Isolation and identification of feather degrading bacteria from feather-dumped soil

Rajesh, Thangamani; Rajasekar, S; Mathan, R. Karthick Hari; Balaiah, Anandaraj

doi:10.1504/ijesd.2016.077393

Cited by 7 publications

(8 citation statements)

References 5 publications

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“…The keratinase enzyme production was carried out in the basal medium by using shaking flask. The composition of the media was (g/l): feather meal powder (10 g), NH 4 Cl (1 g), NaCl (1 g), K 2 HPO 4 (0.6 g), KH 2 PO 4 (0.8 g), MgCl 2 ·6H 2 O (0.48 g) and yeast extract (0.2 g) with pH 7.5 (Rajesh et al 2014 ). 2.5 ml of the bacterial inoculums was added in 50 ml of medium and cultured on a rotary shaking incubator (Stuart SI 500, UK) at 150 rpm and 37 °C for 72 h. After incubation, fermented broth was centrifuged at 5000 rpm for 20 min at 4 °C.…”

Section: Methodsmentioning

confidence: 99%

Production, partial optimization and characterization of keratinase enzyme by Arthrobacter sp. NFH5 isolated from soil samples

Barman

Zohora²,

Das³

et al. 2017

AMB Expr

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The study was conducted to select the best promising keratinolytic bacterial strain. A good keratinase positive bacterium isolated from the soil samples of Hazaribagh tannery industrial zone, Dhaka was identified as Arthrobacter genus depending on the conventional techniques and confirmed as Arthrobacter sp. by sequencing 16S rRNA gene. The medium components and culture conditions were optimized to enhance keratinase production through shake flask culture. Keratin and feather powder (10 g/l or 1%) were good substrates for the highest keratinase production along with yeast extract (0.2 g/l or 0.02%) as an organic nitrogen source and potassium nitrate (1 g or 0.1%) as an inorganic nitrogen source. Maximum yield of keratinase was found after 24 h of incubation at 37 °C with an initial pH of 7.0 and inoculums volume 5% under 150 rpm when keratin, yeast extract and potassium nitrate were used as nutrient sources. Keratinase production was more than 5.0-fold increased when all optimized parameters were applied simultaneously. The optimum reaction temperature and pH were determined to be 40 °C and 8.0 respectively for crude keratinase activity. Therefore, Arthrobacter sp. NFH5 might be used for large scale production of keratinase for industrial purposes in less time.Electronic supplementary materialThe online version of this article (doi:10.1186/s13568-017-0462-6) contains supplementary material, which is available to authorized users.

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Section: Methodsmentioning

confidence: 99%

Production, partial optimization and characterization of keratinase enzyme by Arthrobacter sp. NFH5 isolated from soil samples

Barman

Zohora²,

Das³

et al. 2017

AMB Expr

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“…cereus isolated from a poultry dump area, Vibrio sp. kr2 isolated from decomposing feathers at a poultry processing plant and Pseudomonas aeruginosa isolated from a detergent-contaminated ponds [ 3 , 25 , 26 ]. Few studies have explored the diversity of feather-degrading bacteria from marine environments.…”

Section: Discussionmentioning

confidence: 99%

“…Using keratinase-producing strains to degrade feathers is a promising and utilised method at present. The method has slight effect on the environment, and converts a solid contaminant into nutritionally protein-rich feedstuff for livestock [ 3 ].…”

Section: Introductionmentioning

confidence: 99%

Isolation and identification of a feather degrading Bacillus tropicus strain Gxun-17 from marine environment and its enzyme characteristics

et al. 2022

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Background Feathers are the most abundant agricultural waste produced by poultry farms. The accumulation of a large number of feathers not only seriously pollutes the environment but also causes the waste of protein resources. The degradation of feather waste by keratinase-producing strains is currently a promising method. Therefore, screening high-producing keratinase strains from marine environment and studying the fermentation conditions, enzymatic properties and feather degradation mechanism are crucial for efficient degradation of feathers. Results A novel efficient feather-degrading bacteria, Gxun-17, isolated from the soil sample of a marine duck farm of Beibu Gulf in Guangxi, China, was identified as Bacillus tropicus. The optimum fermentation conditions were obtained by single factor and orthogonal tests as follows: feather concentration of 15 g/L, maltose concentration of 10.0 g/L, MgSO4 concentration of 0.1 g/L, initial pH of 7.0 and temperature of 32.5 °C. The strain completely degraded the feathers within 48 h, and the highest keratinase activity was 112.57 U/mL, which was 3.18-fold that obtained with the basic medium (35.37 U/mL). Detecting the keratinase activity and the content of sulphur-containing compounds in the fermentation products showed that the degradation of feathers by the strain might be a synergistic effect of the enzyme and sulphite. The keratinase showed optimal enzyme activity at pH 7.0 and temperature of 60 °C. The keratinase had the best performance on the casein substrate. When casein was used as the substrate, the Km and Vmax values were 15.24 mg/mL and 0.01 mg/(mL·min), respectively. Mg2+, Ca2+, K+, Co2+, Al3+, phenylmethylsulphonyl fluoride and isopropanol inhibited keratinase activity, which indicated that it was a serine keratinase. Conversely, the keratinase activity strongly increased with the addition of Mn2+ and β-mercaptoethanol. Conclusions A novel feather-degrading B. tropicus Gxun-17 was obtained from marine environment. The strain adapted the extreme conditions such as low temperature, high salt and high pressure. Thus, the keratinase had high activity, wide range of temperature and pH, salt tolerance and other characteristics, which had potential application value.

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“…Submerged fermentation was carried out in an Erlenmeyer shake flask fermenter. Basal modified medium was used for keratinase production containing feather meal powder (10 g/l), NH 4 Cl (1.0 g/l), NaCl (1.0 g/l), KH 2 PO 4 (0.8 g/l), K 2 HPO 4 (0.6 g/l), MgCl 2 .6H 2 O (0.5 g/l), yeast extract (0.2 g/l), and pH (7.5) with 5% bacterial inoculum [ 29 ]. The fermented organisms were cultivated in 250-ml cotton-plugged Erlenmeyer flasks after 72 h shaking at 150 rpm.…”

Section: Methodsmentioning

confidence: 99%

Keratinolytic protease from Pseudomonas aeruginosa for leather skin processing

Moonnee

Foysal

Hashem³

et al. 2021

Journal of Genetic Engineering and Biotechnology

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Background The leather industry generates huge volume of waste each year. Keratin is the principal constituents of this waste that is resistant to degradation. Some bacteria have the ability to degrade keratin through synthesis of a protease called keratinase that can be used as sources of animal feed and industrial production of biodiesel, biofertilizer, and bioplastic. Majority of the studies focused on keratin degradation using gram-positive bacteria. Not much of studies are currently available on production of keratinase from gram-negative bacteria and selection of best parameters for the maximum production of enzyme. The aim of this study was to isolate and characterize both groups of bacteria from soil for keratinase and optimize the production parameters. Results A total of 50 isolates were used for initial screening of enzyme production in skim milk, casein, and feather meal agar. Out of 50, five isolates showed significantly higher enzyme production in preliminary screening assays. Morphological and biochemical characterization revealed 60% of the isolates as gram-negative bacteria including two highest enzyme-producing isolates. The isolates were identified as Pseudomonas aeruginosa through sequencing of 16S rRNA gene. Maximum production of enzyme from P. aeruginosa YK17 was achieved with 2% chicken feather, beef extract, and ammonium nitrate as organic and inorganic nitrogen sources and glucose as a carbon source. Further analysis revealed that 3% inoculum, 40 °C growth temperature and 72-h incubation, resulted in maximum production of keratinase. Conclusion The overall results showed significant higher production of enzyme by the P. aeruginosa YK17 that can be used for the degradation of recalcitrant keratin waste and chemical dehairing in leather industries, thereby preventing environmental pollution.

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Isolation and identification of feather degrading bacteria from feather-dumped soil

Cited by 7 publications

References 5 publications

Production, partial optimization and characterization of keratinase enzyme by Arthrobacter sp. NFH5 isolated from soil samples

Production, partial optimization and characterization of keratinase enzyme by Arthrobacter sp. NFH5 isolated from soil samples

Isolation and identification of a feather degrading Bacillus tropicus strain Gxun-17 from marine environment and its enzyme characteristics

Keratinolytic protease from Pseudomonas aeruginosa for leather skin processing

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