Cohnella terricola sp. nov., isolated from soil

Kim, Jiyoun; Chhetri, Geeta; Kim, Inhyup; Kang, Minchung; Seo, Taegun

doi:10.1099/ijsem.0.004835

Cited by 8 publications

(1 citation statement)

References 44 publications

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“…The genome sizes of Cohnella strains typically range from 3.3 Mbp to 9.4 Mbp. The draft genome size of strain NL03-T5 was reported to be 7.44 Mbp ( Wang et al, 2023 ), while stain C. thermotolerans CCUG 47242 T was determined to be 5.05 Mbp ( Kim et al, 2021 ). The genome size of strain Cohnella sp.…”

Section: Discussionmentioning

confidence: 99%

Identification of a novel xanthan-binding module of a multi-modular Cohnella sp. xanthanase

Han,

Baudrexl,

Ludwig

et al. 2024

Front. Microbiol.

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A new strain of xanthan-degrading bacteria identified as Cohnella sp. has been isolated from a xanthan thickener for food production. The strain was able to utilize xanthan as the only carbon source and to reduce the viscosity of xanthan-containing medium during cultivation. Comparative analysis of the secretomes of Cohnella sp. after growth on different media led to the identification of a xanthanase designated as CspXan9, which was isolated after recombinant production in Escherichia coli. CspXan9 could efficiently degrade the β-1,4-glucan backbone of xanthan after previous removal of pyruvylated mannose residues from the ends of the native xanthan side chains by xanthan lyase treatment (XLT-xanthan). Compared with xanthanase from Paenibacillus nanensis, xanthanase CspXan9 had a different module composition at the N- and C-terminal ends. The main putative oligosaccharides released from XLT-xanthan by CspXan9 cleavage were tetrasaccharides and octasaccharides. To explore the functions of the N- and C-terminal regions of the enzyme, truncated variants lacking some of the non-catalytic modules (CspXan9-C, CspXan9-N, CspXan9-C-N) were produced. Enzyme assays with the purified deletion derivatives, which all contained the catalytic glycoside hydrolase family 9 (GH9) module, demonstrated substantially reduced specific activity on XLT-xanthan of CspXan9-C-N compared with full-length CspXan9. The C-terminal module of CspXan9 was found to represent a novel carbohydrate-binding module of family CBM66 with binding affinity for XLT-xanthan, as was shown by native affinity polyacrylamide gel electrophoresis in the presence of various polysaccharides. The only previously known binding function of a CBM66 member is exo-type binding to the non-reducing fructose ends of the β-fructan polysaccharides inulin and levan.

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Section: Discussionmentioning

confidence: 99%