation within the enlarged cavity formed by the conserved motif W-M(I)-N-D(E)-P-N-G, the so-called loop 1 and the loop 4. 2.4% of wild-typ activity
Y128H
site-directed mutagenesis, the mutation Y128H is in close proximity to the active site, it leads to modified enzyme catalytic activity with increased kcat and kcat/KM compared to untagged wild-type enzyme, while the activity of MBP-tagged wild-type enzyme is higher
Y128H/A316T/E344K/T504M
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme and MBP-fused wild-type enzyme
Y128H/E344K/T504M
site-directed mutagenesis, the mutation E344K is located on the enzyme protein surface, mutation Y128H is in close proximity to the active site. The mutant shows reduced activity compared to wild-type enzyme and MBP-fused wild-type enzyme
Y128H
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site-directed mutagenesis, the mutation Y128H is in close proximity to the active site, it leads to modified enzyme catalytic activity with increased kcat and kcat/KM compared to untagged wild-type enzyme, while the activity of MBP-tagged wild-type enzyme is higher
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Y128H/A316T/E344K/T504M
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site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme and MBP-fused wild-type enzyme
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Y128H/E344K/T504M
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site-directed mutagenesis, the mutation E344K is located on the enzyme protein surface, mutation Y128H is in close proximity to the active site. The mutant shows reduced activity compared to wild-type enzyme and MBP-fused wild-type enzyme
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additional information
additional information
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enzyme immobilization on chitin beads, half-life time of immobilized endo-inulinase in a packed-bed column reactor is 48 days
additional information
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structural and storage and functional thermostabilization of endo-inulinase through semi-rational modification of surface accessible lysine residues by pyridoxal 5'-phosphate and ascorbate reduction, method, molecular dynamics simulation, overview
additional information
maximum activity of recombinant endoinulinase, expressed in Pichia pastoris strain KM71, is 858 U/ml obtained at 120 h of the high cell density fermentation process. Inulooligosaccharides (IOS) are harvested with high concentration of 365.1 g/l and high yield up to 91.3%. IOS with different degrees of polymerization (DP) of mainly DP3-6 are distributed in the final reaction products
additional information
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maximum activity of recombinant endoinulinase, expressed in Pichia pastoris strain KM71, is 858 U/ml obtained at 120 h of the high cell density fermentation process. Inulooligosaccharides (IOS) are harvested with high concentration of 365.1 g/l and high yield up to 91.3%. IOS with different degrees of polymerization (DP) of mainly DP3-6 are distributed in the final reaction products
additional information
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maximum activity of recombinant endoinulinase, expressed in Pichia pastoris strain KM71, is 858 U/ml obtained at 120 h of the high cell density fermentation process. Inulooligosaccharides (IOS) are harvested with high concentration of 365.1 g/l and high yield up to 91.3%. IOS with different degrees of polymerization (DP) of mainly DP3-6 are distributed in the final reaction products
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additional information
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maximum activity of recombinant endoinulinase, expressed in Pichia pastoris strain KM71, is 858 U/ml obtained at 120 h of the high cell density fermentation process. Inulooligosaccharides (IOS) are harvested with high concentration of 365.1 g/l and high yield up to 91.3%. IOS with different degrees of polymerization (DP) of mainly DP3-6 are distributed in the final reaction products
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additional information
Aspergillus niger DSM 2466
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maximum activity of recombinant endoinulinase, expressed in Pichia pastoris strain KM71, is 858 U/ml obtained at 120 h of the high cell density fermentation process. Inulooligosaccharides (IOS) are harvested with high concentration of 365.1 g/l and high yield up to 91.3%. IOS with different degrees of polymerization (DP) of mainly DP3-6 are distributed in the final reaction products
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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
additional information
Fusarium oxysporum ACCC31352
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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
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additional information
mutants M-30 (115.0 U/ml) and M-31 (52.6 U/ml) show improved inulinase production compared to the wild-type. Initial moisture, inoculum, amount ratio of wheat bran to rice bran, temperature, pH for the maximum inulinase production by the mutant M-30 is 60.5%, 2.5%, 0.42, 30°C and 6.50, respectively. Under the optimized conditions, 455.9 U/grams of dry substrate (gds) of inulinase activity is reached in the solid state fermentation culture of the mutant. Glucose repression on the inulinase production by the mutant M-30 is relieved in some degree compared to that in its parent strain when the added glucose concentrations in the media are higher than 2.0%
additional information
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mutants M-30 (115.0 U/ml) and M-31 (52.6 U/ml) show improved inulinase production compared to the wild-type. Initial moisture, inoculum, amount ratio of wheat bran to rice bran, temperature, pH for the maximum inulinase production by the mutant M-30 is 60.5%, 2.5%, 0.42, 30°C and 6.50, respectively. Under the optimized conditions, 455.9 U/grams of dry substrate (gds) of inulinase activity is reached in the solid state fermentation culture of the mutant. Glucose repression on the inulinase production by the mutant M-30 is relieved in some degree compared to that in its parent strain when the added glucose concentrations in the media are higher than 2.0%
additional information
isolation of mutant M-30 with enhanced inulinase production, mutant is stable after cultivation for 20 generations. Inulin, yeast extract, NaCl, temperature, pH for maximum inulinase production by the mutant M-30 are 20.0 g/l, 5.0 g/l, 20.0 g/l, at 28°C and pH 6.5, respectively. Under the optimized conditions, 127.7 U/ml of inulinase activity is reached in the liquid culture
additional information
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mutants M-30 (115.0 U/ml) and M-31 (52.6 U/ml) show improved inulinase production compared to the wild-type. Initial moisture, inoculum, amount ratio of wheat bran to rice bran, temperature, pH for the maximum inulinase production by the mutant M-30 is 60.5%, 2.5%, 0.42, 30°C and 6.50, respectively. Under the optimized conditions, 455.9 U/grams of dry substrate (gds) of inulinase activity is reached in the solid state fermentation culture of the mutant. Glucose repression on the inulinase production by the mutant M-30 is relieved in some degree compared to that in its parent strain when the added glucose concentrations in the media are higher than 2.0%
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additional information
directed evolution yields variants showing up to 5fold improvements in soluble enzyme production compared to the starting point which enables high-yield production of highly purified recombinant enzyme. The distribution of the enzymatic reaction products demonstrates that after 24 h of incubation, the main product (57%) has a degree of polymerization of 3 (DP3). The MBP-fused wild-type enzyme shows increased activity compared to unaltered wild-type enzyme. The evolved endoinulinase mutant variants exhibit increased solubility and activity compared to wild-type
additional information
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directed evolution yields variants showing up to 5fold improvements in soluble enzyme production compared to the starting point which enables high-yield production of highly purified recombinant enzyme. The distribution of the enzymatic reaction products demonstrates that after 24 h of incubation, the main product (57%) has a degree of polymerization of 3 (DP3). The MBP-fused wild-type enzyme shows increased activity compared to unaltered wild-type enzyme. The evolved endoinulinase mutant variants exhibit increased solubility and activity compared to wild-type
additional information
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directed evolution yields variants showing up to 5fold improvements in soluble enzyme production compared to the starting point which enables high-yield production of highly purified recombinant enzyme. The distribution of the enzymatic reaction products demonstrates that after 24 h of incubation, the main product (57%) has a degree of polymerization of 3 (DP3). The MBP-fused wild-type enzyme shows increased activity compared to unaltered wild-type enzyme. The evolved endoinulinase mutant variants exhibit increased solubility and activity compared to wild-type
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