Biotechnology and Bioprocess Engineering:BBE

The Korean Society for Biotechnology and Bioengineering (한국생물공학회)
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Production and Characterization of Keratinase from Paracoccus sp. WJ-98

  • Lee, Yoon-Jeong (Department of Genetic Engineering and Bio-Medicinal Resources Research Center, Paichai University) ;
  • Kim, Jae-Ho (Department of Genetic Engineering and Bio-Medicinal Resources Research Center, Paichai University) ;
  • Kim, Ha-Kun (Department of Genetic Engineering and Bio-Medicinal Resources Research Center, Paichai University) ;
  • Lee, Jong-Soo (Department of Genetic Engineering and Bio-Medicinal Resources Research Center, Paichai University)
  • Published : 2004.01.01
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Abstract

A bacterial strain WJ-98 found to produce active extracellular keratinase was isolated from the soil of a poultry factory. It was identified as Paracoccus sp. based on its 16S rRNA sequence analysis, morphological and physiological characteristics. The optimal culture conditions for the production of keratinase by Paracoccus sp. WJ-98 were investigated. The optimal medium composition for keratinase production was determined to be 1.0% keratin, 0.05% urea and NaCl, 0.03% K$_2$HPO$_4$, 0.04% KH$_2$PO$_4$, and 0.01% MgCl$_2$$.$6H$_2$O. Optimal initial pH and temperature for the production of keratinase were 7.5 and 37$^{\circ}C$, respectively. The maximum keratinase production of 90 U/mL was reached after 84 h of cultivation under the optimal culturing conditions. The keratinase from Paracoccus sp. WJ-98 was partially purified from a culture broth by using ammonium sulfate precipitation, ion-exchange chromatography on DEAE-cellulose, followed by gel filtration chromatography on Sephadex G-75. Optimum pH and temperature for the enzyme reaction were pH 6.8 and 50$^{\circ}C$, respectively and the enzymes were stable in the pH range from 6.0 to 8.0 and below 50$^{\circ}C$. The enzyme activity was significantly inhibited by EDTA, Zn$\^$2+/ and Hg$\^$2+/. Inquiry into the characteristics of keratinase production from these bacteria may yield useful agricultural feed processing applications.

Keywords

References

  1. Appl. Environ. Microbiol. v.56 Isolation, identification, and charcteriation of a feather-degrading bacterium Williams,C.M.;C.S.Richter;M.Kenzie,Jr.;J.C.H.Shih
  2. Biochim. Biophys. Acta. v.77 Keratinase: I. Properties of the enzyme conjugate dlaborated by Streptomyces fradiae Nickerson,W.J.;J.J.Noval;R.S.Robinson https://doi.org/10.1016/0006-3002(63)90470-0
  3. Poult. Sci. v.45 Keratin as a source of protein for the growing chick: I. Amino acid imbalance as the cause for inferior performance of feather as the reason for poor digestibility Moran,E.T.;J.D.Summers;S.J.Slinger https://doi.org/10.3382/ps.0451257
  4. Text. Res. J. v.20 A new wool degrading fungus-Ctenomyces species Sen Gupta S.;R.S.Nigram;R.N.Tandan https://doi.org/10.1177/004051755002001003
  5. Enzyme Nomenclature into Korean Park,I.W.
  6. Aust. J. Biol. Sci. v.12 The digestion of wool by a kerationlytic Bacillus Molyneaux,G.S. https://doi.org/10.1071/BI9590274
  7. J. Appl. Bacteriol. v.67 Enumeration of some microbial groups in thermophilic poultry waste degesters and enrichment of a feather-degrading culture Williams,C.M.;J.C.H.Shih https://doi.org/10.1111/j.1365-2672.1989.tb04951.x
  8. Appl. Environ. Microbiol. v.58 Purification and characterization of a keratinase from a feather-degrading Bacillus licheniformis strain Lin,X.;C.G.Lee;E.S.Casale;J.C.H.Shih
  9. Arch. Nicrobiol. v.178 Native-feather degradation by Fervidobacterium islandicum AW-1, a newly isolated keratinase-producing thermophilic anaerobe Nam,G.W.;D.W.Lee;H.S.Lee;N.J.Lee;N.J.Lee;B.C.Kim;E.A.Choe;J.K.Hwang;M.T.Suhartono;Y.R.Pyun https://doi.org/10.1007/s00203-002-0489-0
  10. Proceeding of Spring Meeting of Kor. Soc. Appl. Microbial. Studies on thermostable keratinase. from Hydrogenophilus thermoluteolus KJ-30 Kim,S.Y.;G.W.Nam;D.W.Lee;B.C.Kim;H.J.Choi;S.B.Kim;Y.R.Pyun
  11. J. Lab. Clim. Med. v.34 The use of azoalbumin as a substrate in the colormetric determination of pepric and tryptic activity Tomarelli,R.W.;J.Charney;M.L.Herding
  12. Kor. J. Microbiol. Biotechnol. v.31 Optimization of β-mannase production from Bacillus subtilis JS-1 Yim,J,S,;J.W.Jung;J.S.Lee;D.K.Kang;H.K.Kim
  13. Kor. J. Appl. Microbiol. Biotechnol. v.29 Isolation of keratinolytic protease producing microorganism and its cultivation condition Chon,D.H.;T.J.Kwon
  14. Biosci. Biotech. Biochem. v.56 Degradation of hyman hair by a thermostable alkaline protease from alkalophilic Bacillus sp. No. AH 101 Tidero,T.;S.Nakamura;R.Aono;K.Horikoshin https://doi.org/10.1271/bbb.56.1667
  15. J. Bacteriol. v.96 Iso;atopm amd purification of an extracellullar keratinase of Trichophyton mentagrophytes Yu,R.J.;S.R.Harmon;F.Blank
  16. J. Bacteriol. v.117 Phosphate-mediated alteration of the Microsporum gypseum germination protease specificity for substrate: Enhanced keratinase activity Page,W.J.;J.J.Stock
  17. Med. Microbiol. Immunol. v.180 Quantification of keratinolytic activity from Dermatophilus congolensis Hamel,H.;J.Kalisch;M.Keil;W.C.Marsch;M.Buslan