• This record comes from PubMed

Keratinolytic enzyme-mediated biodegradation of recalcitrant poultry feathers waste by newly isolated Bacillus sp. NKSP-7 under submerged fermentation

. 2020 Oct ; 65 (5) : 823-834. [epub] 20200516

Language English Country United States Media print-electronic

Document type Journal Article

Links

PubMed 32415568
DOI 10.1007/s12223-020-00793-6
PII: 10.1007/s12223-020-00793-6
Knihovny.cz E-resources

Microbial and enzymatic degradation of keratin waste is more preferred over various conventional approaches which are costly and not environmentally suitable. Diverse niches are auspicious for the discovery of new microorganisms. To discover novel keratinolytic bacteria, 60 isolates from different poultry dumping sites were initially screened, and among these found a potent keratinolytic isolate (NKSP-7) that displayed higher feather-degrading ability. The selected isolate was identified as Bacillus sp. NKSP-7 based on 16S rDNA sequencing as well as physiochemical and morphological characteristics. The strain NKSP-7 showed complete hydrolysis of native chicken feathers (10 g/L) in nutrient medium after 24 h of incubation at 37 °C under agitation (150 rev/min) and produced thermostable extracellular keratinase. The crude enzyme displayed maximal keratinolytic activity (34.7 U/mL) in phosphate buffer of pH 7.0, and at 60 °C using keratin azure as a substrate. Keratinolytic enzyme showed stability at 20-65 °C for 4 h over the pH range of 5.5-8.0. No obvious inhibitory influence was perceived by cations, organic solvents, EDTA, and detergents. Whereas, enzyme activity was enhanced by adding β-mercaptoethanol, Na+, Cd2+, and Mn2+. All these notable features of keratinase make it a promising candidate for various industrial applications especially for dehairing process in leather industry, bioconversion of poultry waste, and in detergents formulations.

See more in PubMed

Abdel-Fattah AM, El-Gamal MS, Ismail SA, Emran MA, Hashem AM (2018) Biodegradation of feather waste by keratinase produced from newly isolated Bacillus licheniformis ALW1. J Genet Eng Biotechnol 16:311–318. https://doi.org/10.1016/j.jgeb.2018.05.005 PubMed DOI PMC

Agrahari S, Wadhwa N (2010) Degradation of chicken feather a poultry waste product by keratinolytic bacteria isolated from dumping site at Ghazipur poultry processing plant. Int J Poult Sci 9:482–489. https://doi.org/10.3923/ijps.2010.482.489 DOI

Agrawal B, Dalal M (2015) Screening and characterization of keratinase enzyme obtained from keratin degrading microorganism isolated from Sanjan poultry waste dumping soil. Eur Acad Res 2:13986–13994

Akram F, Haq IU, Mukhtar H (2018) Gene cloning, characterization and thermodynamic analysis of a novel multidomain hyperthermophilic GH family 3 β-glucosidase (TnBglB) from Thermotoga naphthophila RKU-10 DOI

Basar B, Shamzi MM, Rosfarizan M, Puspaningsih NNT, Ariff AB (2010) Enhanced production of thermophilic xylanase by recombinant Escherichia coli DH5α through optimization of medium and dissolved oxygen level. Int J Agric Biol 12:321–328

Bhari R, Manpreet K, Sarup SR, Ashok P, Christian L (2018) Bioconversion of chicken feathers by Bacillus aerius NSMk2: a potential approach in poultry waste management. Bioresour Technol Rep 3:224–230. https://doi.org/10.1016/j.biteb.2018.07.015 DOI

Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254. https://doi.org/10.1006/abio.1976.9999 DOI

Brandelli A (2005) Production of an extracellular keratinase from Chryseobacterium sp. growing on raw feathers. Electron. J Biotechnol 8:0717–3458. https://doi.org/10.4067/S0717-34582005000100007 DOI

Cai CG, Chen JS, Qi JJ, Yin Y, Zheng XD (2008) Purification and characterization of keratinase from a new Bacillus subtilis strain. J Zhejiang Univ Sci B 9:713–720. https://doi.org/10.1631/jzus.B0820128 PubMed DOI PMC

Cascarosa E, Gea G, Arauzo J (2012) Thermochemical processing of meat and bone meal: a review. Renew Sust Energ Rev 16:942–957. https://doi.org/10.1016/j.rser.2011.09.015 DOI

Ghasemi Y, Shahbazi M, Rasoul-Amini S, Kargar M, Azam S, Kazemi A, Montazeri-Najafabady N (2012) Identification and characterization of feather-degrading bacteria from keratin-rich wastes. Ann Microbiol 62:737–744. https://doi.org/10.1007/s13213-011-0313-7 DOI

Gopinath SCB, Anbu P, Lakshmipriya T, Tang TH, Chen Y, Hashim U, Ruslinda AR, Arshad MKMD (2015) Biotechnological aspects and perspective of microbial keratinase production. Biomed Res Int 140726:10–10. https://doi.org/10.1155/2015/140726 DOI

Holt J G, Krieg NR, Sneath PHA, Staley JT, Willaims ST (1994) Bergey’s manual of determinative bacteriology: Ninth Edition, Baltimore

Kazi YF, Kumar P, Soomro IH (2015) Characterization of the keratinolytic activity of indigenous Bacillus subtilis keratinase. J Chem Pharm Res 7:800–809

Kshetri P, Ningthoujam DS (2016) Keratinolytic activities of alkaliphilic Bacillus sp. MBRL 575 from a novel habitat, limestone deposit site in Manipur, India. Springer plus 5:595. https://doi.org/10.1186/s40064-016-2239-9

Kurane AB, Attar YC (2017) Screening and isolation of keratinase producing microorganisms. Int J Res Appl Sci Eng Technol 5:489–495

Ningthoujam DS, Devi LJ, Devi PJ, Kshetri P, Tamreihao K, Mukherjee S, Devi SS, Betterson N (2016) Optimization of keratinase production by Amycolatopsis sp. strain MBRL 40 from a limestone habitat. J Bioprocess Biotechnol 6:282. https://doi.org/10.4172/2155-9821.1000282 DOI

Peng Z, Zhang J, Du G, Chen J (2019) Keratin waste recycling based on microbial degradation: mechanisms and prospects. ACS Sustain Chem Eng 7:9727–9736 DOI

Prasad HV, Kumar G, Karthik L, Rao BKV (2010) Screening of extracellular keratinase producing bacteria from feather processing areas in Vellore, Tamil Nadu, India. J Sci Res 2(3):559–565. https://doi.org/10.3329/jsr.v2i3.4567 DOI

Raju EVN, Divakar DG (2013) Screening and isolation of keratinase producing bacteria from poultry waste. Int J Pharm Res Allied Sci 2:70–74

Sahoo DK, Das A, Thatoi H, Mondal KC, Pradeep K, Mohapatra D (2012) Keratinase production and biodegradation of whole chicken feather keratin by a newly isolated bacterium under submerged fermentation. Appl Biochem Biotechnol 167:1040–1051. https://doi.org/10.1007/s12010-011-9527-1 PubMed DOI

Saibabu V, Niyonzima FN, More SS (2013) Isolation, partial purification and characterization of keratinase from Bacillus megaterium. Int Res J Biol Sci 2:13–20

Sekar V, Kannan M, Ganesan R, Dheeba B, Sivakumar N, Kannan K (2016) Isolation and screening of keratinolytic bacteria from feather dumping soil in and around Cuddalore and Villupuram, Tamil Nadu. Proc Natl Acad Sci India Sect B Biol Sci 86:567–575. https://doi.org/10.1007/s40011-014-0483-8 DOI

Sharma R, Devi S (2018) Versatility and commercial status of microbial keratinases: a review. Rev Environ Sci Biotechnol 17:19–45. https://doi.org/10.1007/s11157-017-9454-x DOI

Tamreihao K, Mukherjee S, Khunjamayum R, Devi LJ, Asem RS, Ningthoujam DS (2019) Feather degradation by keratinolytic bacteria and biofertilizing potential for sustainable agricultural production. J Basic Microbiol 59:4–13. https://doi.org/10.1002/jobm.201800434 PubMed DOI

Tork S, Aly MM, Nawar L (2010) Biochemical and molecular characterization of a new local keratinase producing Pseudomomanas sp., MS21. Asian J Biotechnol 2:1–13. https://doi.org/10.3923/ajbkr.2010.1.13 DOI

Vigneshwaran C, Shanmugam S, Kumar TS (2010) Screening and characterization of keratinase from Bacillus licheniformis isolated from Namakkal poultry farm. Researcher 2:89–96

Xu B, Zhong Q, Tang X, Yang Y, Huang Z (2009) Isolation and characterization of a new keratinolytic bacterium that exhibits significant feather-degrading capability. Afr J Biotechnol 8:4590–4595

Find record

Citation metrics

Loading data ...

Archiving options

Loading data ...