ArticleMicrobial cell factories2019
Unravelling the diversity of glycoside hydrolase family 13 α-amylases from Lactobacillus plantarum WCFS1.
Article in Microbial cell factories, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 47 citations in OpenAlex.
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- α-Glucosidase-driven metabolism as a potential therapeutic vulnerability inFrontiers in microbiology · 2026Review
- Genomic insights into dominant lactic acid bacteria in spoiled plant-based meat analogues.Current research in food science · 2026Article
- Revisiting the endo and exo mode of action of dextran hydrolyzing enzymes, and their significance for Streptococcus mutans biofilm eradication.World journal of microbiology & biotechnology · 2025Article
- In Vitro Gastrointestinal Digestion ofNutrients · 2025Article
- Genomic Characterisation of Limosilactobacillus fermentum CRL2085 Unveiling Probiotic Traits for Application in Cattle Feed.Environmental microbiology reports · 2025Article
- Metagenomic and Physicochemical Analyses Reveal Microbial Community and Functional Differences Between Three Different Grades of Hongxin Low-Temperature Daqu.Foods (Basel, Switzerland) · 2025Article
- Developing Gut-Healthy Strains for Pets: Probiotic Potential and Genomic Insights of Canine-DerivedMicroorganisms · 2025Article
- Two newly established and mutually related subfamilies GH13_48 and GH13_49 of the α-amylase family GH13.Applied microbiology and biotechnology · 2024Article
- Analyzing Current Trends and Possible Strategies to Improve Sucrose Isomerases' Thermostability.International journal of molecular sciences · 2023Review
- Characterization of an Amylolytic Enzyme from Massilia timonae of the GH13_19 Subfamily with Mixed Maltogenic and CGTase Activity.Applied biochemistry and biotechnology · 2023Article
- Changes in microbial community during hydrolyzed sludge reduction.Frontiers in microbiology · 2023Article
- Comprehensive analysis of the metabolic and genomic features of tannin transforming Lactiplantibacillus plantarum strains.Scientific reports · 2022Article
- Characterization of a novel type of glycogen-degrading amylopullulanase from Lactobacillus crispatus.Applied microbiology and biotechnology · 2022Article
- Modulating Glycoside Hydrolase Activity between Hydrolysis and Transfer Reactions Using an Evolutionary Approach.Molecules (Basel, Switzerland) · 2021Article
- Submerged fermentation improves bioactivity of mulberry fruits and leaves.Chinese herbal medicines · 2021Article
- Aspects and Recent Trends in Microbial α-Amylase: a Review.Applied biochemistry and biotechnology · 2021Review
- Analytical combinations to evaluate the macromolecular composition of extracellular substances (ECS) from Lactobacillus plantarum cell culture media.Analytical and bioanalytical chemistry · 2021Article
- Polyphenol-Mediated Gut Microbiota Modulation: Toward Prebiotics and Further.Frontiers in nutrition · 2021Review
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundα-Amylases specifically catalyse the hydrolysis of the internal α-1, 4-glucosidic linkages of starch. Glycoside hydrolase (GH) family 13 is the main α-amylase family in the carbohydrate-active database. Lactobacillus plantarum WCFS1 possesses eleven proteins included in GH13 family. Among these, proteins annotated as maltose-forming α-amylase (Lp_0179) and maltogenic α-amylase (Lp_2757) were included.
resultsIn this study, Lp_0179 and Lp_2757 L. plantarum α-amylases were structurally and biochemically characterized. Lp_2757 displayed structural features typical of GH13_20 subfamily which were absent in Lp_0179. Genes encoding Lp_0179 (Amy2) and Lp_2757 were cloned and overexpressed in Escherichia coli BL21(DE3). Purified proteins showed high hydrolytic activity on pNP-α-D-maltopyranoside, being the catalytic efficiency of Lp_0179 remarkably higher. In relation to the hydrolysis of starch-related carbohydrates, Lp_0179 only hydrolysed maltopentaose and dextrin, demonstrating that is an exotype glucan hydrolase. However, Lp_2757 was also able to hydrolyze cyclodextrins and other non-cyclic oligo- and polysaccharides, revealing a great preference towards α-1,4-linkages typical of maltogenic amylases.
conclusionsThe substrate range as well as the biochemical properties exhibited by Lp_2757 maltogenic α-amylase suggest that this enzyme could be a very promising enzyme for the hydrolysis of α-1,4 glycosidic linkages present in a broad number of starch-carbohydrates, as well as for the investigation of an hypothetical transglucosylation activity under appropriate reaction conditions.
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