ArticleApplied and environmental microbiology2015
AmyM, a Novel Maltohexaose-Forming α-Amylase from Corallococcus sp. strain EGB.
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 20 papers.
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Who cites it
20 citing papers in PubMed.
- A novel multifunctional starch debranching enzyme from Myxococcus sp. V11.Applied microbiology and biotechnology · 2026Article
- Mechanistic insights into substrate-targeting modification effects on interfacial kinetics of raw starch-degrading amylases.Applied and environmental microbiology · 2026Article
- Cereal biomass-derived xylo- and malto-oligosaccharides as next-generation prebiotics: a comprehensive review of sustainable production and translational benefits for human and animal gut microbiota.Frontiers in microbiology · 2026Review
- Myxobacteria: Versatile cell factories of novel commercial enzymes for bio-manufacturing.Biotechnology advances · 2025Review
- Comparative genomic insight into the myxobacterial carbohydrate-degrading potential.Frontiers in microbiology · 2025Article
- Molecular Cloning, Characterization, and Application of a Novel Multifunctional Isoamylase (MIsA) fromFoods (Basel, Switzerland) · 2024Article
- Heterologous Expression and Characterization of a Novel Mesophilic Maltogenic α-Amylase AmyFlA from Flavobacterium sp. NAU1659.Applied biochemistry and biotechnology · 2024Article
- Secretory CAZymes profile and GH19 enzymes analysis ofFrontiers in microbiology · 2024Article
- Identification and Characterization of Novel Malto-Oligosaccharide-Forming Amylase AmyCf fromFoods (Basel, Switzerland) · 2023Article
- Structural and Functional Properties of Porous Corn Starch Obtained by Treating Raw Starch with AmyM.Foods (Basel, Switzerland) · 2023Article
- Maltooligosaccharides: Properties, Production and Applications.Molecules (Basel, Switzerland) · 2023Review
- Structural and Functional Characterization of a New Bacterial Dipeptidyl Peptidase III Involved in Fruiting Body Formation in Myxobacteria.International journal of molecular sciences · 2022Article
- Article
- Carbohydrate-Binding Module and Linker Allow Cold Adaptation and Salt Tolerance of Maltopentaose-Forming Amylase From Marine BacteriumFrontiers in microbiology · 2021Article
- Article
- Cloning, Expression and Characterization of a Novel α-Amylase from Salinispora arenicola CNP193.The protein journal · 2019Article
- AmyZ1: a novel α-amylase from marine bacteriumBiotechnology for biofuels · 2019Article
- Novel Maltogenic Amylase CoMA from Corallococcus sp. Strain EGB Catalyzes the Conversion of Maltooligosaccharides and Soluble Starch to Maltose.Applied and environmental microbiology · 2018Article
- Functional Analysis of a Novel β-(1,3)-Glucanase from Corallococcus sp. Strain EGB Containing a Fascin-Like Module.Applied and environmental microbiology · 2017Article
- Characterization of the starch-acting MaAmyB enzyme from Microbacterium aurum B8.A representing the novel subfamily GH13_42 with an unusual, multi-domain organization.Scientific reports · 2016Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A novel α-amylase, AmyM, was purified from the culture supernatant of Corallococcus sp. strain EGB. AmyM is a maltohexaose-forming exoamylase with an apparent molecular mass of 43 kDa. Based on the results of matrix-assisted laser desorption ionization-time of flight mass spectrometry and peptide mass fingerprinting of AmyM and by comparison to the genome sequence of Corallococcus coralloides DSM 2259, the AmyM gene was identified and cloned into Escherichia coli. amyM encodes a secretory amylase with a predicted signal peptide of 23 amino acid residues, which showed no significant identity with known and functionally verified amylases. amyM was expressed in E. coli BL21(DE3) cells with a hexahistidine tag. The signal peptide efficiently induced the secretion of mature AmyM in E. coli. Recombinant AmyM (rAmyM) was purified by Ni-nitrilotriacetic acid (NTA) affinity chromatography, with a specific activity of up to 14,000 U/mg. rAmyM was optimally active at 50°C in Tris-HCl buffer (50 mM; pH 7.0) and stable at temperatures of <50°C. rAmyM was stable over a wide range of pH values (from pH 5.0 to 10.0) and highly tolerant to high concentrations of salts, detergents, and various organic solvents. Its activity toward starch was independent of calcium ions. The Km and Vmax of recombinant AmyM for soluble starch were 6.61 mg ml(-1) and 44,301.5 μmol min(-1) mg(-1), respectively. End product analysis showed that maltohexaose accounted for 59.4% of the maltooligosaccharides produced. These characteristics indicate that AmyM has great potential in industrial applications.
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