2.4.1.B34: 4,6-alpha-glucanotransferase
This is an abbreviated version!
For detailed information about 4,6-alpha-glucanotransferase, go to the full flat file.
Reaction
The enzyme uses maltooligosaccharides as donor and acceptor substrates. It cleaves alpha1->4 glucosidic bonds and synthesizes 1->6 and 1->4 glucosidic linkages. =
Synonyms
4, 6-alpha-glucanotransferase, 4,6-alpha-GT, 4,6-alpha-GTase, Achr_35950, Exig_2648, GflML4, Gtf106b, GtfB, GTFB protein, GTFB-like 4,6-alpha-glucanotransferase, GtfB-like 4,6-alpha-glucanotransferases, GTFB-like 4,6-alpha-GT, GTFC, GTFC-like 4,6-alpha-glucanotransferase, GTFC-like 4,6-alpha-GT, GtfD, GtfML4, GtfW, GtfX, GtfY, Lreu_1346, UDP-N-acetylglucosamine-peptide N-acetylglucosaminyltransferase stabilizing protein
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2.4.1.B34 4,6-alpha-glucanotransferaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 2.4.1.B34 - 4,6-alpha-glucanotransferase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
amylose V + maltose
maltotriose + maltotetraose + ?
-
-
-
?
maltodextrin + H2O
?
i.e. short-chain alpha1->4-linked maltodextrins
-
-
?
maltoheptaose + H2O
D-glucose + maltotriose + maltohexaose
-
first clear products of the reaction
-
?
maltohexaose + H2O
D-glucose + maltopentaose
-
first clear reaction products accumulating after 1 h, longer incubation leads to 4-substituted, 6-substituted, and terminal glucose residues at a molar ratio of 63, 17, and 20%
-
?
maltopentaose + H2O
D-glucose + maltotetraose
-
first clear reaction products accumulating after 1 h, longer incubation leads to 4-substituted, 6-substituted, and terminal glucose residues at a molar ratio of 63, 17, and 20%
-
?
amylose + maltose
maltotriose + panose
the enzyme synthesizes larger saccharides with alpha1->4 and alpha1->6 glucosidic linkages
panose i.e. Glc-alpha-(1->6)-maltose
-
?
amylose + maltose
maltotriose + panose
-
the enzyme synthesizes larger saccharides with alpha1->4 and alpha1->6 glucosidic linkages
panose i.e. Glc-alpha-(1->6)-maltose
-
?
amylose V
?
-
GtfB produces a high molecular mass polymer with a molecular mass about 80 times greater than that of the starting amylose V
-
?
amylose V + H2O
?
-
both hydrolysis and transferase activities occur. Besides the presence of alpha1->4 linkages, alpha1->6 linkages are newly formed. In the product mixture derived from amylose V, the alpha1->6/alpha1->4 linkage ratio increases up to 90:10. In the product mixture, free glucose, 4-substituted reducing glucose residues [-(1->4)-alpha-D-Glc], and a small amount of reducing-end glucose residues which are 6 substituted are detected
-
?
amylose V + H2O
?
hydrolytic activity, amylose V with Mw 170 kDa
-
-
?
amylose V + H2O
?
hydrolytic activity, amylose V with Mw 170 kDa
-
-
?
amylose V + maltose
?
transglycosylation activity, amylose V with 170 kDa
-
-
?
amylose V + maltose
?
transglycosylation activity, amylose V with 170 kDa
-
-
?
Maltoheptaose
?
the enzyme synthesize oligosaccharides up to a degree of polymerization of at least 14. The enzyme introduces 1->6 glucosidic linkages (18%) into the final mixture of products
-
-
?
Maltoheptaose
?
-
the enzyme synthesize oligosaccharides up to a degree of polymerization of at least 14. The enzyme introduces 1->6 glucosidic linkages (18%) into the final mixture of products
-
-
?
maltooligosaccharide
?
the enzyme uses maltooligosaccharides as donor and acceptor substrates. The enzyme disproportionates (cleaves 1->4 and synthesizes 1->6 and 1->4 glucosidic linkages) and 1->6 polymerizes maltotetraose and larger maltooligosaccharide substrates. Only linear products are made and that with increasing degrees of polymerization, more 1->6 glucosidic linkages are introduced into the final products
-
-
?
maltooligosaccharide
?
-
the enzyme uses maltooligosaccharides as donor and acceptor substrates. The enzyme disproportionates (cleaves 1->4 and synthesizes 1->6 and 1->4 glucosidic linkages) and 1->6 polymerizes maltotetraose and larger maltooligosaccharide substrates. Only linear products are made and that with increasing degrees of polymerization, more 1->6 glucosidic linkages are introduced into the final products
-
-
?
maltotetraose + H2O
D-glucose + maltotetraose
-
first clear products of the reaction. The enzyme is rather hydrolytic at the start of the reaction. When reaction products start to accumulate, transglycosylation becomes more efficient
-
?
maltotetraose + H2O
D-glucose + maltotetraose
-
first clear products of the reaction. The enzyme is rather hydrolytic at the start of the reaction. When reaction products start to accumulate, transglycosylation becomes more efficient
-
?
additional information
?
-
GtfD shows clear hydrolase/transglycosylase activity with malto-oligosaccharides with degree of polymerzation of 3 to 7 and forms a range of shorter and longer oligosaccharides. The enzyme is unable to synthesize consecutive alpha1->6 glucosidic bonds. Instead, it forms a high molecular mass and branched alpha-glucan with alternating alpha1->4 and alpha1->6 linkages from amylose/starch
-
-
?
additional information
?
-
inactive on sucrose, panose, nigerose, beta-cyclodextrins, and isomalto-oligosaccharides with degree of polymerzation of 2, 3, and 5
-
-
?
additional information
?
-
GtfD shows clear hydrolase/transglycosylase activity with malto-oligosaccharides with degree of polymerzation of 3 to 7 and forms a range of shorter and longer oligosaccharides. The enzyme is unable to synthesize consecutive alpha1->6 glucosidic bonds. Instead, it forms a high molecular mass and branched alpha-glucan with alternating alpha1->4 and alpha1->6 linkages from amylose/starch
-
-
?
additional information
?
-
inactive on sucrose, panose, nigerose, beta-cyclodextrins, and isomalto-oligosaccharides with degree of polymerzation of 2, 3, and 5
-
-
?
additional information
?
-
-
similar to the GTFBlike 4,6-alpha-GTs, GTFC catalyzes cleavage of alpha(1->4) glycosidic linkages and synthesis of consecutive alpha(1->6) linkages. GTFC differs from GTFB in converting amylose/starch substrates into isomalto-/malto-oligosaccharides (IMMO), instead of the (modified) polymers (IMMP) synthesized by GTFB
-
-
-
additional information
?
-
GtfC acts on maltooligosaccharides and amylose-V yielding linear gluco-oligomers also containing, besides alpha1->4, alpha1->6 glycosidic linkages. In the product mixture, free glucose units, 4-substituted reducing-end glucose residues and trace amounts of 6-substituted reducing-end glucose residues are present. The higher the degree of polymerization of the substrate, the higher the percentages of alpha1->6 glycosidic linkages introduced into the product. No substrates: maltose, maltotriose, sucrose, nigerose, isomaltooliogosaccharides, panose, reuteran
-
-
?
additional information
?
-
-
similar to the GTFBlike 4,6-alpha-GTs, GTFC catalyzes cleavage of alpha(1->4) glycosidic linkages and synthesis of consecutive alpha(1->6) linkages. GTFC differs from GTFB in converting amylose/starch substrates into isomalto-/malto-oligosaccharides (IMMO), instead of the (modified) polymers (IMMP) synthesized by GTFB
-
-
-
additional information
?
-
-
similar to the GTFBlike 4,6-alpha-GTs, GTFC catalyzes cleavage of alpha(1->4) glycosidic linkages and synthesis of consecutive alpha(1->6) linkages. GTFC differs from GTFB in converting amylose/starch substrates into isomalto-/malto-oligosaccharides (IMMO), instead of the (modified) polymers (IMMP) synthesized by GTFB
-
-
-
additional information
?
-
GtfC acts on maltooligosaccharides and amylose-V yielding linear gluco-oligomers also containing, besides alpha1->4, alpha1->6 glycosidic linkages. In the product mixture, free glucose units, 4-substituted reducing-end glucose residues and trace amounts of 6-substituted reducing-end glucose residues are present. The higher the degree of polymerization of the substrate, the higher the percentages of alpha1->6 glycosidic linkages introduced into the product. No substrates: maltose, maltotriose, sucrose, nigerose, isomaltooliogosaccharides, panose, reuteran
-
-
?
additional information
?
-
-
similar to the GTFBlike 4,6-alpha-GTs, GTFC catalyzes cleavage of alpha(1->4) glycosidic linkages and synthesis of consecutive alpha(1->6) linkages. GTFC differs from GTFB in converting amylose/starch substrates into isomalto-/malto-oligosaccharides (IMMO), instead of the (modified) polymers (IMMP) synthesized by GTFB
-
-
-
additional information
?
-
-
GTFB predominantly cleaves an alpha(1->4) glycosidic linkage from the non-reducing end of the donor substrate [alpha(1->4)-glucan] and transfers the cleaved glucosyl unit to the non-reducing end of another alpha(1->4)-glucan acceptor substrate, forming mainly alpha(1->6) linkages. Products formed with an alpha(1->6) linkage at the non-reducing end become better acceptor substrates and are further elongated in a linear manner with alpha(1->6) linked glucosyl units. This results in the formation of isomalto/malto-oligosaccharide and polysaccharide mixtures with increasing percentages of alpha(1->6) linkages. Linkage specificity of GTFB-like 4,6-alpha-GTs, overview
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additional information
?
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mutant GtfX-DELTANDELTAC is inactive on sucrose, panose, nigerose, isomaltose, isomaltotriose, maltose, maltotriose, alpha-cyclodextrin, pullulan and dextran, but shows clear hydrolase/transglycosylase activity on malto-oligosaccharides (MOS) of DP4-7, amylose V, starch, and amylopectin. Substrate specificity of mutant GtfX-DELTANDELTAC, 1HNMR analysis product analysis, and structural analysis of polysaccharides generated by GtfX-DELTANDELTAC from amylose V, overview
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additional information
?
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mutant GtfY-DELTANDELTAC is inactive on sucrose, panose, nigerose, isomaltose, isomaltotriose, maltose, maltotriose, alpha-cyclodextrin, pullulan and dextran, but shows clear hydrolase/transglycosylase activity on malto-oligosaccharides (MOS) of DP4-7, amylose V, starch, and amylopectin. Substrate specificity of mutant GtfY-DELTANDELTAC, 1HNMR analysis product analysis, and structural analysis of polysaccharides generated by GtfY-DELTANDELTAC from amylose V, overview
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additional information
?
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mutant GtfX-DELTANDELTAC is inactive on sucrose, panose, nigerose, isomaltose, isomaltotriose, maltose, maltotriose, alpha-cyclodextrin, pullulan and dextran, but shows clear hydrolase/transglycosylase activity on malto-oligosaccharides (MOS) of DP4-7, amylose V, starch, and amylopectin. Substrate specificity of mutant GtfX-DELTANDELTAC, 1HNMR analysis product analysis, and structural analysis of polysaccharides generated by GtfX-DELTANDELTAC from amylose V, overview
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additional information
?
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mutant GtfY-DELTANDELTAC is inactive on sucrose, panose, nigerose, isomaltose, isomaltotriose, maltose, maltotriose, alpha-cyclodextrin, pullulan and dextran, but shows clear hydrolase/transglycosylase activity on malto-oligosaccharides (MOS) of DP4-7, amylose V, starch, and amylopectin. Substrate specificity of mutant GtfY-DELTANDELTAC, 1HNMR analysis product analysis, and structural analysis of polysaccharides generated by GtfY-DELTANDELTAC from amylose V, overview
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-
additional information
?
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-
the enzyme is unable to use sucrose as a donor substrate and is inactive with the sucrose analogs turanose and palatinose, with raffinose, with the DP5 and DP6 isomaltooligosaccharides and with panose
-
-
?
additional information
?
-
the enzyme is unable to use sucrose as a donor substrate and is inactive with the sucrose analogs turanose and palatinose, with raffinose, with the DP5 and DP6 isomaltooligosaccharides and with panose
-
-
?
additional information
?
-
enzyme cleaves alpha1->4 glycosidic linkages and adds the released glucose moieties one by one to the non-reducing end of growing linear alpha-glucan chains via alpha1->6 glycosidic linkages (alpha1->4 to alpha1->6 transfer activity). It converts pure maltooligosaccharide substrates into linear alpha-glucan product mixtures with about 50% alpha1->6 glycosidic bonds (isomalto/maltooligosaccharides). Largest products synthesized from maltoheptaose have a degree of polymerizatition bleow 50
-
-
?
additional information
?
-
enzyme cleaves alpha1->4 glycosidic linkages and adds the released glucose moieties one by one to the non-reducing end of growing linear alpha-glucan chains via alpha1->6 glycosidic linkages (alpha1->4 to alpha1->6 transfer activity). It converts pure maltooligosaccharide substrates into linear alpha-glucan product mixtures with about 50% alpha1->6 glycosidic bonds (isomalto/maltooligosaccharides). Largest products synthesized from maltoheptaose have a degree of polymerizatition bleow 50
-
-
?
additional information
?
-
-
enzyme is a alpha-glucanotransferase enzyme with disproportionating (cleaving alpha1->4 and synthesizing alpha1->6 and alpha1->4 glycosidic linkages) and alpha1->6 polymerizing types of activity on maltotetraose and larger maltooligosaccharide substrates. Only linear products are made and with increasing degrees of polymerization, more alpha1->6 glycosidic linkages are introduced into the final products, ranging from 18% in the incubation mixture to 33% in an enriched fraction. In view of its primary structure, GTFB is a member of the glycoside hydrolase 70 family. The GTFB enzyme reaction and product specificities, however, resemble those of the GH13 alpha-amylase type of enzymes
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?
additional information
?
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enzyme is a alpha-glucanotransferase enzyme with disproportionating (cleaving alpha1->4 and synthesizing alpha1->6 and alpha1->4 glycosidic linkages) and alpha1->6 polymerizing types of activity on maltotetraose and larger maltooligosaccharide substrates. Only linear products are made and with increasing degrees of polymerization, more alpha1->6 glycosidic linkages are introduced into the final products, ranging from 18% in the incubation mixture to 33% in an enriched fraction. In view of its primary structure, GTFB is a member of the glycoside hydrolase 70 family. The GTFB enzyme reaction and product specificities, however, resemble those of the GH13 alpha-amylase type of enzymes
-
-
?
additional information
?
-
-
no substrates: maltose, maltotriose, sucrose, turanose and palatinose, raffinose, panose, DP5 and DP6 isomaltooligosaccharides
-
-
?
additional information
?
-
no substrates: maltose, maltotriose, sucrose, turanose and palatinose, raffinose, panose, DP5 and DP6 isomaltooligosaccharides
-
-
?
additional information
?
-
-
GTFB predominantly cleaves an alpha(1->4) glycosidic linkage from the non-reducing end of the donor substrate [alpha(1->4)-glucan] and transfers the cleaved glucosyl unit to the non-reducing end of another alpha(1->4)-glucan acceptor substrate, forming mainly alpha(1->6) linkages. Products formed with an alpha(1->6) linkage at the non-reducing end become better acceptor substrates and are further elongated in a linear manner with alpha(1->6) linked glucosyl units. This results in the formation of isomalto/malto-oligosaccharide and polysaccharide mixtures with increasing percentages of alpha(1->6) linkages. Linkage specificity of GTFB-like 4,6-alpha-GTs, overview
-
-
-
additional information
?
-
malto-oligosaccharide binding structures with wild-type and mutant enzymes, overview
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-
-
additional information
?
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-
structure of the IMMP product of 4,6-alpha-GTase (e.g. GtfB) with maltodextrins, overview. NMR analysis of EPS samples produced by the GtfB enzyme in vitro and by Lactobacillus reuteri 121 cells in vivo. Enzyme reaction product analysis
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additional information
?
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structure of the IMMP product of 4,6-alpha-GTase (e.g. GtfB) with maltodextrins, overview. NMR analysis of EPS samples produced by the GtfB enzyme in vitro and by Lactobacillus reuteri 121 cells in vivo. Enzyme reaction product analysis
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additional information
?
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structure of the IMMP product of 4,6-alpha-GTase Gtf106b with maltodextrins, overview. Enzyme reaction product analysis
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additional information
?
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structure of the IMMP product of 4,6-alpha-GTase Gtf106b with maltodextrins, overview. Enzyme reaction product analysis
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additional information
?
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structure of the IMMP product of 4,6-alpha-GTase GtfML4 with maltodextrins, overview. Enzyme reaction product analysis
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additional information
?
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structure of the IMMP product of 4,6-alpha-GTase GtfML4 with maltodextrins, overview. Enzyme reaction product analysis
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additional information
?
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structure of the IMMP product of 4,6-alpha-GTase GtfW with maltodextrins, overview. Enzyme reaction product analysis
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additional information
?
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structure of the IMMP product of 4,6-alpha-GTase GtfW with maltodextrins, overview. Enzyme reaction product analysis
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additional information
?
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the enzyme performs transglycosylation and/or hydrolytic activity. The linear alpha(1->4)-linked glucose units disappear and linear alpha(1->6)-linked glucose units appear. The total enzyme activity of GtfB-DELTAN-DELTAV is determined by the amylose-iodine staining method. Synthesis of isomalto/malto-polysaccharides (IMMP) from starch. Reaction product analyses, the IMMP product consists of terminal, and 6-substituted glucosyl units, overview. IMMP with 18.3 kDa
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additional information
?
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GTFB predominantly cleaves an alpha(1->4) glycosidic linkage from the non-reducing end of the donor substrate [alpha(1->4)-glucan] and transfers the cleaved glucosyl unit to the non-reducing end of another alpha(1->4)-glucan acceptor substrate, forming mainly alpha(1->6) linkages. Products formed with an alpha(1->6) linkage at the non-reducing end become better acceptor substrates and are further elongated in a linear manner with alpha(1->6) linked glucosyl units. This results in the formation of isomalto/malto-oligosaccharide and polysaccharide mixtures with increasing percentages of alpha(1->6) linkages. Linkage specificity of GTFB-like 4,6-alpha-GTs, overview
-
-
-
additional information
?
-
structure of the IMMP product of 4,6-alpha-GTase (e.g. GtfB) with maltodextrins, overview. NMR analysis of EPS samples produced by the GtfB enzyme in vitro and by Lactobacillus reuteri 121 cells in vivo. Enzyme reaction product analysis
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additional information
?
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the enzyme performs transglycosylation and/or hydrolytic activity. The linear alpha(1->4)-linked glucose units disappear and linear alpha(1->6)-linked glucose units appear. The total enzyme activity of GtfB-DELTAN-DELTAV is determined by the amylose-iodine staining method. Synthesis of isomalto/malto-polysaccharides (IMMP) from starch. Reaction product analyses, the IMMP product consists of terminal, and 6-substituted glucosyl units, overview. IMMP with 18.3 kDa
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additional information
?
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malto-oligosaccharide binding structures with wild-type and mutant enzymes, overview
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additional information
?
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the enzyme is unable to use sucrose as a donor substrate and is inactive with the sucrose analogs turanose and palatinose, with raffinose, with the DP5 and DP6 isomaltooligosaccharides and with panose
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-
?
additional information
?
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-
GTFB predominantly cleaves an alpha(1->4) glycosidic linkage from the non-reducing end of the donor substrate [alpha(1->4)-glucan] and transfers the cleaved glucosyl unit to the non-reducing end of another alpha(1->4)-glucan acceptor substrate, forming mainly alpha(1->6) linkages. Products formed with an alpha(1->6) linkage at the non-reducing end become better acceptor substrates and are further elongated in a linear manner with alpha(1->6) linked glucosyl units. This results in the formation of isomalto/malto-oligosaccharide and polysaccharide mixtures with increasing percentages of alpha(1->6) linkages. Linkage specificity of GTFB-like 4,6-alpha-GTs, overview
-
-
-
additional information
?
-
enzyme cleaves alpha1->4 glycosidic linkages and adds the released glucose moieties one by one to the non-reducing end of growing linear alpha-glucan chains via alpha1->6 glycosidic linkages (alpha1->4 to alpha1->6 transfer activity). It converts pure maltooligosaccharide substrates into linear alpha-glucan product mixtures with about 50% alpha1->6 glycosidic bonds (isomalto/maltooligosaccharides). Largest products synthesized from maltoheptaose have a degree of polymerizatition bleow 50
-
-
?
additional information
?
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structure of the IMMP product of 4,6-alpha-GTase Gtf106b with maltodextrins, overview. Enzyme reaction product analysis
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additional information
?
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structure of the IMMP product of 4,6-alpha-GTase GtfML4 with maltodextrins, overview. Enzyme reaction product analysis
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additional information
?
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structure of the IMMP product of 4,6-alpha-GTase GtfW with maltodextrins, overview. Enzyme reaction product analysis
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additional information
?
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Limosilactobacillus reuteri LMG 18388
structure of the IMMP product of 4,6-alpha-GTase (e.g. GtfB) with maltodextrins, overview. NMR analysis of EPS samples produced by the GtfB enzyme in vitro and by Lactobacillus reuteri 121 cells in vivo. Enzyme reaction product analysis
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additional information
?
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GTFB predominantly cleaves an alpha(1->4) glycosidic linkage from the non-reducing end of the donor substrate [alpha(1->4)-glucan] and transfers the cleaved glucosyl unit to the non-reducing end of another alpha(1->4)-glucan acceptor substrate, forming mainly alpha(1->6) linkages. Products formed with an alpha(1->6) linkage at the non-reducing end become better acceptor substrates and are further elongated in a linear manner with alpha(1->6) linked glucosyl units. This results in the formation of isomalto/malto-oligosaccharide and polysaccharide mixtures with increasing percentages of alpha(1->6) linkages. Linkage specificity of GTFB-like 4,6-alpha-GTs, overview
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additional information
?
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structure of the IMMP product of 4,6-alpha-GTase Gtf106b with maltodextrins, overview. Enzyme reaction product analysis
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additional information
?
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structure of the IMMP product of 4,6-alpha-GTase GtfML4 with maltodextrins, overview. Enzyme reaction product analysis
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additional information
?
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structure of the IMMP product of 4,6-alpha-GTase GtfW with maltodextrins, overview. Enzyme reaction product analysis
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additional information
?
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enzyme cleaves alpha1->4 glycosidic linkages and adds the released glucose moieties one by one to the non-reducing end of growing linear alpha-glucan chains via alpha1->6 glycosidic linkages (alpha1->4 to alpha1->6 transfer activity). It converts pure maltooligosaccharide substrates into linear alpha-glucan product mixtures with about 50% alpha1->6 glycosidic bonds (isomalto/maltooligosaccharides). Largest products synthesized from maltoheptaose have a degree of polymerizatition bleow 50
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?
additional information
?
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Limosilactobacillus reuteri TMW1.106
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structure of the IMMP product of 4,6-alpha-GTase Gtf106b with maltodextrins, overview. Enzyme reaction product analysis
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additional information
?
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Limosilactobacillus reuteri TMW1.106
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structure of the IMMP product of 4,6-alpha-GTase GtfML4 with maltodextrins, overview. Enzyme reaction product analysis
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additional information
?
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Limosilactobacillus reuteri TMW1.106
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structure of the IMMP product of 4,6-alpha-GTase GtfW with maltodextrins, overview. Enzyme reaction product analysis
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additional information
?
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the enzyme GtfD shows both hydrolysis and transglycosylase (disproportionation) activity. 1HNMR analysis of the product mixture generated from amylose V reveals the presence of two broad anomeric signals corresponding to the (alpha1->4) and the newly formed (alpha1->6) linkages. Substrate specificity with maltooligosaccharides, overview. The Paenibacillus beijingensis GtfD enzyme is inactive on sucrose, panose, nigerose, and isomalto-oligosaccharides with DP2, DP3, and DP5, while the enzyme catalyzes the conversion of malto-oligosaccharides (MOS) of DP3 to 7 showing both hydrolysis and transglycosylase (disproportionation) activity revealing the formation of lower- and higher-molecular-mass products
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additional information
?
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the enzyme GtfD shows both hydrolysis and transglycosylase (disproportionation) activity. 1HNMR analysis of the product mixture generated from amylose V reveals the presence of two broad anomeric signals corresponding to the (alpha1->4) and the newly formed (alpha1->6) linkages. Substrate specificity with maltooligosaccharides, overview. The Paenibacillus beijingensis GtfD enzyme is inactive on sucrose, panose, nigerose, and isomalto-oligosaccharides with DP2, DP3, and DP5, while the enzyme catalyzes the conversion of malto-oligosaccharides (MOS) of DP3 to 7 showing both hydrolysis and transglycosylase (disproportionation) activity revealing the formation of lower- and higher-molecular-mass products
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additional information
?
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GTFB predominantly cleaves an alpha(1->4) glycosidic linkage from the non-reducing end of the donor substrate [alpha(1->4)-glucan] and transfers the cleaved glucosyl unit to the non-reducing end of another alpha(1->4)-glucan acceptor substrate, forming mainly alpha(1->6) linkages. Products formed with an alpha(1->6) linkage at the non-reducing end become better acceptor substrates and are further elongated in a linear manner with alpha(1-> 6) linked glucosyl units. This results in the formation of isomalto/malto-oligosaccharide and polysaccharide mixtures with increasing percentages of alpha(1->6) linkages. Linkage specificity of GTFB-like 4,6-alpha-GTs, overview
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additional information
?
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purified recombinant truncated GtfB shows transglycosylation activities toward starch, resulting in branch points of alpha(1->6)-glycosidic linkages plus linear chains of alpha(1->4)-glycosidic linkages. GtfB catalyzes the transglycosylation reactions of amylose through cleaving alpha(1->4)-glycosidic linkage and synthesizing alpha(1->6)-glycosidic linkages. Usage of modified wheat starch, after the GtfB-modified wheat starches are gelatinized and stored at 4°C for 1-2 weeks, their endothermic enthalpies are significantly lower than that of the control sample, indicating low retrogradation rates. The GtfB-treated amylose is significantly different from the GtfB-untreated amylose, with more short-branch chains (DP1-4) of alpha(1->4)-glycosidic linkages. Amylose and amylopectin contents of natural and GtfB modified wheat starches, and conformational structure of GtfB-modified wheat starch, overview
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additional information
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Streptococcus thermophilus NCC2408
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purified recombinant truncated GtfB shows transglycosylation activities toward starch, resulting in branch points of alpha(1->6)-glycosidic linkages plus linear chains of alpha(1->4)-glycosidic linkages. GtfB catalyzes the transglycosylation reactions of amylose through cleaving alpha(1->4)-glycosidic linkage and synthesizing alpha(1->6)-glycosidic linkages. Usage of modified wheat starch, after the GtfB-modified wheat starches are gelatinized and stored at 4°C for 1-2 weeks, their endothermic enthalpies are significantly lower than that of the control sample, indicating low retrogradation rates. The GtfB-treated amylose is significantly different from the GtfB-untreated amylose, with more short-branch chains (DP1-4) of alpha(1->4)-glycosidic linkages. Amylose and amylopectin contents of natural and GtfB modified wheat starches, and conformational structure of GtfB-modified wheat starch, overview
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