ArticleApplied and environmental microbiology2015
Biochemical Characterization of the Lactobacillus reuteri Glycoside Hydrolase Family 70 GTFB Type of 4,6-α-Glucanotransferase Enzymes That Synthesize Soluble Dietary Starch Fibers.
Article in Applied and environmental microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- 4,6-α-Glucanotransferase: An enzymatic biocatalyst for the modification of starch and starch-food systems.Food chemistry: X · 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
- Optimization of 4,6-α and 4,3-α-Glucanotransferase Production inFoods (Basel, Switzerland) · 2024Article
- Impact of Starch Binding Domain Fusion on Activities and Starch Product Structure of 4-α-Glucanotransferase.Molecules (Basel, Switzerland) · 2023Article
- Insights into Broad-Specificity Starch Modification from the Crystal Structure ofJournal of agricultural and food chemistry · 2021Article
- Development of Slowly Digestible Starch Derived α-Glucans with 4,6-α-Glucanotransferase and Branching Sucrase Enzymes.Journal of agricultural and food chemistry · 2020Article
- In Vitro Fermentation Behavior of Isomalto/Malto-Polysaccharides Using Human Fecal Inoculum Indicates Prebiotic Potential.Molecular nutrition & food research · 2018Article
- 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
- Enhanced Probiotic Potential ofFrontiers in microbiology · 2017Article
- Article
- 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
- Expression of an (Engineered) 4,6-α-Glucanotransferase in Potato Results in Changes in Starch Characteristics.PloS one · 2016Article
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7 authors.
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No grant is acknowledged in the PubMed record.
Abstract
4,6-α-Glucanotransferase (4,6-α-GTase) enzymes, such as GTFB and GTFW of Lactobacillus reuteri strains, constitute a new reaction specificity in glycoside hydrolase family 70 (GH70) and are novel enzymes that convert starch or starch hydrolysates into isomalto/maltopolysaccharides (IMMPs). These IMMPs still have linear chains with some α1→4 linkages but mostly (relatively long) linear chains with α1→6 linkages and are soluble dietary starch fibers. 4,6-α-GTase enzymes and their products have significant potential for industrial applications. Here we report that an N-terminal truncation (amino acids 1 to 733) strongly enhances the soluble expression level of fully active GTFB-ΔN (approximately 75-fold compared to full-length wild type GTFB) in Escherichia coli. In addition, quantitative assays based on amylose V as the substrate are described; these assays allow accurate determination of both hydrolysis (minor) activity (glucose release, reducing power) and total activity (iodine staining) and calculation of the transferase (major) activity of these 4,6-α-GTase enzymes. The data show that GTFB-ΔN is clearly less hydrolytic than GTFW, which is also supported by nuclear magnetic resonance (NMR) analysis of their final products. From these assays, the biochemical properties of GTFB-ΔN were characterized in detail, including determination of kinetic parameters and acceptor substrate specificity. The GTFB enzyme displayed high conversion yields at relatively high substrate concentrations, a promising feature for industrial application.
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