Dataset Information

Fervidobacterium pennivorans subsp. keratinolyticus subsp. nov., a Novel Feather-Degrading Anaerobic Thermophile.

ABSTRACT: Fervidobacterium pennivorans subsp. keratinolyticus subsp. nov. strain T was isolated from a terrestrial, high-altitude hot spring in Tajikistan. This strain is an obligate anaerobic rod and their cells occur singly, in pairs, or as short chains under the optimal growth conditions of a temperature of 65 °C and pH 6.5, with peptone, glucose, and galactose as the preferred substrates. The minimum generation time of this strain is 150 min. Strain T can efficiently degrade feather keratin at 65-75 °C; this unusual feature is also exhibited by a few other members of the Fervidobacterium genus. The total genome size of this bacterial strain is 2,002,515 base pairs, with a C + G content of 39.0%. The maximum digital DNA-DNA hybridization (dDDH) value of 76.9% was observed on comparing the genome of this strain with that of Fervidobacterium pennivorans type strain DSM9078. This study describes the physiological and genomic properties of strain T, with an emphasis on its keratinolytic power and differences from other members of the genus Fervidobacterium.

SUBMITTER: Javier-Lopez R

PROVIDER: S-EPMC9861569 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature

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Fervidobacterium pennivorans subsp. keratinolyticus subsp. nov., a Novel Feather-Degrading Anaerobic Thermophile.

Javier-Lopez Rubén R Mandolini Edoardo E Dzhuraeva Munavvara M Bobodzhanova Khursheda K Birkeland Nils-Kåre NK

Microorganisms 20221221 1

Fervidobacterium pennivorans subsp. keratinolyticus subsp. nov. strain T was isolated from a terrestrial, high-altitude hot spring in Tajikistan. This strain is an obligate anaerobic rod and their cells occur singly, in pairs, or as short chains under the optimal growth conditions of a temperature of 65 °C and pH 6.5, with peptone, glucose, and galactose as the preferred substrates. The minimum generation time of this strain is 150 min. Strain T can efficiently degrade feather kera ...[more]

PMID: 36677314

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Project description:In this study, five keratinolytic bacteria were isolated from poultry farm waste of Eastern Province, Saudi Arabia. The highest keratinase activity was obtained at 40-45 °C, pH 8-9, feather concentration 0.5-1%, and using white chicken feather as keratin substrate for 72 h. Enhancement of keratinase activity through physical mutagen UV radiation and/or chemical mutagen ethyl methanesulfonate (EMS) resulted in five mutants with 1.51-3.73-fold increased activity over the wild type. When compared with the wild type, scanning electron microscopy validated the mutants' effectiveness in feather degradation. Bacterial isolates are classified as members of the S8 family peptidase Bacillus cereus group based on sequence analysis of the 16S rRNA and keratinase genes. Interestingly, keratinase KerS gene shared 95.5-100% identity to keratinase, thermitase alkaline serine protease, and thermophilic serine protease of the B. cereus group. D137N substitution was observed in the keratinase KerS gene of the mutant strain S13 (KerS13uv+ems), and also seven substitution variations in KerS26 and KerS26uv of strain S26 and its mutant S26uv. Functional analysis revealed that the subtilisin-like serine protease domain containing the Asp/His/Ser catalytic triad of KerS gene was not affected by the predicted substitutions. Prediction of physicochemical properties of KerS gene showed instability index between 17.5-19.3 and aliphatic index between 74.7-75.7, which imply keratinase stability and significant thermostability. The docking studies revealed the impact of substitutions on the superimposed structure and an increase in binding of mutant D137N of KerS13uv+ems (affinity: -7.17; S score: -6.54 kcal/mol) and seven mutants of KerS26uv (affinity: -7.43; S score: -7.17 kcal/mol) compared to the wild predicted structure (affinity: -6.57; S score: -6.68 kcal/mol). Together, the keratinolytic activity, similarity to thermostable keratinases, and binding affinity suggest that keratinases KerS13uv+ems and KerS26uv could be used for feather processing in the industry.

Dataset Information

Fervidobacterium pennivorans subsp. keratinolyticus subsp. nov., a Novel Feather-Degrading Anaerobic Thermophile.

Publications

<i>Fervidobacterium pennivorans</i> subsp. <i>keratinolyticus</i> subsp. nov., a Novel Feather-Degrading Anaerobic Thermophile.

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