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The N- terminally truncated glucansucrase GtfA of Lactobacillus reuteri strain 121, belongs to glycosyl hydrolase family GH70. The enzyme synthesizes branched glucans with 57 % α(1→4), and 43 % α(1→6)-glycosidic linkages (reuteran) using sucrose as a substrate.
This product is sold for research use only.
*Activity was measured by following the release of fructose from sucrose. One unit of enzyme activity is defined as the release of 1 μmol of fructose per minute.
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The N- and V-terminally truncated glucansucrase Gtf180 of Lactobacillus reuteri 180, belongs to the glycosyl hydrolase family GH70. Compared to Gtf180-ΔN, Gtf180-ΔN-ΔV is impaired in polysaccharide synthesis. Instead this enzyme produces a large number of oligosaccharides. The enzyme forms α(1→6)- and α(1→3)-glycosidic linkages using sucrose as a substrate.
This product is sold for research use only.
*Activity was measured by following the release of fructose from sucrose. One unit of enzyme activity is defined as the release of 1 μmol of fructose per minute.
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The N-terminally truncated enzyme of Lactobacillus reuteri strain ATCC 55730 (LB BIO) is a hydrolytic reuteransucrase producing a soluble glucan, in which the majority ~79 % of the linkages are of the α(1→4) glucosidic type. This reuteran also contains 21 % α(1→6)- linked glucosyl units, and 4,6-disubstituted α-glucosyl units at the branching points.
This product is sold for research use only.
*Activity was measured by following the release of fructose from sucrose. One unit of enzyme activity is defined as the release of 1 μmol of fructose per minute.
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The N-terminally truncated glucansucrase Gtf180 of Lactobacillus reuteri L940W mutant, belongs to glycosyl hydrolase family GH70. The wild type enzyme synthesizes dextran-like α-glucans containing α(1→6) and α(1→3) glycosidic linkages in presence of sucrose. Instead, the GTF180-ΔN mutant L940W is unable to form (α1→3) linkages in its products. The enzyme synthesizes mainly linear isomalto-oligosaccharides (IMOs) and a minor amount of α-glucans (up to 6.3MDa) using sucrose as a substrate. The products contain α(1→6) glycosidic linkages only. The product size is relatively small compared with the wild type enzyme. Enzyme mutations of Leu940 in domain B significantly changed the linkage specificity, reaction specificity, and activity.
This product is sold for research use only.
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The N-terminally truncated glucansucrase GtfML1 of Lactobacillus reuteri strain ML1, belongs to the glycosyl hydrolase family GH70. The enzyme synthesizes a highly branched mutan-like polymer containing 65 % α(1→3), and 35 % α(1→6) linkages using sucrose as substrate.
This product is sold for research use only.
*Activity was measured by following the release of fructose from sucrose. One unit of enzyme activity is defined as the release of 1 μmol of fructose per minute.
