5.1.3.37: mannuronan 5-epimerase
This is an abbreviated version!
For detailed information about mannuronan 5-epimerase, go to the full flat file.
Word Map on EC 5.1.3.37
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5.1.3.37
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epimerases
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vinelandii
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azotobacter
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epimerization
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beta-d-mannuronic
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alpha-l-guluronic
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polysaccharide
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guluronic
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mannuronic
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c-5-epimerase
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epimerized
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homopolymeric
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polymannuronate
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laminaria
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analysis
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phaeophyceae
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alginate-producing
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syneresis
- 5.1.3.37
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epimerases
- vinelandii
- azotobacter
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epimerization
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beta-d-mannuronic
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alpha-l-guluronic
- polysaccharide
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guluronic
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mannuronic
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c-5-epimerase
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epimerized
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homopolymeric
- polymannuronate
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laminaria
- analysis
- phaeophyceae
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alginate-producing
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syneresis
Reaction
Synonyms
AlgE1, AlgE2, AlgE3, AlgE4, AlgE5, AlgE6, AlgE7, algG, alginate epimerase, C5-mannuronan epimerase, c5epi, ManC5-E, mannuronan C5-epimerase, MC5E, MEP13, MEP13-C5, MEP18, MEP18-C5, Mep2, MEP2-C5, MEP21, MEP21-C5, MEP25, MEP25-C5, MEP26, MEP26-C5, MEP27, MEP27-C5, MEP28, MEP28-C5, MEP29, MEP29-C5, Mep4, MEP4-C5, Mep6, MEP6-C5, Mep7, MEP7-C5, poly(beta-D-mannuronate) C5 epimerase 4
ECTree
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Engineering on EC 5.1.3.37 - mannuronan 5-epimerase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D152G
mutation eliminates almost all of both the lyase and epimerase activities
additional information
additional information
a truncated form of isoform AlgE1 (AlgE1-1) is converted to a combined epimerase and lyase by replacing the 5'-798 base pairs in the algE1-1 gene with the corresponding A-module-encoding DNA sequence from algE7
additional information
a truncated form of isoform AlgE1 (AlgE1-1) is converted to a combined epimerase and lyase by replacing the 5'-798 base pairs in the algE1-1 gene with the corresponding A-module-encoding DNA sequence from algE7
additional information
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a truncated form of isoform AlgE1 (AlgE1-1) is converted to a combined epimerase and lyase by replacing the 5'-798 base pairs in the algE1-1 gene with the corresponding A-module-encoding DNA sequence from algE7
additional information
a truncated form of isoform AlgE1 (AlgE1-1) is converted to a combined epimerase and lyase by replacing the 5'-798 base pairs in the algE1-1 gene with the corresponding A-module-encoding DNA sequence from bifunctional isoform algE7
additional information
a truncated form of isoform AlgE1 (AlgE1-1) is converted to a combined epimerase and lyase by replacing the 5'-798 base pairs in the algE1-1 gene with the corresponding A-module-encoding DNA sequence from bifunctional isoform algE7
additional information
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a truncated form of isoform AlgE1 (AlgE1-1) is converted to a combined epimerase and lyase by replacing the 5'-798 base pairs in the algE1-1 gene with the corresponding A-module-encoding DNA sequence from bifunctional isoform algE7
additional information
construction of a variety of truncated forms of isoform AlgE1. An A module alone is sufficient for epimerization and module A1 catalyzes the formation of contiguous stretches of G residues in the polymer, while module A2 introduces single G residues. The epimerization reaction is Ca2+ dependent, and both the A and R modules bind this cation. The R modules appear to reduce the Ca2+ concentration needed for full activity and also stimulate the reaction rate when positioned both N- and C-terminally
additional information
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construction of a variety of truncated forms of isoform AlgE1. An A module alone is sufficient for epimerization and module A1 catalyzes the formation of contiguous stretches of G residues in the polymer, while module A2 introduces single G residues. The epimerization reaction is Ca2+ dependent, and both the A and R modules bind this cation. The R modules appear to reduce the Ca2+ concentration needed for full activity and also stimulate the reaction rate when positioned both N- and C-terminally
additional information
construction of mutant enzymes that introduce a high level of G-blocks in poly(beta-(1->4)-D-mannuronate) more efficiently than the wild-type enzymes from Azotobacter vinelandii when employed for in vitro epimerization reactions. Shuffling of the genes encoding isoforms AlgE1 to AlgE6 leads to two epimerases that are more efficient in introducing G-blocks in poly(beta-(1->4)-D-mannuronate) than the naturally occurring enzymes, and one of these acts kinetically different than the G-block former AlgE6
additional information
division of algE1 into two parts based on the modular type of structure, and expression of each part in Escherichia coli. AlgE1 contains two catalytic domains, AlgE1-1, which introduces both G-blocks and MG-blocks, and AlgE1-2, which only introduces MG-blocks. AlgE1-1 has a much lower specific activity than both AlgE1-2 and AlgE1
additional information
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division of algE1 into two parts based on the modular type of structure, and expression of each part in Escherichia coli. AlgE1 contains two catalytic domains, AlgE1-1, which introduces both G-blocks and MG-blocks, and AlgE1-2, which only introduces MG-blocks. AlgE1-1 has a much lower specific activity than both AlgE1-2 and AlgE1
additional information
exchanging the R-modules between AlgE4 and AlgE6 resulted in a novel epimerase called AlgE64 with increased G-block forming ability compared with AlgE6
additional information
exchanging the R-modules between AlgE4 and AlgE6 resulted in a novel epimerase called AlgE64 with increased G-block forming ability compared with AlgE6
additional information
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exchanging the R-modules between AlgE4 and AlgE6 resulted in a novel epimerase called AlgE64 with increased G-block forming ability compared with AlgE6
additional information
mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it
additional information
mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it
additional information
mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it
additional information
mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it
additional information
mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it
additional information
mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it
additional information
mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it
additional information
mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it. Construction of thehybrid enzyme AlgE6A with A-module, and the hybrid enzyme AlgE64 constituted by the Amodule from AlgE6 and the R-module from AlgE4, modular structure, overview. The A-module is the minimal size for an active epimerase, even though the active site is located in proximity of the N-terminus. Reducing the size of AlgE6 influences the epimerization of modified alginates in solution
additional information
mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it. Construction of thehybrid enzyme AlgE6A with A-module, and the hybrid enzyme AlgE64 constituted by the Amodule from AlgE6 and the R-module from AlgE4, modular structure, overview. The A-module is the minimal size for an active epimerase, even though the active site is located in proximity of the N-terminus. Reducing the size of AlgE6 influences the epimerization of modified alginates in solution
additional information
mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it. Construction of thehybrid enzyme AlgE6A with A-module, and the hybrid enzyme AlgE64 constituted by the Amodule from AlgE6 and the R-module from AlgE4, modular structure, overview. The A-module is the minimal size for an active epimerase, even though the active site is located in proximity of the N-terminus. Reducing the size of AlgE6 influences the epimerization of modified alginates in solution
additional information
mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it. Construction of thehybrid enzyme AlgE6A with A-module, and the hybrid enzyme AlgE64 constituted by the Amodule from AlgE6 and the R-module from AlgE4, modular structure, overview. The A-module is the minimal size for an active epimerase, even though the active site is located in proximity of the N-terminus. Reducing the size of AlgE6 influences the epimerization of modified alginates in solution
additional information
mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it. Construction of thehybrid enzyme AlgE6A with A-module, and the hybrid enzyme AlgE64 constituted by the Amodule from AlgE6 and the R-module from AlgE4, modular structure, overview. The A-module is the minimal size for an active epimerase, even though the active site is located in proximity of the N-terminus. Reducing the size of AlgE6 influences the epimerization of modified alginates in solution
additional information
mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it. Construction of thehybrid enzyme AlgE6A with A-module, and the hybrid enzyme AlgE64 constituted by the Amodule from AlgE6 and the R-module from AlgE4, modular structure, overview. The A-module is the minimal size for an active epimerase, even though the active site is located in proximity of the N-terminus. Reducing the size of AlgE6 influences the epimerization of modified alginates in solution
additional information
mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it. Construction of thehybrid enzyme AlgE6A with A-module, and the hybrid enzyme AlgE64 constituted by the Amodule from AlgE6 and the R-module from AlgE4, modular structure, overview. The A-module is the minimal size for an active epimerase, even though the active site is located in proximity of the N-terminus. Reducing the size of AlgE6 influences the epimerization of modified alginates in solution
additional information
mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it. Enzyme modular structure, overview
additional information
mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it. Enzyme modular structure, overview
additional information
mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it. Enzyme modular structure, overview
additional information
mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it. Enzyme modular structure, overview
additional information
mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it. Enzyme modular structure, overview
additional information
mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it. Enzyme modular structure, overview
additional information
mannuronan C5-epimerases (AlgE1-AlgE7) produced by Azotobacter vinelandii are able to convert beta-D-mannuronate to its epimer alpha-L-guluronate in alginates. The introduction of new G-blocks into the polymer by in vitro epimerization is a strategy to improve the mechanical properties of alginates as biomaterial. Epimerization is hampered when the substrate is modified or in the gelled state. Reducing the size of the epimerases enables the epimerization of otherwise inaccessible regions in the alginate polymer. Even though the reduction of the size affects the productive binding of epimerases to the substrate, and hence their activity, the smaller epimerases can more freely diffuse into calcium-alginate hydrogel and epimerize it. Enzyme modular structure, overview
