2.4.1.5: dextransucrase
This is an abbreviated version!
For detailed information about dextransucrase, go to the full flat file.
Word Map on EC 2.4.1.5
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2.4.1.5
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streptococcus
-
mutans
-
glucosylation
-
glucans
-
leuconostoc
-
dental
-
mesenteroides
-
caries
-
udp-glucose
-
oligosaccharide
-
cariogenic
-
sobrinus
-
glucoside
-
water-insoluble
-
difficile
-
plaque
-
maltose
-
glycosyltransferases
-
serotype
-
saliva
-
tooth
-
sanguis
-
gordonii
-
fructosyltransferase
-
udp-glc
-
monoglucosylated
-
dextranase
-
tcda
-
glucansucrase
-
pellicle
-
salivarius
-
gtases
-
galactosyltransferase
-
saliva-coated
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calnexin
-
viscosus
-
lipid-linked
-
industry
-
food industry
-
aureobasidium
-
oralis
-
pharmacology
-
pseudomembranous
-
medicine
-
3-o-glucoside
-
levansucrase
-
biotechnology
-
alpha-1,6
-
weissella
-
man9glcnac2
-
transglucosylation
-
synthesis
-
glc3man9glcnac2
-
nutrition
-
isomaltose
-
sordellii
-
holotoxins
- 2.4.1.5
- streptococcus
- mutans
-
glucosylation
- glucans
- leuconostoc
-
dental
- mesenteroides
- caries
- udp-glucose
- oligosaccharide
-
cariogenic
- sobrinus
- glucoside
-
water-insoluble
- difficile
- plaque
- maltose
- glycosyltransferases
-
serotype
- saliva
- tooth
- sanguis
- gordonii
- fructosyltransferase
- udp-glc
-
monoglucosylated
- dextranase
- tcda
- glucansucrase
- pellicle
- salivarius
- gtases
-
galactosyltransferase
-
saliva-coated
- calnexin
- viscosus
-
lipid-linked
- industry
- food industry
- aureobasidium
- oralis
- pharmacology
-
pseudomembranous
- medicine
- 3-o-glucoside
- levansucrase
- biotechnology
-
alpha-1,6
- weissella
- man9glcnac2
-
transglucosylation
- synthesis
- glc3man9glcnac2
- nutrition
- isomaltose
- sordellii
-
holotoxins
Reaction
Synonyms
B-512F dextransucrase, B-512FMC dextransucrase, Cab3, CEP, DexT, dextran-sucrase, DS, DSase, DSR, Dsr S protein, DSR-F, DSR-S, DSRB742, DSRBCB4, DSRC39-2, DsrE563, DsrP, DSRS, DSRWC, DsrX, FT045B dextransucrase, glucansucrase, glucosyltransferase, glucosyltransferase, sucrose-1,6-alpha-glucan, glycosyltransferase R, Gtf, Gtf-DSM, GTFR, More, SGE, sucrose 6-glucosyltransferase, sucrose:1, 6-alpha-D-glucan 6-alpha-glucosyltransferase, sucrose:1,6-alpha-D-glucan-6-alpha-D-glucosyltransferase, Wc392-rDSR, WcCab3-DSR
ECTree
2.4.1.5 dextransucraseAdvanced search results
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results (Engineering
Engineering on EC 2.4.1.5 - dextransucrase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A670V
the mutation increases the percentage of alpha(1->3) linkages (9% at most) and decreases the percentage of alpha(1->6) linkages in the product
D530N
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D590A
the mutation introduces a decrease the percentage of alpha(1->3) linkage in the product
D641N
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E568Q
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E664K
the mutation introduces additional alpha(1->3) glycosidic linkages and also some additional alpha(1->2) glycosidic linkages, the mutation decreases the percentage of alpha(1->6) linkages in the product
F196S
-
site-directed mutagenesis, the mutant DRN1 shows a higher expression level in Escherichia coli and increased activity compared to DSRB742
H161R
-
mutant protein retains a very low dextran synthesis activity
K395T
-
site-directed mutagenesis, the mutant DRN3 shows a higher expression level in Escherichia coli and increased activity compared to DSRB742
K955T
activity of the mutant enzyme is similar to activity of wild-type enzyme
N555Y
the mutation increases the percentage of alpha(1->3) linkages (9% at most) and decreases the percentage of alpha(1->6) linkages in the product
P473S/P856S
the mutant enzyme shows a significant increase in thermal inactivation with a 7.4fold increase in half-life at 35°C and a 2fold increase in catalytic efficiency compared with the wild-type. Highest enzymatic activity mutant. Mutant enzyme P478S/P856S is slightly more stable than wild-type enzyme
P980T
-
site-directed mutagenesis, the mutant DRN4 shows a lower expression level in Escherichia coli compared to DSRB742
Q1029K
the mutation has no significant effect on the linkage specificity
Q666R
the mutation introduces a small amount of additional alpha(1->4) glycosidic linkages, the mutation decreases the percentage of alpha(1->6) linkages in the product
S455K
-
produces a glucan with 85% 6-linked glucopyranosyl residues
S663N
the mutation increases the percentage of alpha(1->3) linkages (9% at most) and decreases the percentage of alpha(1->6) linkages in the product
T350K
-
produces a glucan with 85% 6-linked glucopyranosyl residues
T350K/S455K
V553A
the mutation introduces a small amount of additional alpha(1->4) glycosidic linkages, the mutation decreased the production of alpha(1->3) linkage polysaccharides
V556I
the mutation introduces a small amount of additional alpha(1->4) glycosidic linkages, the mutation decreased the production of alpha(1->3) linkage polysaccharides
V665A
the mutation introduces a small amount of additional alpha(1->4) glycosidic linkages, the mutation decreases the percentage of alpha(1->6) linkages in the product
W591G
the mutation introduces a decrease the percentage of alpha(1->3) linkage in the product
Y346N
-
site-directed mutagenesis, the mutant DRN2 shows a lower expression level in Escherichia coli compared to DSRB742
D590A
-
the mutation introduces a decrease the percentage of alpha(1->3) linkage in the product
-
N555Y
-
the mutation increases the percentage of alpha(1->3) linkages (9% at most) and decreases the percentage of alpha(1->6) linkages in the product
-
V553A
-
the mutation introduces a small amount of additional alpha(1->4) glycosidic linkages, the mutation decreased the production of alpha(1->3) linkage polysaccharides
-
V556I
-
the mutation introduces a small amount of additional alpha(1->4) glycosidic linkages, the mutation decreased the production of alpha(1->3) linkage polysaccharides
-
D530N
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
D641N
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
E568Q
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
H161R
-
mutant protein retains a very low dextran synthesis activity
-
S455K
-
produces a glucan with 85% 6-linked glucopyranosyl residues
-
T350K
-
produces a glucan with 85% 6-linked glucopyranosyl residues
-
T350K/S455K
N1134S/N1135E/S1136V
-
mutation converts glucosyltransferase from a mainly alpha-(1,4) (about 45%, reuteran) to a mainly alpha-(1,6) (about 80%, dextran) synthesizing enzyme
P1026V/I1029V/N1134S/N1135E/S1136V
-
mutant enzyme synthesizes an alpha-glucan containing only a very small percentage of alpha-(1,4) glucosidic linkages (about 5%) and a further increased percentage of alpha-(1,6) glucosidic linkages (about 85%)
N1134S/N1135E/S1136V
-
mutation converts glucosyltransferase from a mainly alpha-(1,4) (about 45%, reuteran) to a mainly alpha-(1,6) (about 80%, dextran) synthesizing enzyme
-
P1026V/I1029V/N1134S/N1135E/S1136V
-
mutant enzyme synthesizes an alpha-glucan containing only a very small percentage of alpha-(1,4) glucosidic linkages (about 5%) and a further increased percentage of alpha-(1,6) glucosidic linkages (about 85%)
-
N1134S
-
the mutation in GTFA results in a drastically changed specificity but no major changes in polymer versus oligosaccharide formation
R624G
-
the R624G mutations near the transition state stabilizer is involved in the phenotype which exhibits a drastic switch in regioselectivity from a dextran type with mainly alpha-1,6-glucosidic linkages to a mutant type polymer with predominantly alpha-1,3-glucosidic linkages
R624G/V630I
-
the mutant exhibits a drastic switch in regioselectivity from a dextran type with mainly alpha-1,6-glucosidic linkages to a mutant type polymer with predominantly alpha-1,3-glucosidic linkages, both mutations near the transition state stabilizer, R624G and V630I, are contributing to this alteration
R624G/V630I/D717A
-
the mutant exhibits a drastic switch in regioselectivity from a dextran type with mainly alpha-1,6-glucosidic linkages to a mutant type polymer with predominantly alpha-1,3-glucosidic linkages, both mutations near the transition state stabilizer, R624G and V630I, are contributing to this alteration
S628D
-
saturation mutagenesis, the mutation guides the reaction toward the synthesis of short chain oligosaccharides with a drastically increased yield of 47% isomaltose or 64% leucrose
S628R
-
saturation mutagenesis, the mutation guides the reaction toward the synthesis of short chain oligosaccharides with a drastically increased yield of 47% isomaltose or 64% leucrose
V630I
-
the V630I mutations near the transition state stabilizer is involved in the phenotype which exhibits a drastic switch in regioselectivity from a dextran type with mainly alpha-1,6-glucosidic linkages to a mutant type polymer with predominantly alpha-1,3-glucosidic linkages
additional information
T350K/S455K
-
mutant enzyme exhibits a 10fold increase in glucosyltransferase activity over those of the parental DSRS-His6 and its T350K and S455K mutants
T350K/S455K
-
produces adhesive, water-insoluble glucan with 77% 6-linked glucopyranosyl residues, 8% 3,6-linked glucopyranosyl residues and 4% 2,6-linked glucopyranosyl residues
T350K/S455K
-
mutant enzyme exhibits a 10fold increase in glucosyltransferase activity over those of the parental DSRS-His6 and its T350K and S455K mutants
-
T350K/S455K
-
produces adhesive, water-insoluble glucan with 77% 6-linked glucopyranosyl residues, 8% 3,6-linked glucopyranosyl residues and 4% 2,6-linked glucopyranosyl residues
-
additional information
construction of a truncated active variant DSR-F-DELTASPDELTAGBD of 1251 amino acids, with a molecular mass of 145544 Da, the mutant lacks the sequence encoding signal peptide and a portion of the C-terminal domain, i.e. the glucan binding domain
additional information
-
construction of a truncated active variant DSR-F-DELTASPDELTAGBD of 1251 amino acids, with a molecular mass of 145544 Da, the mutant lacks the sequence encoding signal peptide and a portion of the C-terminal domain, i.e. the glucan binding domain
additional information
-
construction of a truncated active variant DSR-F-DELTASPDELTAGBD of 1251 amino acids, with a molecular mass of 145544 Da, the mutant lacks the sequence encoding signal peptide and a portion of the C-terminal domain, i.e. the glucan binding domain
-
additional information
directed evolution of a B-742CB dextransucrase gene (dsrB742) that elaborates a novel extracellular dextransucrase gene (dsrB742ck) after ultrasoft X-ray irradiation, producing a dextransucrase of increased activity and synthesis of a highly branched dextran
additional information
-
rational deletions of the signal peptide, the beginning of the variable region and the last four repeats of the C-terminal end cause no loss of activity. The new variant successfully purified is remarkably stable. With a kcat of 584 per s, it is the most efficient recombinant glucansucrase described to date. The synthesized polymer possesses more than 95% of alpha-1,6 links, like the dextran produced by the native enzyme
additional information
-
co-immobilization of dextransucrase and dextranase on calcium alginate for the facilitated synthesis of isomalto-oligosaccharides, reaction scheme, method optimization, and modeling, overview
additional information
-
construction of constitutive mutants by chemical mutagenesis using ethyl methane sulfonate in strain Lm M281, overview
additional information
-
construction of engineered enzyme variants for production of isomalto-oligosaccharides and dextrans of controlled molecular weight of about 10-40 kDa in a one-step process, method optimization, overview
additional information
-
construction of fourteen truncated forms of strain NRRL B512-F dextransucrase by N-, C- or N- plus C-terminal domain truncations, dextran binding properties of mutant enzymes, overview
additional information
-
the enzyme is usable in the production of isomaltooligosaccharide, a promising dietary component with prebiotic effect, the long-chain IMOs are preferred to short chain ones owing to the longer persistence in the colon, optimization of synthesis of long-chain IMOs, alteration of the ratio of sucrose to maltose and the amount of each sugar, overview
additional information
-
the partially purified native enzyme from strain PCSIR-4 is immobilized on alginate for application in the production of dextran from sucrose, method optimization, overview
additional information
construction of a fusion enzyme DXSR of dextransucrase, encoded by gene dsrBCB4, and dextranase, encoded by gene dex2, for one-step synthesis of isomalto-oligosaccharides. DXSR shows 150% increased endo-dextranase activity and 98% decreased dextransucrase activity. The engineered recombinant mutant enzyme DXSR, a fusion of dextransucrase and dextranase, produces linear isomalto-oligosaccharides with DP2-DP10 using sucrose as a sole substrate. DXSR gives 30fold higher production of isomalto-oligosaccharides than that of an equal activity mixture of the two enzymes such as dextranase and dextransucrase
additional information
-
construction of a truncated mutant of enzyme B-512F, the mutant shows sigmoidal shaped curves when the initial velocities are plotted against the concentration of added dextran. The increase in the reaction rate and the decrease in the sigmoidal curve with increasing dextran concentrations indicate that dextran binds at a noncatalytic or allosteric site to give a more active enzyme
additional information
-
optimization of culture conditions for high-level lactose-inducible expression of Leuconostoc mesenteroides dextransucrase in recombinant Escherichia coli strain BL 21(DE3), overview. Maximal activity of 60.18 U/ml from a fed-batch culture at 5 g/l lactose, added at an OD600 of 3.0, at 25°C for 7 h
additional information
construction and optimal expression of a fusion enzyme DSXR having dextransucrase and dextranase activities, for optimization of protein expression, response surface methodology is used
additional information
-
generation of diverse mutant enzymes using UV irradiation random mutagensis, mutant screeening, overview. Mutant KIBGE IB-22M20 exhibits 6.75fold increased dextransucrase activity compared to the wild-type enzyme
additional information
-
immobilisation of the enzyme directly on a 27 MHz quartz crystal microbalance, QCM, plate, or on a dextran-acceptor-QCM plate, method evaluation and binding kinetics,overview. The enzymatic activity of DSase is not affected by immobilization, possibly due to the use of a long PEG spacer group. Typical frequency changes of the dextran-immobilized QCM as a function of time in response to the addition of DSase and sucrose substrate in 50 mM acetate buffer pH 5.2, 150 mM NaCl, and 1 mM CaCl2 at 25°C
additional information
construction of two truncated derivative mutants DsrE563DCD2DGBD (DsrE563-1) and DsrE563DCD2DVR (DsrE563-2). Mutant DsrE563-1 with a deletion of 1620 amino acids from the C-terminus, and mutant DsrE563-2 with deletion of 1258 amino acids from the C-terminus and 349 amino acids from the N-terminus, are catalytically active synthesizing less-soluble dextran, mainly containing alpha-1,6 glucosidic linkage, the synthesized less-soluble dextran also has a branched alpha-1,3 linkage. Mutant DsrE563-2 shows 4.5fold higher dextransucrase activity than mutant DsrE563-1 and a higher acceptor reaction efficiency compared to the wild-type enzyme from Leuconostoc mesenteroides strain 512 FMCM when various mono- or disaccharides are used as acceptors
additional information
-
construction of two truncated derivative mutants DsrE563DCD2DGBD (DsrE563-1) and DsrE563DCD2DVR (DsrE563-2). Mutant DsrE563-1 with a deletion of 1620 amino acids from the C-terminus, and mutant DsrE563-2 with deletion of 1258 amino acids from the C-terminus and 349 amino acids from the N-terminus, are catalytically active synthesizing less-soluble dextran, mainly containing alpha-1,6 glucosidic linkage, the synthesized less-soluble dextran also has a branched alpha-1,3 linkage. Mutant DsrE563-2 shows 4.5fold higher dextransucrase activity than mutant DsrE563-1 and a higher acceptor reaction efficiency compared to the wild-type enzyme from Leuconostoc mesenteroides strain 512 FMCM when various mono- or disaccharides are used as acceptors
additional information
screening of diverse mutants of the eight conserved residues that are determined to be important for enzyme activity, overview. Construction of enzyme mutant DSR-S vardel DELTA4N
additional information
a dextransucrase efficient in synthesizing oligosaccharides is designed. The truncation mutant DSR-S1-DELTAA (residues 1-3087 bp) by deleting the 1494 bp fragment of the C-terminal.The mutant enzyme (MW: 110 kDa) loses activity, when sucrose is used as only substrate. After adding an acceptor, DSR-S1-DELTAA is fully activated but with heavily impaired polysaccharide synthesis ability. The enzyme produces a large amount of oligosaccharides. DSR-S1-DELTAA shows transglycosylation for synthesizing more oligosaccharides of lower degree of polymerization (DP) with different acceptors, and it also improves the selection range of dextransucrase acceptor response to acceptors. The enzyme can be applied in glycodiversifcation studies
additional information
DSR-S1-DELTAV (residues 1-1425) and DSR-S2-DELTA(V) (residues 1-1279) are constructed by deleting partial YG repeats of domain V. DSR-S3-DELTA(V) (residues 1-1160), DSR-S-DELTA IV (residues 1-1124), and DSR-S-DELTA(B) (residues 1-1110) are constructed by deleting the relevant fragments from C-terminal ends. The truncation mutant DSR-S1-DELTA(A) (residues 1-1029) is constructed by deleting partial domain A while containing complete conserved Motif regions I. DSR-S2-DELTA(A) (residues 1-1022) is constructed by deleting partial domain A including conserved Motif regions I. DSRS3-DELTA(A) (residues 1-1000) is constructed by deleting more domain A fragment, allowing further investigation of the functions of C-terminal end domain. 102 amino acids of C-terminal end has no effect on dextran synthesis, but it will improve enzyme protein expression by deleting these amino acids. After further deletion, polysaccharidesynthesizing capability of dextransucrase will be inhibited. With the addition of maltose as postreceptors, truncated enzymes undergoes glycosylation reaction and transferred glucosyl from sucrose to acceptor effectively. By deleting the 417 amino acid fragment, its oligosaccharide synthesizing capability significantly increases. This is an effective way to make use of dextransucrase for prebiotic synthesis
additional information
-
DSR-S1-DELTAV (residues 1-1425) and DSR-S2-DELTA(V) (residues 1-1279) are constructed by deleting partial YG repeats of domain V. DSR-S3-DELTA(V) (residues 1-1160), DSR-S-DELTA IV (residues 1-1124), and DSR-S-DELTA(B) (residues 1-1110) are constructed by deleting the relevant fragments from C-terminal ends. The truncation mutant DSR-S1-DELTA(A) (residues 1-1029) is constructed by deleting partial domain A while containing complete conserved Motif regions I. DSR-S2-DELTA(A) (residues 1-1022) is constructed by deleting partial domain A including conserved Motif regions I. DSRS3-DELTA(A) (residues 1-1000) is constructed by deleting more domain A fragment, allowing further investigation of the functions of C-terminal end domain. 102 amino acids of C-terminal end has no effect on dextran synthesis, but it will improve enzyme protein expression by deleting these amino acids. After further deletion, polysaccharidesynthesizing capability of dextransucrase will be inhibited. With the addition of maltose as postreceptors, truncated enzymes undergoes glycosylation reaction and transferred glucosyl from sucrose to acceptor effectively. By deleting the 417 amino acid fragment, its oligosaccharide synthesizing capability significantly increases. This is an effective way to make use of dextransucrase for prebiotic synthesis
additional information
-
mutant dextransucrases are constructed by inserting amino acid into catalytic pocket. The mutant enzymes are constructed by inserting amino acid between A552 and V553 (inserted mutantion motif II, IMII) and D662 and S663 (inserted mutantion motif IV, IMIV). Variants with catalytic activity are screened of library which synthesize high molecular weight alpha-glucans with different proportions of alpha(1-4) linkages ranging from 0 to 52%. Mutant dextransucrases which synthesize hyperbranched dextran are obtained
additional information
-
mutant dextransucrases are constructed by inserting amino acid into catalytic pocket. The mutant enzymes are constructed by inserting amino acid between A552 and V553 (inserted mutantion motif II, IMII) and D662 and S663 (inserted mutantion motif IV, IMIV). Variants with catalytic activity are screened of library which synthesize high molecular weight alpha-glucans with different proportions of alpha(1-4) linkages ranging from 0 to 52%. Mutant dextransucrases which synthesize hyperbranched dextran are obtained
-
additional information
-
optimization of culture conditions for high-level lactose-inducible expression of Leuconostoc mesenteroides dextransucrase in recombinant Escherichia coli strain BL 21(DE3), overview. Maximal activity of 60.18 U/ml from a fed-batch culture at 5 g/l lactose, added at an OD600 of 3.0, at 25°C for 7 h
-
additional information
-
DSR-S1-DELTAV (residues 1-1425) and DSR-S2-DELTA(V) (residues 1-1279) are constructed by deleting partial YG repeats of domain V. DSR-S3-DELTA(V) (residues 1-1160), DSR-S-DELTA IV (residues 1-1124), and DSR-S-DELTA(B) (residues 1-1110) are constructed by deleting the relevant fragments from C-terminal ends. The truncation mutant DSR-S1-DELTA(A) (residues 1-1029) is constructed by deleting partial domain A while containing complete conserved Motif regions I. DSR-S2-DELTA(A) (residues 1-1022) is constructed by deleting partial domain A including conserved Motif regions I. DSRS3-DELTA(A) (residues 1-1000) is constructed by deleting more domain A fragment, allowing further investigation of the functions of C-terminal end domain. 102 amino acids of C-terminal end has no effect on dextran synthesis, but it will improve enzyme protein expression by deleting these amino acids. After further deletion, polysaccharidesynthesizing capability of dextransucrase will be inhibited. With the addition of maltose as postreceptors, truncated enzymes undergoes glycosylation reaction and transferred glucosyl from sucrose to acceptor effectively. By deleting the 417 amino acid fragment, its oligosaccharide synthesizing capability significantly increases. This is an effective way to make use of dextransucrase for prebiotic synthesis
-
additional information
-
a dextransucrase efficient in synthesizing oligosaccharides is designed. The truncation mutant DSR-S1-DELTAA (residues 1-3087 bp) by deleting the 1494 bp fragment of the C-terminal.The mutant enzyme (MW: 110 kDa) loses activity, when sucrose is used as only substrate. After adding an acceptor, DSR-S1-DELTAA is fully activated but with heavily impaired polysaccharide synthesis ability. The enzyme produces a large amount of oligosaccharides. DSR-S1-DELTAA shows transglycosylation for synthesizing more oligosaccharides of lower degree of polymerization (DP) with different acceptors, and it also improves the selection range of dextransucrase acceptor response to acceptors. The enzyme can be applied in glycodiversifcation studies
-
additional information
-
construction of two truncated derivative mutants DsrE563DCD2DGBD (DsrE563-1) and DsrE563DCD2DVR (DsrE563-2). Mutant DsrE563-1 with a deletion of 1620 amino acids from the C-terminus, and mutant DsrE563-2 with deletion of 1258 amino acids from the C-terminus and 349 amino acids from the N-terminus, are catalytically active synthesizing less-soluble dextran, mainly containing alpha-1,6 glucosidic linkage, the synthesized less-soluble dextran also has a branched alpha-1,3 linkage. Mutant DsrE563-2 shows 4.5fold higher dextransucrase activity than mutant DsrE563-1 and a higher acceptor reaction efficiency compared to the wild-type enzyme from Leuconostoc mesenteroides strain 512 FMCM when various mono- or disaccharides are used as acceptors
-
additional information
-
construction of a fusion enzyme DXSR of dextransucrase, encoded by gene dsrBCB4, and dextranase, encoded by gene dex2, for one-step synthesis of isomalto-oligosaccharides. DXSR shows 150% increased endo-dextranase activity and 98% decreased dextransucrase activity. The engineered recombinant mutant enzyme DXSR, a fusion of dextransucrase and dextranase, produces linear isomalto-oligosaccharides with DP2-DP10 using sucrose as a sole substrate. DXSR gives 30fold higher production of isomalto-oligosaccharides than that of an equal activity mixture of the two enzymes such as dextranase and dextransucrase
-
additional information
-
the enzyme is usable in the production of isomaltooligosaccharide, a promising dietary component with prebiotic effect, the long-chain IMOs are preferred to short chain ones owing to the longer persistence in the colon, optimization of synthesis of long-chain IMOs, alteration of the ratio of sucrose to maltose and the amount of each sugar, overview
-
additional information
-
construction of a truncated mutant of enzyme B-512F, the mutant shows sigmoidal shaped curves when the initial velocities are plotted against the concentration of added dextran. The increase in the reaction rate and the decrease in the sigmoidal curve with increasing dextran concentrations indicate that dextran binds at a noncatalytic or allosteric site to give a more active enzyme
-
additional information
-
generation of diverse mutant enzymes using UV irradiation random mutagensis, mutant screeening, overview. Mutant KIBGE IB-22M20 exhibits 6.75fold increased dextransucrase activity compared to the wild-type enzyme
-
additional information
-
construction of constitutive mutants by chemical mutagenesis using ethyl methane sulfonate in strain Lm M281, overview
-
additional information
-
co-immobilization of dextransucrase and dextranase on calcium alginate for the facilitated synthesis of isomalto-oligosaccharides, reaction scheme, method optimization, and modeling, overview
-
additional information
-
construction of engineered enzyme variants for production of isomalto-oligosaccharides and dextrans of controlled molecular weight of about 10-40 kDa in a one-step process, method optimization, overview
-
additional information
-
rational deletions of the signal peptide, the beginning of the variable region and the last four repeats of the C-terminal end cause no loss of activity. The new variant successfully purified is remarkably stable. With a kcat of 584 per s, it is the most efficient recombinant glucansucrase described to date. The synthesized polymer possesses more than 95% of alpha-1,6 links, like the dextran produced by the native enzyme
-
additional information
-
screening of diverse mutants of the eight conserved residues that are determined to be important for enzyme activity, overview. Construction of enzyme mutant DSR-S vardel DELTA4N
-
additional information
-
construction of fourteen truncated forms of strain NRRL B512-F dextransucrase by N-, C- or N- plus C-terminal domain truncations, dextran binding properties of mutant enzymes, overview
-
additional information
-
the partially purified native enzyme from strain PCSIR-4 is immobilized on alginate for application in the production of dextran from sucrose, method optimization, overview
-
additional information
-
usage of two different artificial intelligence techniques, artificial neural network and genetic algorithm, for optimizing fermentation medium for the production of glucansucrase resulting in production of 6.75 U/ml, method development, overview
additional information
-
usage of two different artificial intelligence techniques, artificial neural network and genetic algorithm, for optimizing fermentation medium for the production of glucansucrase resulting in production of 6.75 U/ml, method development, overview
-
additional information
-
random mutagenesis of the most conserved motif around the transition state stabilizer in glucansucrase GTFR of Streptococcus oralis, yielding different variants with altered reaction specificity, generation of a mutant gtfR library, overview
additional information
-
co-immobilization of the enzyme with dextranase, EC 3.2.1.11, on calcium alginate, optimization of isomalto-oligosacchrides by the system, overview
