The Family Thermoactinomycetaceae

Carrillo, L.; Benítez-Ahrendts, Marcelo Rafael

doi:10.1007/978-3-642-30120-9_355

Cited by 4 publications

(1 citation statement)

References 66 publications

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“…The family Thermoactinomycetaceae Matsuo et al 2006, belonging to the order Caryophanales, class Bacilli, phylum Bacillota, encompasses aerobic, Gram-positive bacteria that form aerial and/or substrate mycelia with endospores [1][2][3][4][5]. Strains belonging to this family have been isolated from various sources, including soil, compost, marine sediments, sputa, sugarcane, clinical specimens and hot springs [6]. The genus Polycladomyces Tsubouchi et al 2013 [7] is one of the 24 validly published genera of this family and includes two species, namely Polycladomyces abyssicola JIR-001 T [7,8] and Polycladomyces subterraneus KSR 13 T [9], isolated from deep seafloor sediment off the Shimokita Peninsula of Japan and from forest soil in Thailand, respectively, with P. abyssicola as the type species.…”

Section: Introductionmentioning

confidence: 99%

Polycladomyces zharkentensis sp. nov., a novel thermophilic cellulose- and starch-degrading member of the Bacillota from a geothermal aquifer in Kazakhstan

Mashzhan,

Kistaubayeva,

Javier-López

et al. 2024

International Journal of Systematic and Evolutionary Microbiology

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A thermophilic, aerobic and heterotrophic filamentous bacterium, designated strain ZKZ2T, was isolated from a pipeline producing hydrothermal water originating from a >2.3 km deep subsurface geothermal source in Zharkent, Almaty region, Kazakhstan. The isolate was Gram-stain-positive, non-motile, heat-resistant and capable of producing a variety of extracellular hydrolases. Growth occurred at temperatures between 55 and 75 °C, with an optimum around 70 °C, and at pH values between 5.5 and 9.0, with an optimum at pH 7.0–7.5 with the formation of aerial mycelia; endospores were produced along the aerial mycelium. The isolate was able to utilize the following substrates for growth: glycerol, l-arabinose, ribose, d-xylose, d-glucose, d-fructose, d-mannose, rhamnose, d-mannitol, methyl-d-glucopyranoside, aesculin, salicin, cellobiose, maltose, melibiose, sucrose, trehalose, melezitose, raffinose, starch, turanose and 5-keto-gluconate. Furthermore, it was able to hydrolyse carboxymethylcellulose, starch, skimmed milk, Tween 60 and Tween 80. The major cellular fatty acids were iso-C15 : 0, iso-C17 : 0, iso-C16 : 0 and C16 : 0. Our 16S rRNA gene sequence analysis placed ZKZ2T within the genus Polycladomyces, family Thermoactinomycetaceae, with the highest similarity to the type species Polycladomyces abyssicola JIR-001T (99.18 % sequence identity). Our draft genome sequence analysis revealed a genome size of 3.3 Mbp with a G+C value of 52.5 mol%. The orthologous average nucleotide identity value as compared to that of its closest relative, P. abyssicola JIR-001T, was 90.23 %, with an in silico DNA–DNA hybridization value of 40.7 %, indicating that ZKZ2T represents a separate genome species. Based on the phenotypic and genome sequence differences from the other two Polycladomyces species, we propose that strain ZKZ2T represents a novel species, for which we propose the name Polycladomyces zharkentensis sp. nov. The type strain is ZKZ2T (=CECT 30708T=KCTC 43421T).

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Section: Introductionmentioning

confidence: 99%

Polycladomyces zharkentensis sp. nov., a novel thermophilic cellulose- and starch-degrading member of the Bacillota from a geothermal aquifer in Kazakhstan

Mashzhan,

Kistaubayeva,

Javier-López

et al. 2024

International Journal of Systematic and Evolutionary Microbiology

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Gene sequence, modeling, and enzymatic characterization of α-amylase AmyLa from the thermophileLaceyellasp. DS3

et al. 2017

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α‐Amylase (AmyLa) from Laceyella sp. DS3 was purified 13.8‐fold by ammonium sulfate precipitation, gel filtration, and ion exchange chromatography. The purified AmyLa showed an optimum pH of 7 and an optimum temperature 55°C. It had activation energy, Km, and Vmax of 196.1 kJ, 0.81 mg/mL, and 2.85 mg/min, respectively. Co2+, Cu2+, Hg2+, and Na+ were strong inhibitors of AmyLa whereas Cl− was an activator. Although AmyLa is a Ca2+ independent α‐amylase, it was activated by Ca2+. The AmyLa gene encoding α‐amylase activity was sequenced. It revealed putative triple promoters and an open reading frame of 1449 bp (483 amino acids) including a 29 amino acid putative signal peptide. AmyLa was shown to possess four conserved sequence regions of the GH13 family. Polyacrylamide gel electrophoresis identified 69.2 and 72.5 kDa proteins whose α‐amylase activities were confirmed by native gel staining. Modeling of AmyLa revealed three domains A–C with domain A containing a catalytic (β/α)8 barrel. Phylogenetic and evolutionary tree analysis suggests that AmyLa might be have been transferred from fungi to an ancient thermoactinomycete ancestor, then adapted to bacterial genome features.

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Thermoactinomycetes isolated from geothermal springs in Armenia capable of producing extracellular hydrolases

Panosyan

2019

Environmental Sustainability

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The Family Thermoactinomycetaceae

Cited by 4 publications

References 66 publications

Polycladomyces zharkentensis sp. nov., a novel thermophilic cellulose- and starch-degrading member of the Bacillota from a geothermal aquifer in Kazakhstan

Polycladomyces zharkentensis sp. nov., a novel thermophilic cellulose- and starch-degrading member of the Bacillota from a geothermal aquifer in Kazakhstan

Gene sequence, modeling, and enzymatic characterization of α-amylase AmyLa from the thermophileLaceyellasp. DS3

Thermoactinomycetes isolated from geothermal springs in Armenia capable of producing extracellular hydrolases

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