ArticleApplied microbiology and biotechnology2013
4,6-α-Glucanotransferase activity occurs more widespread in Lactobacillus strains and constitutes a separate GH70 subfamily.
Article in Applied microbiology and biotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 71 citations in OpenAlex.
- Enzymatic Modification of Potato Starch: Starch-Acting Enzyme Resources, Structure-Function Relationships and Value-Added Applications.Foods (Basel, Switzerland) · 2026Review
- Characterization and Monitoring of Isomalto/Malto-Polysaccharide Formation by Different 4,6-α-Glucanotransferases.Journal of agricultural and food chemistry · 2025Article
- Screening of 14 Lactic Acid Bacteria for Fermentative Isomalto/Malto-Polysaccharide Synthesis.Journal of agricultural and food chemistry · 2025Article
- Unprecedented Diversity of the Glycoside Hydrolase Family 70: A Comprehensive Analysis of Sequence, Structure, and Function.Journal of agricultural and food chemistry · 2024Article
- Crystal Structure of 4,6-α-Glucanotransferase GtfC-ΔC from ThermophilicJournal of agricultural and food chemistry · 2022Article
- Isolation, characterization and comparative genomics of potentially probiotic Lactiplantibacillus plantarum strains from Indian foods.Scientific reports · 2022Article
- Insights into Broad-Specificity Starch Modification from the Crystal Structure ofJournal of agricultural and food chemistry · 2021Article
- Bacterial α-Glucan and Branching Sucrases from GH70 Family: Discovery, Structure-Function Relationship Studies and Engineering.Microorganisms · 2021Review
- Mining novel starch-converting Glycoside Hydrolase 70 enzymes from the Nestlé Culture Collection genome database: The Lactobacillus reuteri NCC 2613 GtfB.Scientific reports · 2017Article
- 4,3-α-Glucanotransferase, a novel reaction specificity in glycoside hydrolase family 70 and clan GH-H.Scientific reports · 2017Article
- Article
- Enhanced Probiotic Potential ofFrontiers in microbiology · 2017Article
- Structure-function relationships of family GH70 glucansucrase and 4,6-α-glucanotransferase enzymes, and their evolutionary relationships with family GH13 enzymes.Cellular and molecular life sciences : CMLS · 2016Review
- Structural Insights into the Carbohydrate Binding Ability of an α-(1→2) Branching Sucrase from Glycoside Hydrolase Family 70.The Journal of biological chemistry · 2016Article
- Characterization of the First α-(1→3) Branching Sucrases of the GH70 Family.The Journal of biological chemistry · 2016Article
- The Exiguobacterium sibiricum 255-15 GtfC Enzyme Represents a Novel Glycoside Hydrolase 70 Subfamily of 4,6-α-Glucanotransferase Enzymes.Applied and environmental microbiology · 2016Article
- Biochemical Characterization of the Lactobacillus reuteri Glycoside Hydrolase Family 70 GTFB Type of 4,6-α-Glucanotransferase Enzymes That Synthesize Soluble Dietary Starch Fibers.Applied and environmental microbiology · 2015Article
- Characterization of the 4,6-α-glucanotransferase GTFB enzyme of Lactobacillus reuteri 121 isolated from inclusion bodies.BMC biotechnology · 2015Article
- Biopolymers from lactic acid bacteria. Novel applications in foods and beverages.Frontiers in microbiology · 2015Review
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Family 70 glycoside hydrolase glucansucrase enzymes exclusively occur in lactic acid bacteria and synthesize a wide range of α-D-glucan (abbreviated as α-glucan) oligo- and polysaccharides. Of the 47 characterized GH70 enzymes, 46 use sucrose as glucose donor. A single GH70 enzyme was recently found to be inactive with sucrose and to utilize maltooligosaccharides [(1→4)-α-D-glucooligosaccharides] as glucose donor substrates for α-glucan synthesis, acting as a 4,6-α-glucanotransferase (4,6-αGT) enzyme. Here, we report the characterization of two further GH70 4,6-αGT enzymes, i.e., from Lactobacillus reuteri strains DSM 20016 and ML1, which use maltooligosaccharides as glucose donor. Both enzymes cleave α1→4 glycosidic linkages and add the released glucose moieties one by one to the non-reducing end of growing linear α-glucan chains via α1→6 glycosidic linkages (α1→4 to α1→6 transfer activity). In this way, they convert pure maltooligosaccharide substrates into linear α-glucan product mixtures with about 50% α1→6 glycosidic bonds (isomalto/maltooligosaccharides). These new α-glucan products may provide an exciting type of carbohydrate for the food industry. The results show that 4,6-αGTs occur more widespread in family GH70 and can be considered as a GH70 subfamily. Sequence analysis allowed identification of amino acid residues in acceptor substrate binding subsites +1 and +2, differing between GH70 GTF and 4,6-αGT enzymes.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.