Recombinant Expression and Characterization of a New Endogenous and Halophilic GH13_5 Subfamily α-Amylase from Paenibacillus pabuli.

Karina Lima Dos Reis, Ione Parra Barbosa-Tessmann

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Article in Applied biochemistry and biotechnology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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2 authors.

Karina Lima Dos ReisBiochemistry Department, Biological Sciences Center, State University of Maringá, Av. Colombo, 5790, Maringá, Paraná, 87020-900, Brazil.ORCID http://orcid.org/0000-0002-1035-7519

Ione Parra Barbosa-TessmannBiochemistry Department, Biological Sciences Center, State University of Maringá, Av. Colombo, 5790, Maringá, Paraná, 87020-900, Brazil. ipbtessmann@uem.br.ORCID http://orcid.org/0000-0001-9860-378X

Funding

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior 001Coordenação de Aperfeiçoamento de Pessoal de Nível Superior Scholarship

6 · The paper itself

Abstract

Halophilic α-amylases remain active at high concentrations of salt. Therefore, they can be used in starch-processing industries operating under extreme saline conditions, such as the baking and detergent industries, as well as in effluent remediation processes. In the present work, an endogenous halophilic α-amylase from the CAZy GH13_5 subfamily was recombinantly expressed and characterized from a non-halophilic Paenibacillus pabuli isolate. The predicted structural model revealed the three characteristic domains of α-amylases. In addition, the protein contained the seven conserved sequence regions (CSRs) and the catalytic triad (Asp-Glu-Asp) of α-amylases. The 60.1 kDa purified enzyme had an optimum pH of 7.0 and an optimum temperature of 40 °C. The enzyme's T

Indexed as

alpha-AmylasesBacterial ProteinsPaenibacillusEnzyme StabilityHydrogen-Ion ConcentrationRecombinant ProteinsStarchSubstrate SpecificityTemperaturealpha-AmylasesBacterial ProteinsRecombinant ProteinsStarchEndogenousEscherichia coliHalophilicPaenibacillus pabuliRecombinant α-amylaseSubfamily GH13_5

Identifiers

PMID41335388

DOI10.3389/fmicb.2019.01895

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