메뉴 건너뛰기




Volumn 7, Issue 2, 2011, Pages

Feather keratin hydrolysis by an aquatic bacterium meiothermus i40 from hot spring water

Author keywords

feather degradation; keratinase; Meiothermus; optimization; Plackett Burman; response surface methodology

Indexed keywords

FEATHER DEGRADATION; KERATINASE; MEIOTHERMUS; PLACKETT-BURMAN; RESPONSE SURFACE METHODOLOGY;

EID: 79953730334     PISSN: 15563758     EISSN: None     Source Type: Journal    
DOI: 10.2202/1556-3758.2201     Document Type: Article
Times cited : (4)

References (62)
  • 1
    • 22144496043 scopus 로고    scopus 로고
    • A biotechnological process for treatment and recycling poultry feathers as a feed ingredient
    • DOI 10.1016/j.biortech.2004.12.026, PII S0960852405000374
    • Bertsch A, Cello N (2005) A biotechnological process for treatment and recycling poultry feathers as a feed ingredient. Bioresource Tech, 96, 1703-1708. (Pubitemid 40980257)
    • (2005) Bioresource Technology , vol.96 , Issue.15 , pp. 1703-1708
    • Bertsch, A.1    Coello, N.2
  • 2
    • 0028883655 scopus 로고
    • Characterization of a keratinolytic serine proteinase from Streptomyces pactum DSM 40530
    • Bockle, B., Galunsky, B. and Muller, R. (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
    • Bockle, B.1    Galunsky, B.2    Muller, R.3
  • 4
    • 0033013666 scopus 로고    scopus 로고
    • Purification and characterization of a keratinolytic serine proteinase from Streptomyces albidoflavus
    • Bressollier, P., Letourneau, F., Urdaci, M. and Verneuil, B. (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
    • 0036740530 scopus 로고    scopus 로고
    • Meiothermus taiwanensis sp. nov., a novel filamentous, thermophilic species isolated in Taiwan
    • Chen, M.Y., Lin, G.H., Lin, Y.T. and Tsay, S.S. (2002) Meiothermus taiwanensis sp. nov., a novel filamentous, thermophilic species isolated in Taiwan. Int J Syst Evol Microbiol, 52, 1647-1654.
    • (2002) Int J Syst Evol Microbiol , vol.52 , pp. 1647-1654
    • Chen, M.Y.1    Lin, G.H.2    Lin, Y.T.3    Tsay, S.S.4
  • 7
    • 0029437916 scopus 로고
    • Production and characterization of a feather degrading Bacillus licheniformis PWD-1
    • Cheng, S.W., Hu, H.M., Shen, S. W., Takagi, H., Asano, M. and Tsai, Y. C. (1995) Production and characterization of a feather degrading Bacillus licheniformis PWD-1. Biosci Biotechnol Biochem, 59, 2239-2243.
    • (1995) Biosci Biotechnol Biochem , vol.59 , pp. 2239-2243
    • Cheng, S.W.1    Hu, H.M.2    Shen, S.W.3    Takagi, H.4    Asano, M.5    Tsai, Y.C.6
  • 8
    • 85010550117 scopus 로고    scopus 로고
    • Effect of feather meal on growth and body composition of the juvenile Pacific white shrimp, Litopenaeus vannamei
    • Cheng, Z.J., Behnke, K.C. and Dominy, W.G. (2002) Effect of feather meal on growth and body composition of the juvenile Pacific white shrimp, Litopenaeus vannamei. J Appl Aquac, 12, 57-69.
    • (2002) J Appl Aquac , vol.12 , pp. 57-69
    • Cheng, Z.J.1    Behnke, K.C.2    Dominy, W.G.3
  • 9
    • 0033021799 scopus 로고    scopus 로고
    • Keratinolytic activity from the broth of a feather-degrading thermophilic Streptomyces thermoviolaceus strain SD8
    • DOI 10.1046/j.1365-2672.1999.00484.x
    • Chitte, R.R., Nalawade, V.K. and Dey, S. (1999) Keratinolytic activity from the broth of a feather-degrading thermophilic Streptomyces thermoviolaceus strain SD8. Lett Appl Microbiol, 28, 131-136. (Pubitemid 29078248)
    • (1999) Letters in Applied Microbiology , vol.28 , Issue.2 , pp. 131-136
    • Chitte, R.R.1    Nalawade, V.K.2    Dey, S.3
  • 10
    • 79958235000 scopus 로고    scopus 로고
    • The effect of process variables for production of cobia (Rachycentron canadum) skin gelatin hydrolysates with antioxidant properties
    • In press
    • Chow, C.J. and Yang, J.I. (2011). The effect of process variables for production of cobia (Rachycentron canadum) skin gelatin hydrolysates with antioxidant properties. Food Biochem (In press).
    • (2011) Food Biochem
    • Chow, C.J.1    Yang, J.I.2
  • 12
    • 0031613817 scopus 로고    scopus 로고
    • An overview of the role and diversity of compatible solutes in bacteria and archaea
    • da Costa, M.S., Santos, H. and Galinski, E.A. (1998) An overview of the role and diversity of compatible solutes in bacteria and archaea. Adv Bioche Eng Biotechno, 61, 117-153.
    • (1998) Adv Bioche Eng Biotechno , vol.61 , pp. 117-153
    • Da Costa, M.S.1    Santos, H.2    Galinski, E.A.3
  • 13
    • 0032898034 scopus 로고    scopus 로고
    • Characterization of glycolipids from Meiothermus spp
    • Ferreira, A. M., Wait, R., Nobre, M. F. and da Costa M. S. (1999) Characterization of glycolipids from Meiothermus spp. Microbiol, 145, 1191-1199.
    • (1999) Microbiol , vol.145 , pp. 1191-1199
    • Ferreira, A.M.1    Wait, R.2    Nobre, M.F.3    Da Costa, M.S.4
  • 14
    • 0029659518 scopus 로고    scopus 로고
    • Keratin degradation by Fervidobacterium pennavorans, a novel thermophilic anaerobic species of the order Thermotogales
    • Friedrich, A. and Antranikian, G. (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.1    Antranikian, G.2
  • 15
    • 0037426295 scopus 로고    scopus 로고
    • Novel alkaline proteases from alkaliphilic bacteria grown on chicken feather
    • DOI 10.1016/S0141-0229(02)00324-1
    • Gessesse, A., Hatti-Kaul, R., Gashe, B.A. and Mattiasson, B. (2003) Novel alkaline proteases from alkalophilic bacteria grown on chicken feather. Enzyme Microb Technol, 32, 519-524. (Pubitemid 36324338)
    • (2003) Enzyme and Microbial Technology , vol.32 , Issue.5 , pp. 519-524
    • Gessesse, A.1    Hatti-Kaul, R.2    Gashe, B.A.3    Mattiasson, B.4
  • 18
    • 31944434558 scopus 로고    scopus 로고
    • Nutritional improvement of feather protein by treatment with microbial keratinase
    • DOI 10.1016/j.anifeedsci.2005.06.002, PII S0377840105002609
    • Grazziotin, A., Pimentel, F.A., de Jong, E.V. and Brandelli, A. (2006) Nutritional improvement of feather protein by treatment with microbial keratinase. Animal Feed Science and Technology 126, 135-144. (Pubitemid 43188007)
    • (2006) Animal Feed Science and Technology , vol.126 , Issue.1-2 , pp. 135-144
    • Grazziotin, A.1    Pimentel, F.A.2    De Jong, E.V.3    Brandelli, A.4
  • 19
    • 32644435175 scopus 로고    scopus 로고
    • Microbial keratinases and their prospective applications: An overview
    • DOI 10.1007/s00253-005-0239-8
    • Gupta, R. and Ramnani, P. (2006) Microbial keratinases and their prospective applications: an overview. Appl Microbiol Biotechnol, 70, 21-33. (Pubitemid 43239500)
    • (2006) Applied Microbiology and Biotechnology , vol.70 , Issue.1 , pp. 21-33
    • Gupta, R.1    Ramnani, P.2
  • 21
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: A user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall, T.A. (1999) BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp Ser, 41, 95-98.
    • (1999) Nucleic Acids Symp ser , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 22
    • 59849114883 scopus 로고    scopus 로고
    • Processing of poultry feathers by alkaline keratin hydrolyzing enzyme from Serratia sp. HPC 1383
    • Khardenavis, A.A., Kapley, A, and Purohit, H.J. (2009) Processing of poultry feathers by alkaline keratin hydrolyzing enzyme from Serratia sp. HPC 1383. Waste Management, 29, 1409-1415.
    • (2009) Waste Management , vol.29 , pp. 1409-1415
    • Khardenavis, A.A.1    Kapley, A.2    Purohit, H.J.3
  • 23
    • 0034794287 scopus 로고    scopus 로고
    • Feather-degrading Bacillus species from poultry waste
    • DOI 10.1016/S0032-9592(01)00206-0, PII S0032959201002060
    • Kim, J.M., Lim, W.J. and Suh, H.J. (2001) Feather-degrading Bacillus species from poultry waste. Process Biochem, 37, 287-291. (Pubitemid 32936619)
    • (2001) Process Biochemistry , vol.37 , Issue.3 , pp. 287-291
    • Kim, J.M.1    Lim, W.J.2    Suh, H.J.3
  • 25
    • 78649637565 scopus 로고    scopus 로고
    • Process optimization for production of antioxidant gelatin hydrolysates from tilapia skin
    • Kuo, J.M., Lee, G.C., Liang, W.S., Yang J.I. (2009) Process optimization for production of antioxidant gelatin hydrolysates from tilapia skin. J. Fish. Soc. Taiwan, 36, 15-38.
    • (2009) J. Fish. Soc. Taiwan , vol.36 , pp. 15-38
    • Kuo, J.M.1    Lee, G.C.2    Liang, W.S.3    Yang, J.I.4
  • 27
    • 0001119066 scopus 로고
    • Processing of feather to maximize its nutritional value for poultry
    • Latshaw, J.D., Musharaf, N. and Retrum, R. (1994) Processing of feather to maximize its nutritional value for poultry. Animal Feed Sci Technol, 47, 179-188.
    • (1994) Animal Feed Sci Technol , vol.47 , pp. 179-188
    • Latshaw, J.D.1    Musharaf, N.2    Retrum, R.3
  • 31
    • 0037298784 scopus 로고    scopus 로고
    • Isolation and characterization of a new keratinolytic Bacillus licheniformis strain
    • DOI 10.1023/A:1022576826372
    • Manczinger, L., Rozs, M., Vagvolgyi, C. and Kevei, F. (2003) Isolation and characterization of a new keratinolytic Bacillus licheniformis strain. World J Microbiol Biotechnol, 19, 35-39 (Pubitemid 36357485)
    • (2003) World Journal of Microbiology and Biotechnology , vol.19 , Issue.1 , pp. 35-39
    • Manczinger, L.1    Rozs, M.2    Vagvolgyi, Cs.3    Kevei, F.4
  • 32
    • 28844433303 scopus 로고    scopus 로고
    • Influence of plasticizers on the water sorption isotherms and water vapor permeability of chicken feather keratin films
    • DOI 10.1016/j.lwt.2004.12.014, PII S0023643805000095
    • Martelli, S.M., Moore, G., Paes, S.S., Gandolfo, C., and Laurindo, J.B. (2006) Influence of plasticizers on the water sorption isotherms and water vapor permeability of chicken feather keratin films. LWT Food Sci Technol, 39, 292-301. (Pubitemid 41774216)
    • (2006) LWT - Food Science and Technology , vol.39 , Issue.3 , pp. 292-301
    • Maria Martelli, S.1    Moore, G.2    Silva Paes, S.3    Gandolfo, C.4    Laurindo, J.B.5
  • 33
    • 0035226832 scopus 로고    scopus 로고
    • Indicators of nutritional value of hydrolyzed feather meal
    • Moritz, J.S. and Latshaw, J.D. (2001) Indicators of nutritional value of hydrolyzed feather meal. Poultry Sci, 80, 79-86. (Pubitemid 33659804)
    • (2001) Poultry Science , vol.80 , Issue.1 , pp. 79-86
    • Moritz, J.S.1    Latshaw, J.D.2
  • 34
    • 0036428747 scopus 로고    scopus 로고
    • Native-feather degradation by Fervidobacterium islandicum AW-1, a newly isolated keratinase-producing thermophilic anaerobe
    • DOI 10.1007/s00203-002-0489-0
    • Nam, G.W., Lee, D.W., Lee, H.S., Lee, N.J., Kim, B.C., Choe, E.A., Hwang, J.K., Suhartono, M.T. and Pyun, Y.R. (2002) Native feather degradation by Fervidobacterium islandicum AW-1, a newly isolated keratinase-producing thermophilic anaerobe. Arch Microbiol, 178, 538-547. (Pubitemid 35340987)
    • (2002) Archives of Microbiology , vol.178 , Issue.6 , pp. 538-547
    • Nam, G.-W.1    Lee, D.-W.2    Lee, H.-S.3    Lee, N.-J.4    Kim, B.-C.5    Choe, E.-A.6    Hwang, J.-K.7    Suhartono, M.T.8    Pyun, Y.-R.9
  • 35
    • 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
    • Nobre, M.F., Truper, H.G. and da Costa, M.S. (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) Thermus. Int J Syst Bacteriol , vol.46 , pp. 604-606
    • Nobre, M.F.1    Truper, H.G.2    Da Costa, M.S.3
  • 36
    • 0043163529 scopus 로고    scopus 로고
    • Keratinase in starter diets improves growth of broiler chicks
    • Odetallah, N.H., Wang, J.J., Garlich, J.D. and Shih, J.C.H. (2003) Keratinase in starter diets improves growth of broiler chicks. Poultry Science, 82, 664-670. (Pubitemid 38641945)
    • (2003) Poultry Science , vol.82 , Issue.4 , pp. 664-670
    • Odetallah, N.H.1    Wang, J.J.2    Garlich, J.D.3    Shih, J.C.H.4
  • 37
    • 0032192726 scopus 로고    scopus 로고
    • A review: Potentials for biotechnological applications of keratin-degrading microorganisms and their enzymes for nutritional improvement of feathers and other keratins as livestock feed resources
    • DOI 10.1016/S0960-8524(98)00033-9, PII S0960852498000339
    • Onifade, A.A., Al-Sane, N.A., Musallam, A.A. and Al-Zarban, S. (1998) A review: potentials for biotechnological applications of keratin degrading microorganisms and their enzymes for nutritional improvement of feathers and other keratins as livestock feed resources. Bioresource Technol 66, 1-11. (Pubitemid 28353644)
    • (1998) Bioresource Technology , vol.66 , Issue.1 , pp. 1-11
    • Onifade, A.A.1    Al-Sane, N.A.2    Al-Musallam, A.A.3    Al-Zarban, S.4
  • 38
    • 0030203863 scopus 로고    scopus 로고
    • TreeView: An application to display phylogenetic trees on personal computers
    • Page, R.D. (1996) TreeView: an application to display phylogenetic trees on personal computers. Comput Appl Biosc,i 12, 357-358.
    • (1996) Comput Appl Biosc,i , vol.12 , pp. 357-358
    • Page, R.D.1
  • 40
    • 53549104987 scopus 로고    scopus 로고
    • Biodegradation of poultry waste for the production of mosquitocidal toxins
    • Poopathi, S. and Abidha, S. (2008) Biodegradation of poultry waste for the production of mosquitocidal toxins. International Biodeterioration & Biodegradation, 62, 479-482.
    • (2008) International Biodeterioration & Biodegradation , vol.62 , pp. 479-482
    • Poopathi, S.1    Abidha, S.2
  • 41
    • 0001098191 scopus 로고
    • Effect of growth temperature on the lipid composition of two strains of Thermus sp
    • Prado, A., da Costa, M.S. and Madeira, V.M.C. (1988) Effect of growth temperature on the lipid composition of two strains of Thermus sp. J Gen Microbiol, 134, 1653-1660.
    • (1988) J Gen Microbiol , vol.134 , pp. 1653-1660
    • Prado, A.1    Da Costa, M.S.2    Madeira, V.M.C.3
  • 43
    • 0015131695 scopus 로고
    • Effect of growth temperature on the lipid composition of Thermus aquaticus
    • Ray, P.H., White, D.C. and Brock, T. D. (1971) Effect of growth temperature on the lipid composition of Thermus aquaticus. J Bacteriol, 108, 227-235.
    • (1971) J Bacteriol , vol.108 , pp. 227-235
    • Ray, P.H.1    White, D.C.2    Brock, T.D.3
  • 44
    • 0035748508 scopus 로고    scopus 로고
    • Isolation of Thermoanaerobacter keratinophilus sp. nov., a novel thermophilic, anaerobic bacterium with keratinolytic activity
    • DOI 10.1007/s007920100209
    • Riessen, S. and Antranikian, G. (2001) Isolation of Thermoanaerobacter keratinophilus sp. nov., a novel thermophilic, anaerobic bacterium with keratinolytic activity. Extremophiles, 5, 399-408. (Pubitemid 33737390)
    • (2001) Extremophiles , vol.5 , Issue.6 , pp. 399-408
    • Riessen, S.1    Antranikian, G.2
  • 45
    • 0023375195 scopus 로고
    • The neighbour-joining method: A new method for reconstructing phylogenetic trees
    • Saitou, N. and Nei, M. (1987) The neighbour-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol, 4, 406-425.
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 46
    • 0029860158 scopus 로고    scopus 로고
    • Keratinolytic activity of Aspergillus fumigatus fresenius
    • DOI 10.1007/s002849900129
    • Santos, R.M.D.B., Firmino, A., Sà, C. and Felix, C. (1996) Keratinolytic activity of Aspergillus fumigatus fresenius. Curr. Microbiol, 33, 364-370. (Pubitemid 26399206)
    • (1996) Current Microbiology , vol.33 , Issue.6 , pp. 364-370
    • Santos, R.M.D.B.1    Firmino, A.A.P.2    De Sa, C.M.3    Felix, C.R.4
  • 47
    • 0031785262 scopus 로고    scopus 로고
    • Activation and thermostabilization effects of cyclic 2,3- diphosphoglycerate on enzymes from the hyperthermophilic Methanopyrus kandleri
    • DOI 10.1007/s002030050669
    • Shima, S., Herault, D.A., Berkessel, A. and Thauer, R.K. (1998) Activation and thermostabilization effects of cyclic 2,3-diphosphoglycerate on enzymes from the hyperthermophilic Methanopyrus kandleri. Arch Microbiol 170, 469-472. (Pubitemid 28523653)
    • (1998) Archives of Microbiology , vol.170 , Issue.6 , pp. 469-472
    • Shima, S.1    Herault, D.A.2    Berkessel, A.3    Thauer, R.K.4
  • 48
    • 33749245479 scopus 로고    scopus 로고
    • Decomposition of extremely hard-to-degrade animal proteins by thermophilic bacteria
    • DOI 10.1263/jbb.102.73, PII S1389172306706326
    • Suzuki, Y., Tsujimoto, Y., Matsui, H., and Watanabe, K. (2006) Decomposition of extremely hard-to-degrade animal proteins by thermophilic bacteria. Journal of Bioscience and Bioengineering, 102, 73-81. (Pubitemid 44486913)
    • (2006) Journal of Bioscience and Bioengineering , vol.102 , Issue.2 , pp. 73-81
    • Suzuki, Y.1    Tsujimoto, Y.2    Matsui, H.3    Watanabe, K.4
  • 49
    • 0028882122 scopus 로고
    • Thermus silvanus sp. nov. and Thermus chliarophilus sp. nov., two new species related to Thermus ruber but with lower growth temperatures
    • Tenreiro, S., Nobre, M.F. and da Costa, M.S. (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
  • 50
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • DOI 10.1093/nar/25.24.4876
    • Thompson, J.D., Gibson, T.J., Plewniak, F., Jeanmougin, F. and Higgins, D.G. (1997) The CLUSTAL X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res, 25, 4876-4882. (Pubitemid 28022245)
    • (1997) Nucleic Acids Research , vol.25 , Issue.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 51
    • 3843111064 scopus 로고    scopus 로고
    • Characterization of a protease of a feather-degrading Microbacterium species
    • DOI 10.1111/j.1472-765X.2004.01558.x
    • Thys, R.C.S., Lucas, F.S., Riffel, A., Heeb, P. and Brandelli, A. (2004) Characterization of a protease of a feather-degrading Microbacterium species. Lett Appl Microbiol, 39, 181-186. (Pubitemid 39043648)
    • (2004) Letters in Applied Microbiology , vol.39 , Issue.2 , pp. 181-186
    • Thys, R.C.S.1    Lucas, F.S.2    Riffel, A.3    Heeb, P.4    Brandelli, A.5
  • 52
    • 0036371019 scopus 로고    scopus 로고
    • Growth performance, carcass characteristics, nutrient digestibility and fecal odorous compounds in growing-finishing pigs fed diets containing hydrolyzed feather meal
    • Van Heugten, E. and Van Kempen, T.A.T.G. (2002) Growth performance, carcass characteristics, nutrient digestibility and fecal odorous compounds in growing-finishing pigs fed diets containing hydrolyzed feather meal. J Anim Sci, 80, 171-178.
    • (2002) J Anim Sci , vol.80 , pp. 171-178
    • Van Heugten, E.1    Van Kempen, T.A.T.G.2
  • 53
    • 0030884118 scopus 로고    scopus 로고
    • Characterization of novel long-chain 1,2-diols in Thermus species and demonstration that Thermus strains contain both glycerol-linked and diol- linked glycolipids
    • Wait, R., Carreto, L., Nobre, M.F., Ferreira, A.M. and da Costa, M.S. (1997) Characterization of novel long-chain 1,2-diols in Thermus species and demonstration that Thermus strains contain both glycerol-linked and diol-linked glycolipids. J Bacteriol 179, 6154-6162. (Pubitemid 27419043)
    • (1997) Journal of Bacteriology , vol.179 , Issue.19 , pp. 6154-6162
    • Wait, R.1    Carreto, L.2    Nobre, M.F.3    Ferreira, A.M.4    Da Costa, M.S.5
  • 54
    • 14844287025 scopus 로고    scopus 로고
    • Development of an asporogenic Bacillus licheniformis for the production of keratinase
    • DOI 10.1111/j.1365-2672.2004.02515.x
    • Wang, J.J., Greenhut, W.B. and Shih, J.C.H. (2005) Development of an asporogenic Bacillus licheniformis for the production of keratinase. J Appl Microbiol, 98, 761-767. (Pubitemid 40349303)
    • (2005) Journal of Applied Microbiology , vol.98 , Issue.3 , pp. 761-767
    • Wang, J.-J.1    Greenhut, W.B.2    Shih, J.C.H.3
  • 55
    • 0032808211 scopus 로고    scopus 로고
    • Fermentation production of keratinase from Bacillus licheniformis PWD-1 and a recombinant B. subtilis FDB-29
    • DOI 10.1038/sj.jim.2900667
    • Wang, J.J. and Shih, J.C.H. (1999) Fermentation production of keratinase from Bacillus licheniformis PWD-1 and a recombinant B. subtilis FDB-29. J Ind Microbiol Biotechnol, 22, 608-616. (Pubitemid 29381201)
    • (1999) Journal of Industrial Microbiology and Biotechnology , vol.22 , Issue.6 , pp. 608-616
    • Wang, J.-J.1    Shih, J.C.H.2
  • 57
    • 0001912051 scopus 로고
    • The genus Thermus and related microorganisms
    • ed. Balows, A., Truper, H.G., Dworkin M., Harder, W. and Schleifer, K. H., New York: Springer
    • William, R.A.D. and da Costa, M.S. (1992). The genus Thermus and related microorganisms. In The Prokaryotes ed. Balows, A., Truper, H.G., Dworkin, M., Harder, W. and Schleifer, K. H. pp. 3745-3753. New York: Springer.
    • (1992) The Prokaryotes , pp. 3745-3753
    • William, R.A.D.1    Da Costa, M.S.2
  • 58
    • 0036795411 scopus 로고    scopus 로고
    • Application of statistically based experimental designs for the optimization of exo-polysaccharide production by Cordyceps militaris NG3
    • Xu, C.P., Kim, S.W., Hwang, H. J. and Yun, J. W. (2002) Application of statistically based experimental designs for the optimization of exo-polysaccharide production by Cordyceps militaris NG3. Biotechnol Appl Biochem, 36, 127-131.
    • (2002) Biotechnol Appl Biochem , vol.36 , pp. 127-131
    • Xu, C.P.1    Kim, S.W.2    Hwang, H.J.3    Yun, J.W.4
  • 60
    • 33747129752 scopus 로고    scopus 로고
    • Structural elucidation of phosphoglycolipids from strains of the bacterial thermophiles Thermus and Meiothermus
    • DOI 10.1194/jlr.M600034-JLR200
    • Yang, Y.L., Yang, F.L., Jao, S.C., Chen, M.Y., Tsay, S.S., Zou, W. and Wu S.H. (2006) Structural elucidation of phosphoglycolipids from strains of the bacterial thermophiles Thermus and Meiothermus. J Lipid Res, 47, 1823-1832. (Pubitemid 44222833)
    • (2006) Journal of Lipid Research , vol.47 , Issue.8 , pp. 1823-1832
    • Yang, Y.-L.1    Yang, F.-L.2    Jao, S.-C.3    Chen, M.-Y.4    Tsay, S.-S.5    Zou, W.6    Wu, S.-H.7
  • 61
    • 0034761352 scopus 로고    scopus 로고
    • Development of a method for assessing haze-active protein in beer by dye binding
    • Yang, J.I. and Siebert, K.J. (2001) Development of a method for assessing haze-active protein in beer by dye binding. J Am Soc Brew Chem 59, 172-182. (Pubitemid 33037505)
    • (2001) Journal of the American Society of Brewing Chemists , vol.59 , Issue.4 , pp. 172-182
    • Yang, J.I.1    Siebert, K.J.2
  • 62
    • 69249230831 scopus 로고    scopus 로고
    • Process for production of tilapia retorted skin gelatin hydrolysates with optimized antioxidative properties
    • Yang, J.I., Liang, W.S., Chow, C.J. and Siebert, K.J. (2009) Process for production of tilapia retorted skin gelatin hydrolysates with optimized antioxidative properties. Process Biochem, 44, 1152-1157.
    • (2009) Process Biochem , vol.44 , pp. 1152-1157
    • Yang, J.I.1    Liang, W.S.2    Chow, C.J.3    Siebert, K.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.