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Volumn 82, Issue 5, 2009, Pages 941-950

Sustainable and practical degradation of intact chicken feathers by cultivating a newly isolated thermophilic Meiothermus ruber H328

Author keywords

Hard to degrade; Keratin; Protease; Thermophile

Indexed keywords

AEROBIC CULTIVATIONS; CHICKEN FEATHERS; DEGRADATION EFFICIENCIES; FEATHER DEGRADATIONS; FEEDSTUFFS; FREE AMINO ACIDS; HARD-TO-DEGRADE; KERATIN; MATRIX-ASSISTED LASER DESORPTION IONIZATION-MASS SPECTROMETRIES; MEIOTHERMUS RUBER; MODERATELY THERMOPHILIC; OLIGO-PEPTIDES; OLIGOPEPTIDE; PRE TREATMENTS; PROTEASE; PROTEOLYTIC DIGESTIONS; SOLUBLE FRACTIONS; THERMOPHILE; THERMOPHILIC BACTERIUM; TIME-OF-FLIGHT ANALYSIS;

EID: 62949235842     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-009-1880-4     Document Type: Article
Times cited : (53)

References (38)
  • 1
    • 0036225062 scopus 로고    scopus 로고
    • Production, purification and characterization of an extracellular keratinase from Lysobacter NCIMB 9497
    • JD Allpress G Mountain PC Gowland 2002 Production, purification and characterization of an extracellular keratinase from Lysobacter NCIMB 9497 Lett Appl Microbiol 34 337 342
    • (2002) Lett Appl Microbiol , vol.34 , pp. 337-342
    • Allpress, J.D.1    Mountain, G.2    Gowland, P.C.3
  • 3
    • 0028883655 scopus 로고
    • Characterization of a keratinolytic serine proteinase from Streptomyces pactum DSM 40530
    • B Böckle B Galunsky R Müller 1995 Characterization of a keratinolytic serine proteinase from Streptomyces pactum DSM 40530 Appl Environ Microbiol 61 3705 3710
    • (1995) Appl Environ Microbiol , vol.61 , pp. 3705-3710
    • Böckle, B.1    Galunsky, B.2    Müller, R.3
  • 4
    • 0033013666 scopus 로고    scopus 로고
    • Purification and characterization of a keratinolytic serine proteinase from Streptomyces albidoflavus
    • P Bressollier F Letourneau M Urdaci B Verneuil 1999 Purification and characterization of a keratinolytic serine proteinase from Streptomyces albidoflavus Appl Environ Microbiol 65 2570 2576
    • (1999) Appl Environ Microbiol , vol.65 , pp. 2570-2576
    • Bressollier, P.1    Letourneau, F.2    Urdaci, M.3    Verneuil, B.4
  • 5
    • 0030951547 scopus 로고    scopus 로고
    • Enzymic modification of feather keratin hydrolyzates with lysine aimed at increasing the biological value
    • P Dalev I Ivanov A Liubomirova 1997 Enzymic modification of feather keratin hydrolyzates with lysine aimed at increasing the biological value J Sci Food Agric 73 242 244
    • (1997) J Sci Food Agric , vol.73 , pp. 242-244
    • Dalev, P.1    Ivanov, I.2    Liubomirova, A.3
  • 6
    • 18844416154 scopus 로고    scopus 로고
    • Physical and chemical characterization of crude meat and bone meal combustion residue: "waste or raw material?"
    • E Deydier R Guilet S Sarda P Sharrock 2005 Physical and chemical characterization of crude meat and bone meal combustion residue: "Waste or raw material?" J Hazard Mater 121 141 148
    • (2005) J Hazard Mater , vol.121 , pp. 141-148
    • Deydier, E.1    Guilet, R.2    Sarda, S.3    Sharrock, P.4
  • 7
    • 0029659518 scopus 로고    scopus 로고
    • Keratin degradation by Fervidobacterium pennavorans, a novel thermophilic anaerobic species of the order Thermotogales
    • AB Friedrich G Antranikian 1996 Keratin degradation by Fervidobacterium pennavorans, a novel thermophilic anaerobic species of the order Thermotogales Appl Environ Microbiol 62 2875 2882
    • (1996) Appl Environ Microbiol , vol.62 , pp. 2875-2882
    • Friedrich, A.B.1    Antranikian, G.2
  • 8
    • 0021307696 scopus 로고
    • A comparison of genomic coding sequences for feather and scale keratins: Structural and evolutionary implications
    • K Gregg SD Wilton DA Parry GE Rogers 1984 A comparison of genomic coding sequences for feather and scale keratins: structural and evolutionary implications EMBO J 3 175 178
    • (1984) EMBO J , vol.3 , pp. 175-178
    • Gregg, K.1    Wilton, S.D.2    Parry, D.A.3    Rogers, G.E.4
  • 9
    • 32644435175 scopus 로고    scopus 로고
    • Microbial keratinases and their prospective applications: An overview
    • R Gupta P Ramnani 2006 Microbial keratinases and their prospective applications: an overview Appl Microbiol Biotechnol 70 21 33
    • (2006) Appl Microbiol Biotechnol , vol.70 , pp. 21-33
    • Gupta, R.1    Ramnani, P.2
  • 10
    • 0022527223 scopus 로고
    • Chemotaxonomic and molecular-genetic studies of the genus Thermus: Evidence for a phylogenetic relationship of Thermus aquaticus and Thermus ruber to the Genus Deinococcus
    • R Hensel W Demharter O Kandler RM Kroppensterdt E Stackebrandt 1986 Chemotaxonomic and molecular-genetic studies of the genus Thermus: evidence for a phylogenetic relationship of Thermus aquaticus and Thermus ruber to the Genus Deinococcus Int J Syst Bacteriol 36 444 453
    • (1986) Int J Syst Bacteriol , vol.36 , pp. 444-453
    • Hensel, R.1    Demharter, W.2    Kandler, O.3    Kroppensterdt, R.M.4    Stackebrandt, E.5
  • 11
    • 33748770627 scopus 로고    scopus 로고
    • Characteristic features in the structure and collagen-binding ability of a thermophilic collagenolytic protease from the thermophile Geobacillus collagenovorans MO-1
    • Y Itoi M Horinaka Y Tsujimoto H Matsui K Watanabe 2006 Characteristic features in the structure and collagen-binding ability of a thermophilic collagenolytic protease from the thermophile Geobacillus collagenovorans MO-1 J Bacteriol 188 6572 6579
    • (2006) J Bacteriol , vol.188 , pp. 6572-6579
    • Itoi, Y.1    Horinaka, M.2    Tsujimoto, Y.3    Matsui, H.4    Watanabe, K.5
  • 12
  • 14
    • 0026795739 scopus 로고
    • Purification and characterization of a keratinase from a feather-degrading Bacillus licheniformis strain
    • X Lin CG Lee ES Casale JC Shih 1992 Purification and characterization of a keratinase from a feather-degrading Bacillus licheniformis strain Appl Environ Microbiol 58 3271 3275
    • (1992) Appl Environ Microbiol , vol.58 , pp. 3271-3275
    • Lin, X.1    Lee, C.G.2    Casale, E.S.3    Shih, J.C.4
  • 17
    • 0020058862 scopus 로고
    • Physical and genetic characterization of symbiotic and auxotrophic mutants of Rhizobium meliloti induced by transposon Tn5 mutagenesis
    • HM Meade SR Long GB Ruvkun SE Brown FM Ausubel 1982 Physical and genetic characterization of symbiotic and auxotrophic mutants of Rhizobium meliloti induced by transposon Tn5 mutagenesis J Bacteriol 149 114 122
    • (1982) J Bacteriol , vol.149 , pp. 114-122
    • Meade, H.M.1    Long, S.R.2    Ruvkun, G.B.3    Brown, S.E.4    Ausubel, F.M.5
  • 18
    • 20644433074 scopus 로고    scopus 로고
    • Two thimet oligopeptidase-like Pz peptidases produced by a collagen-degrading thermophile Geobacillus collagenovorans MO-1
    • R Miyake Y Shigeri Y Tatsu N Yumoto M Umekawa Y Tsujimoto H Matsui K Watanabe 2005 Two thimet oligopeptidase-like Pz peptidases produced by a collagen-degrading thermophile Geobacillus collagenovorans MO-1 J Bacteriol 187 4140 4148
    • (2005) J Bacteriol , vol.187 , pp. 4140-4148
    • Miyake, R.1    Shigeri, Y.2    Tatsu, Y.3    Yumoto, N.4    Umekawa, M.5    Tsujimoto, Y.6    Matsui, H.7    Watanabe, K.8
  • 20
    • 1842558262 scopus 로고    scopus 로고
    • An Aneurinibacillus sp. strain AM-1 produces a proline-specific aminopeptidase useful for collagen degradation
    • A Murai Y Tsujimoto H Matsui K Watanabe 2004 An Aneurinibacillus sp. strain AM-1 produces a proline-specific aminopeptidase useful for collagen degradation J Appl Microbiol 96 810 818
    • (2004) J Appl Microbiol , vol.96 , pp. 810-818
    • Murai, A.1    Tsujimoto, Y.2    Matsui, H.3    Watanabe, K.4
  • 21
    • 0036428747 scopus 로고    scopus 로고
    • Native-feather degradation by Fervidobacterium islandicum AW-1, a newly isolated keratinase-producing thermophilic anaerobe
    • GW Nam D Lee H Lee N Lee B Kim E Choe J Hwang MT Suhartono Y Pyun 2002 Native-feather degradation by Fervidobacterium islandicum AW-1, a newly isolated keratinase-producing thermophilic anaerobe Arch Microbiol 178 538 547
    • (2002) Arch Microbiol , vol.178 , pp. 538-547
    • Nam, G.W.1    Lee, D.2    Lee, H.3    Lee, N.4    Kim, B.5    Choe, E.6    Hwang, J.7    Suhartono, M.T.8    Pyun, Y.9
  • 22
    • 0029863893 scopus 로고    scopus 로고
    • Transfer of Thermus ruber (Loginova et al. 1984), Thermus silvanus (Tenreiro et al. 1995), and Thermus chliarophilus (Tenreiro et al. 1995) to Meiothermus gen nov. as Meiothermus ruber comb nov., Meiothermus silvanus comb nov, and Meiothermus chliarophilus comb nov., respectively, and emendation of the genus Thermus
    • MF Nobre HG Trüper MS da Costa 1996 Transfer of Thermus ruber (Loginova et al. 1984), Thermus silvanus (Tenreiro et al. 1995), and Thermus chliarophilus (Tenreiro et al. 1995) to Meiothermus gen nov. as Meiothermus ruber comb nov., Meiothermus silvanus comb nov, and Meiothermus chliarophilus comb nov., respectively, and emendation of the genus Thermus Int J Syst Bacteriol 46 604 606
    • (1996) Int J Syst Bacteriol , vol.46 , pp. 604-606
    • Nobre, M.F.1    Trüper, H.G.2    Da Costa, M.S.3
  • 23
    • 0034789606 scopus 로고    scopus 로고
    • A thermostable collagenolytic protease with a very large molecular mass produced by thermophilic Bacillus sp strain MO-1
    • M Okamoto Y Yonejima Y Tsujimoto Y Suzuki K Watanabe 2001 A thermostable collagenolytic protease with a very large molecular mass produced by thermophilic Bacillus sp strain MO-1 Appl Microbiol Biotechnol 57 103 108
    • (2001) Appl Microbiol Biotechnol , vol.57 , pp. 103-108
    • Okamoto, M.1    Yonejima, Y.2    Tsujimoto, Y.3    Suzuki, Y.4    Watanabe, K.5
  • 25
    • 0031657562 scopus 로고    scopus 로고
    • Hard α-keratin intermediate filament chains: Substructure of the N-and C-terminal domains and the predicted structure and function of the C-terminal domains of type i and type II chains
    • DAD Parry ACT North 1998 Hard α-keratin intermediate filament chains: substructure of the N-and C-terminal domains and the predicted structure and function of the C-terminal domains of type I and type II chains J Struct Biol 122 279 290
    • (1998) J Struct Biol , vol.122 , pp. 279-290
    • Parry, D.A.D.1    North, A.C.T.2
  • 26
    • 0024357840 scopus 로고
    • Avian keratin genes. I. A molecular analysis of the structure and expression of a group of feather keratin genes
    • RB Presland K Gregg PL Molloy CP Morris LA Crocker GE Rogers 1989 Avian keratin genes. I. A molecular analysis of the structure and expression of a group of feather keratin genes J Mol Biol 209 549 559
    • (1989) J Mol Biol , vol.209 , pp. 549-559
    • Presland, R.B.1    Gregg, K.2    Molloy, P.L.3    Morris, C.P.4    Crocker, L.A.5    Rogers, G.E.6
  • 27
    • 22844446261 scopus 로고    scopus 로고
    • Keratinolytic potential of Bacillus licheniformis RG1: Structural and biochemical mechanism of feather degradation
    • P Ramnani R Singh R Gupta 2005 Keratinolytic potential of Bacillus licheniformis RG1: structural and biochemical mechanism of feather degradation Can J Microbiol 51 191 196
    • (2005) Can J Microbiol , vol.51 , pp. 191-196
    • Ramnani, P.1    Singh, R.2    Gupta, R.3
  • 28
    • 0035748508 scopus 로고    scopus 로고
    • Isolation of Thermoanaerobacter keratinophilus sp nov, a novel thermophilic, anaerobic bacterium with keratinolytic activity
    • S Riessen G Antranikian 2001 Isolation of Thermoanaerobacter keratinophilus sp nov, a novel thermophilic, anaerobic bacterium with keratinolytic activity Extremophiles 5 399 408
    • (2001) Extremophiles , vol.5 , pp. 399-408
    • Riessen, S.1    Antranikian, G.2
  • 29
    • 0029860158 scopus 로고    scopus 로고
    • Keratinolytic activity of Aspergillus fumigatus fresenius
    • RMDB Santos AA Firmino CM de Sa CR Felix 1996 Keratinolytic activity of Aspergillus fumigatus fresenius Curr Microbiol 33 364 370
    • (1996) Curr Microbiol , vol.33 , pp. 364-370
    • Rmdb, S.1    Firmino, A.A.2    De Sa, C.M.3    Felix, C.R.4
  • 30
    • 0000722572 scopus 로고
    • Properties of Thermus ruber strains isolated from Icelandic hot springs and DNA:DNA homology of Thermus ruber and Thermus aquaticus
    • RJ Sharp RA Williams 1988 Properties of Thermus ruber strains isolated from Icelandic hot springs and DNA:DNA homology of Thermus ruber and Thermus aquaticus Appl Environ Microbiol 54 2049 2053
    • (1988) Appl Environ Microbiol , vol.54 , pp. 2049-2053
    • Sharp, R.J.1    Williams, R.A.2
  • 31
    • 33749245479 scopus 로고    scopus 로고
    • Decomposition of extremely hard-to-degrade animal proteins by thermophilic bacteria
    • Y Suzuki Y Tsujimoto H Matsui K Watanabe 2006 Decomposition of extremely hard-to-degrade animal proteins by thermophilic bacteria J Biosci Bioeng 102 73 81
    • (2006) J Biosci Bioeng , vol.102 , pp. 73-81
    • Suzuki, Y.1    Tsujimoto, Y.2    Matsui, H.3    Watanabe, K.4
  • 32
    • 0034278342 scopus 로고    scopus 로고
    • Application of a metal switch to aqualysin I, a subtilisin-type bacterial serine protease, to the S3 site residues, ser102 and gly131
    • T Tanaka Y Kikuchi H Matsuzawa T Ohta 2000 Application of a metal switch to aqualysin I, a subtilisin-type bacterial serine protease, to the S3 site residues, ser102 and gly131 Biosci Biotechnol Biochem 64 2008 2011
    • (2000) Biosci Biotechnol Biochem , vol.64 , pp. 2008-2011
    • Tanaka, T.1    Kikuchi, Y.2    Matsuzawa, H.3    Ohta, T.4
  • 33
    • 0028882122 scopus 로고
    • Thermus silvanus sp nov and Thermus chliarophilus sp nov, two new species related to Thermus ruber but with lower growth temperatures
    • S Tenreiro MF Nobre MS da Costa 1995 Thermus silvanus sp nov and Thermus chliarophilus sp nov, two new species related to Thermus ruber but with lower growth temperatures Int J Syst Bacteriol 45 633 639
    • (1995) Int J Syst Bacteriol , vol.45 , pp. 633-639
    • Tenreiro, S.1    Nobre, M.F.2    Da Costa, M.S.3
  • 34
    • 1242292972 scopus 로고    scopus 로고
    • Collagenolytic proteases from bacteria
    • K Watanabe 2004 Collagenolytic proteases from bacteria Appl Microbiol Biotechnol 63 520 526
    • (2004) Appl Microbiol Biotechnol , vol.63 , pp. 520-526
    • Watanabe, K.1
  • 35
    • 0001840538 scopus 로고
    • Evaluation of a bacterial feather fermentation product, feather-lysate, as a feed protein
    • CM Williams CG Lee JD Garlich JCH Shih 1991 Evaluation of a bacterial feather fermentation product, feather-lysate, as a feed protein Poultry Sci 70 85 94
    • (1991) Poultry Sci , vol.70 , pp. 85-94
    • Williams, C.M.1    Lee, C.G.2    Garlich, J.D.3    Shih, J.C.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.