Production and characterization of thermostable metallo-keratinase from newly isolated Bacillus subtilis NRC 3

Novel keratinolytic enzyme (32kDa) secreted by a newly isolated Bacillus strain (Bacillus subtilis NRC3) cultivated in medium containing chicken feather meal was purified and partially characterized in a set of biochemical assays. The purification was carried out by applying a protocol of two succes...

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Published inInternational journal of biological macromolecules Vol. 55; pp. 169 - 175
Main Authors Tork, Sanaa E., Shahein, Yasser E., El-Hakim, Amr E., Abdel-Aty, Azza M., Aly, Magda M.
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.04.2013
Subjects
16S rDNA
Bacillus subtilis
Bacillus subtilis - classification
Bacillus subtilis - genetics
Bacillus subtilis - isolation & purification
Bacillus subtilis - metabolism
barium
calcium
cation exchange chromatography
cations
chickens
Enzyme Activation
enzyme activity
Enzyme Stability
enzymes
feather meal
feathers
gel chromatography
Hydrogen-Ion Concentration
Hydrolysis
keratin
Kinetics
magnesium
Metallo-keratinase
PCR-based RFLP
Peptide Hydrolases - biosynthesis
Peptide Hydrolases - chemistry
Peptide Hydrolases - isolation & purification
Peptide Hydrolases - metabolism
Phylogeny
potassium
RNA, Ribosomal, 16S
SDS-PAGE
sodium
Temperature
thermal stability
Thermostability
Thermostability
SDS-PAGE
PCR-based RFLP
16S rDNA
Metallo-keratinase
Bacillus subtilis
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Abstract Novel keratinolytic enzyme (32kDa) secreted by a newly isolated Bacillus strain (Bacillus subtilis NRC3) cultivated in medium containing chicken feather meal was purified and partially characterized in a set of biochemical assays. The purification was carried out by applying a protocol of two successive chromatographic steps; cation exchange chromatography on CM-cellulose and gel filtration on sephadex G-75 columns. The purified enzyme showed a specific activity of 5233units/mg protein against 169units/mg protein for crude extract with 31 fold purification. The enzymatic activity of the purified keratinolytic enzyme stimulated by Na+, K+, Mg2+, Ba2+, Ca2+, and inhibited by entire tested cations and metalloproteinase inhibitors, indicating that it belongs to metallo-keratinase enzymes. The optimum pH and temperature for the purified enzyme were (7.5, 8.0) and (50, 40°C) when using keratin azure and azocasein as substrates, respectively. The purified enzyme was highly stable at broad pH and temperature ranged (5–10) and (20–60°C), respectively. These results suggest that this keratinase may be a useful alternative and ecofriendly route for handling the abundant amount of waste feathers.
AbstractList Novel keratinolytic enzyme (32kDa) secreted by a newly isolated Bacillus strain (Bacillus subtilis NRC3) cultivated in medium containing chicken feather meal was purified and partially characterized in a set of biochemical assays. The purification was carried out by applying a protocol of two successive chromatographic steps; cation exchange chromatography on CM-cellulose and gel filtration on sephadex G-75 columns. The purified enzyme showed a specific activity of 5233units/mg protein against 169units/mg protein for crude extract with 31 fold purification. The enzymatic activity of the purified keratinolytic enzyme stimulated by Na(+), K(+), Mg(2+), Ba(2+), Ca(2+), and inhibited by entire tested cations and metalloproteinase inhibitors, indicating that it belongs to metallo-keratinase enzymes. The optimum pH and temperature for the purified enzyme were (7.5, 8.0) and (50, 40°C) when using keratin azure and azocasein as substrates, respectively. The purified enzyme was highly stable at broad pH and temperature ranged (5-10) and (20-60°C), respectively. These results suggest that this keratinase may be a useful alternative and ecofriendly route for handling the abundant amount of waste feathers.
Novel keratinolytic enzyme (32kDa) secreted by a newly isolated Bacillus strain (Bacillus subtilis NRC3) cultivated in medium containing chicken feather meal was purified and partially characterized in a set of biochemical assays. The purification was carried out by applying a protocol of two successive chromatographic steps; cation exchange chromatography on CM-cellulose and gel filtration on sephadex G-75 columns. The purified enzyme showed a specific activity of 5233units/mg protein against 169units/mg protein for crude extract with 31 fold purification. The enzymatic activity of the purified keratinolytic enzyme stimulated by Na⁺, K⁺, Mg²⁺, Ba²⁺, Ca²⁺, and inhibited by entire tested cations and metalloproteinase inhibitors, indicating that it belongs to metallo-keratinase enzymes. The optimum pH and temperature for the purified enzyme were (7.5, 8.0) and (50, 40°C) when using keratin azure and azocasein as substrates, respectively. The purified enzyme was highly stable at broad pH and temperature ranged (5–10) and (20–60°C), respectively. These results suggest that this keratinase may be a useful alternative and ecofriendly route for handling the abundant amount of waste feathers.
Novel keratinolytic enzyme (32kDa) secreted by a newly isolated Bacillus strain (Bacillus subtilis NRC3) cultivated in medium containing chicken feather meal was purified and partially characterized in a set of biochemical assays. The purification was carried out by applying a protocol of two successive chromatographic steps; cation exchange chromatography on CM-cellulose and gel filtration on sephadex G-75 columns. The purified enzyme showed a specific activity of 5233units/mg protein against 169units/mg protein for crude extract with 31 fold purification. The enzymatic activity of the purified keratinolytic enzyme stimulated by Na+, K+, Mg2+, Ba2+, Ca2+, and inhibited by entire tested cations and metalloproteinase inhibitors, indicating that it belongs to metallo-keratinase enzymes. The optimum pH and temperature for the purified enzyme were (7.5, 8.0) and (50, 40°C) when using keratin azure and azocasein as substrates, respectively. The purified enzyme was highly stable at broad pH and temperature ranged (5–10) and (20–60°C), respectively. These results suggest that this keratinase may be a useful alternative and ecofriendly route for handling the abundant amount of waste feathers.
Author Shahein, Yasser E.
Abdel-Aty, Azza M.
El-Hakim, Amr E.
Tork, Sanaa E.
Aly, Magda M.
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  givenname: Amr E.
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  givenname: Azza M.
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Cites_doi 10.1086/379664
10.1007/s00253-005-0239-8
10.3923/ajbkr.2010.1.13
10.1007/s00203-003-0525-8
10.1016/j.biortech.2006.05.047
10.1007/s002530050008
10.1128/AEM.71.7.3420-3426.2005
10.1016/S0141-0229(02)00324-1
10.1007/s00253-009-2398-5
10.1038/227680a0
10.3382/ps.0700085
10.1128/AEM.58.10.3271-3275.1992
10.1023/A:1011075707553
10.1046/j.1365-2672.1999.00484.x
10.1111/j.1365-2672.2006.03080.x
10.1111/j.1574-6968.2001.tb10951.x
10.1016/0003-2697(81)90175-5
10.1016/j.biortech.2004.12.026
10.1023/A:1016341702908
10.1016/0003-2697(76)90527-3
10.1016/j.procbio.2004.09.006
10.1111/j.1570-7458.1990.tb01400.x
10.1042/BA20030228
10.1128/AEM.56.6.1509-1515.1990
10.1007/s007920050130
10.1016/j.biortech.2006.05.003
10.1128/AEM.61.10.3705-3710.1995
10.1128/jb.173.2.697-703.1991
10.1007/s007920100239
10.1016/S0032-9592(01)00206-0
10.1016/S0960-8524(02)00177-3
10.1007/s00253-005-1993-3
10.1128/AEM.71.1.594-596.2005
10.1007/s11274-008-9782-7
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Keywords Thermostability
SDS-PAGE
PCR-based RFLP
16S rDNA
Metallo-keratinase
Bacillus subtilis
Language English
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References Kluskens, Voorhorst, Siezen, Schwerdtfeger, Antranikian, van der Oost (bib0070) 2002; 6
Gradišar, Friedrich, Križaj, Jerala (bib0025) 2005; 71
Ramnani, Gupta (bib0060) 2004; 40
Brandelli, Daroit, Riffel (bib0100) 2010; 85
Macedo, da Silva, Gava, Driemeier, Henriques, Termignoni (bib0145) 2005; 71
Böckle, Galunski, Müller (bib0035) 1995; 61
Zouari, Hmidet, Haddar, Kanoun, Nasri (bib0170) 2010; 162
Williams, Richter, Mackenzie, Shih (bib0030) 1990; 56
Chitte, Nalawade, Dey (bib0040) 1999; 28
Lin, Lee, Casale, Shih (bib0120) 1992; 58
El-Refai, AbdelNaby, Gaballa, El-Araby, Abdel Fattah (bib0165) 2005; 40
Gradisar, Kern, Friedrich (bib0010) 2000; 53
Williams, Lee, Garlich, Shih (bib0005) 1991; 70
Kim, Lim, Suh (bib0140) 2001; 37
Suntornsuk, Suntornsuk (bib0055) 2003; 86
Bradford (bib0135) 1976; 72
Weisberg, Barns, Pelletier, Lane (bib0110) 1991; 173
Balaji, Kumar, Karthikeyan (bib0180) 2008; 24
Nilegaonkar, Zambare, Kanekar, Dhakephalkar, Sarnaik (bib0065) 2007; 98
Rozs, Manczinger, Vagvolgyi, Kevei (bib0155) 2001; 205
Yoshioka, Miwa, Horii, Takata, Yokoyama, Nishizawa (bib0090) 2007; 102
Liu (bib0105) 1984
Tork, Aly, Nawar (bib0080) 2010; 2
Doi, Shibata, Matoba (bib0130) 1981; 118
Noronha, Lime, Sá, Felix (bib0045) 2002; 18
Anbu, Gopinath, Hilda, Lakshmipriya, Annadurai (bib0050) 2007; 98
Bertsch, Coello (bib0015) 2005; 96
Langeveld, Wang, van de Wiel, Shih, Garssen, Bossers, Shih (bib0085) 2003; 188
Bálint, Bagi, Rákhely, Perei, Kovács (bib0020) 2005; 69
Gessesse, Hatti-Kaul, Gashe, Mattiasson (bib0160) 2003; 32
Lemos, Campos, Silva, Xavier-Filho (bib0115) 1990; 56
Gupta, Ramnani (bib0095) 2006; 70
Riffel, Lucas, Heeb, Brandelli (bib0075) 2003; 179
Laemmli (bib0125) 1970; 227
Takami, Nogi, Horikoshi (bib0150) 1999; 3
Suh, Lee (bib0175) 2001; 20
Suh (10.1016/j.ijbiomac.2013.01.002_bib0175) 2001; 20
Laemmli (10.1016/j.ijbiomac.2013.01.002_bib0125) 1970; 227
Anbu (10.1016/j.ijbiomac.2013.01.002_bib0050) 2007; 98
Brandelli (10.1016/j.ijbiomac.2013.01.002_bib0100) 2010; 85
Liu (10.1016/j.ijbiomac.2013.01.002_bib0105) 1984
Nilegaonkar (10.1016/j.ijbiomac.2013.01.002_bib0065) 2007; 98
Balaji (10.1016/j.ijbiomac.2013.01.002_bib0180) 2008; 24
Gradišar (10.1016/j.ijbiomac.2013.01.002_bib0025) 2005; 71
Rozs (10.1016/j.ijbiomac.2013.01.002_bib0155) 2001; 205
Gessesse (10.1016/j.ijbiomac.2013.01.002_bib0160) 2003; 32
Yoshioka (10.1016/j.ijbiomac.2013.01.002_bib0090) 2007; 102
Weisberg (10.1016/j.ijbiomac.2013.01.002_bib0110) 1991; 173
Lemos (10.1016/j.ijbiomac.2013.01.002_bib0115) 1990; 56
Bradford (10.1016/j.ijbiomac.2013.01.002_bib0135) 1976; 72
Kluskens (10.1016/j.ijbiomac.2013.01.002_bib0070) 2002; 6
Suntornsuk (10.1016/j.ijbiomac.2013.01.002_bib0055) 2003; 86
Bálint (10.1016/j.ijbiomac.2013.01.002_bib0020) 2005; 69
Lin (10.1016/j.ijbiomac.2013.01.002_bib0120) 1992; 58
Williams (10.1016/j.ijbiomac.2013.01.002_bib0005) 1991; 70
Zouari (10.1016/j.ijbiomac.2013.01.002_bib0170) 2010; 162
Macedo (10.1016/j.ijbiomac.2013.01.002_bib0145) 2005; 71
Ramnani (10.1016/j.ijbiomac.2013.01.002_bib0060) 2004; 40
Kim (10.1016/j.ijbiomac.2013.01.002_bib0140) 2001; 37
Bertsch (10.1016/j.ijbiomac.2013.01.002_bib0015) 2005; 96
Tork (10.1016/j.ijbiomac.2013.01.002_bib0080) 2010; 2
Riffel (10.1016/j.ijbiomac.2013.01.002_bib0075) 2003; 179
Chitte (10.1016/j.ijbiomac.2013.01.002_bib0040) 1999; 28
Williams (10.1016/j.ijbiomac.2013.01.002_bib0030) 1990; 56
El-Refai (10.1016/j.ijbiomac.2013.01.002_bib0165) 2005; 40
Gupta (10.1016/j.ijbiomac.2013.01.002_bib0095) 2006; 70
Doi (10.1016/j.ijbiomac.2013.01.002_bib0130) 1981; 118
Noronha (10.1016/j.ijbiomac.2013.01.002_bib0045) 2002; 18
Gradisar (10.1016/j.ijbiomac.2013.01.002_bib0010) 2000; 53
Takami (10.1016/j.ijbiomac.2013.01.002_bib0150) 1999; 3
Böckle (10.1016/j.ijbiomac.2013.01.002_bib0035) 1995; 61
Langeveld (10.1016/j.ijbiomac.2013.01.002_bib0085) 2003; 188
References_xml – volume: 24
  start-page: 2741
  year: 2008
  end-page: 2745
  ident: bib0180
  publication-title: World Journal of Microbiology and Biotechnology
  contributor:
    fullname: Karthikeyan
– volume: 6
  start-page: 185
  year: 2002
  end-page: 194
  ident: bib0070
  publication-title: Extremophiles
  contributor:
    fullname: van der Oost
– year: 1984
  ident: bib0105
  article-title: Bacillus and cocci
  publication-title: Bergey's Manual of Systematic Bacteriology
  contributor:
    fullname: Liu
– volume: 118
  start-page: 173
  year: 1981
  end-page: 184
  ident: bib0130
  publication-title: Analytical Biochemistry
  contributor:
    fullname: Matoba
– volume: 28
  start-page: 131
  year: 1999
  end-page: 136
  ident: bib0040
  publication-title: Letters in Applied Microbiology
  contributor:
    fullname: Dey
– volume: 2
  start-page: 1
  year: 2010
  end-page: 13
  ident: bib0080
  publication-title: Asian Journal of Biotechnology
  contributor:
    fullname: Nawar
– volume: 227
  start-page: 680
  year: 1970
  end-page: 685
  ident: bib0125
  publication-title: Nature
  contributor:
    fullname: Laemmli
– volume: 61
  start-page: 3705
  year: 1995
  end-page: 3710
  ident: bib0035
  publication-title: Applied and Environment Microbiology
  contributor:
    fullname: Müller
– volume: 53
  start-page: 196
  year: 2000
  end-page: 200
  ident: bib0010
  publication-title: Applied Microbiology and Biotechnology
  contributor:
    fullname: Friedrich
– volume: 20
  start-page: 165
  year: 2001
  end-page: 169
  ident: bib0175
  publication-title: Journal of Protein Chemistry
  contributor:
    fullname: Lee
– volume: 40
  start-page: 191
  year: 2004
  end-page: 196
  ident: bib0060
  publication-title: Biotechnology and Applied Biochemistry
  contributor:
    fullname: Gupta
– volume: 37
  start-page: 287
  year: 2001
  end-page: 291
  ident: bib0140
  publication-title: Process Biochemistry
  contributor:
    fullname: Suh
– volume: 40
  start-page: 2325
  year: 2005
  end-page: 2332
  ident: bib0165
  publication-title: Process Biochemistry
  contributor:
    fullname: Abdel Fattah
– volume: 72
  start-page: 248
  year: 1976
  end-page: 254
  ident: bib0135
  publication-title: Analytical Biochemistry
  contributor:
    fullname: Bradford
– volume: 58
  start-page: 3271
  year: 1992
  end-page: 3275
  ident: bib0120
  publication-title: Applied and Environment Microbiology
  contributor:
    fullname: Shih
– volume: 188
  start-page: 1782
  year: 2003
  end-page: 1789
  ident: bib0085
  publication-title: Journal of Infectious Diseases
  contributor:
    fullname: Shih
– volume: 70
  start-page: 21
  year: 2006
  end-page: 33
  ident: bib0095
  publication-title: Applied Microbiology and Biotechnology
  contributor:
    fullname: Ramnani
– volume: 96
  start-page: 1703
  year: 2005
  end-page: 1708
  ident: bib0015
  publication-title: Bioresource Technology
  contributor:
    fullname: Coello
– volume: 56
  start-page: 219
  year: 1990
  end-page: 228.X
  ident: bib0115
  publication-title: Entomologia Experimentia et Applicata
  contributor:
    fullname: Xavier-Filho
– volume: 98
  start-page: 1298
  year: 2007
  end-page: 1303
  ident: bib0050
  publication-title: Bioresource Technology
  contributor:
    fullname: Annadurai
– volume: 70
  start-page: 85
  year: 1991
  end-page: 94
  ident: bib0005
  publication-title: Poultry Science
  contributor:
    fullname: Shih
– volume: 179
  start-page: 258
  year: 2003
  end-page: 265
  ident: bib0075
  publication-title: Archives of Microbiology
  contributor:
    fullname: Brandelli
– volume: 102
  start-page: 509
  year: 2007
  end-page: 515
  ident: bib0090
  publication-title: Journal of Applied Microbiology
  contributor:
    fullname: Nishizawa
– volume: 71
  start-page: 3420
  year: 2005
  end-page: 3426
  ident: bib0025
  publication-title: Applied and Environment Microbiology
  contributor:
    fullname: Jerala
– volume: 56
  start-page: 1509
  year: 1990
  end-page: 1515
  ident: bib0030
  publication-title: Applied and Environment Microbiology
  contributor:
    fullname: Shih
– volume: 71
  start-page: 594
  year: 2005
  end-page: 596
  ident: bib0145
  publication-title: Applied and Environment Microbiology
  contributor:
    fullname: Termignoni
– volume: 3
  start-page: 293
  year: 1999
  end-page: 296
  ident: bib0150
  publication-title: Extremophiles
  contributor:
    fullname: Horikoshi
– volume: 205
  start-page: 221
  year: 2001
  end-page: 224
  ident: bib0155
  publication-title: FEMS Microbiology Letters
  contributor:
    fullname: Kevei
– volume: 86
  start-page: 239
  year: 2003
  end-page: 243
  ident: bib0055
  publication-title: Bioresource Technology
  contributor:
    fullname: Suntornsuk
– volume: 98
  start-page: 1238
  year: 2007
  end-page: 1245
  ident: bib0065
  publication-title: Bioresource Technology
  contributor:
    fullname: Sarnaik
– volume: 69
  start-page: 404
  year: 2005
  end-page: 410
  ident: bib0020
  publication-title: Applied Microbiology and Biotechnology
  contributor:
    fullname: Kovács
– volume: 18
  start-page: 563
  year: 2002
  end-page: 568
  ident: bib0045
  publication-title: Journal of Microbiology and Biotechnology
  contributor:
    fullname: Felix
– volume: 162
  start-page: 329
  year: 2010
  end-page: 344
  ident: bib0170
  publication-title: Applied Microbiology and Biotechnology
  contributor:
    fullname: Nasri
– volume: 85
  start-page: 1735
  year: 2010
  end-page: 1750
  ident: bib0100
  publication-title: Applied Microbiology and Biotechnology
  contributor:
    fullname: Riffel
– volume: 173
  start-page: 697
  year: 1991
  end-page: 703
  ident: bib0110
  publication-title: Journal of Bacteriology
  contributor:
    fullname: Lane
– volume: 32
  start-page: 519
  year: 2003
  end-page: 524
  ident: bib0160
  publication-title: Enzyme and Microbial Technology
  contributor:
    fullname: Mattiasson
– volume: 188
  start-page: 1782
  issue: 11
  year: 2003
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0085
  publication-title: Journal of Infectious Diseases
  doi: 10.1086/379664
  contributor:
    fullname: Langeveld
– volume: 70
  start-page: 21
  issue: 1
  year: 2006
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0095
  publication-title: Applied Microbiology and Biotechnology
  doi: 10.1007/s00253-005-0239-8
  contributor:
    fullname: Gupta
– volume: 2
  start-page: 1
  issue: 1
  year: 2010
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0080
  publication-title: Asian Journal of Biotechnology
  doi: 10.3923/ajbkr.2010.1.13
  contributor:
    fullname: Tork
– volume: 179
  start-page: 258
  issue: 4
  year: 2003
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0075
  publication-title: Archives of Microbiology
  doi: 10.1007/s00203-003-0525-8
  contributor:
    fullname: Riffel
– volume: 98
  start-page: 1298
  year: 2007
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0050
  publication-title: Bioresource Technology
  doi: 10.1016/j.biortech.2006.05.047
  contributor:
    fullname: Anbu
– volume: 53
  start-page: 196
  year: 2000
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0010
  publication-title: Applied Microbiology and Biotechnology
  doi: 10.1007/s002530050008
  contributor:
    fullname: Gradisar
– volume: 71
  start-page: 3420
  issue: 7
  year: 2005
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0025
  publication-title: Applied and Environment Microbiology
  doi: 10.1128/AEM.71.7.3420-3426.2005
  contributor:
    fullname: Gradišar
– volume: 32
  start-page: 519
  issue: 5
  year: 2003
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0160
  publication-title: Enzyme and Microbial Technology
  doi: 10.1016/S0141-0229(02)00324-1
  contributor:
    fullname: Gessesse
– volume: 85
  start-page: 1735
  issue: 6
  year: 2010
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0100
  publication-title: Applied Microbiology and Biotechnology
  doi: 10.1007/s00253-009-2398-5
  contributor:
    fullname: Brandelli
– volume: 227
  start-page: 680
  year: 1970
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0125
  publication-title: Nature
  doi: 10.1038/227680a0
  contributor:
    fullname: Laemmli
– volume: 70
  start-page: 85
  issue: 1
  year: 1991
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0005
  publication-title: Poultry Science
  doi: 10.3382/ps.0700085
  contributor:
    fullname: Williams
– volume: 58
  start-page: 3271
  year: 1992
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0120
  publication-title: Applied and Environment Microbiology
  doi: 10.1128/AEM.58.10.3271-3275.1992
  contributor:
    fullname: Lin
– volume: 20
  start-page: 165
  issue: 2
  year: 2001
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0175
  publication-title: Journal of Protein Chemistry
  doi: 10.1023/A:1011075707553
  contributor:
    fullname: Suh
– volume: 28
  start-page: 131
  year: 1999
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0040
  publication-title: Letters in Applied Microbiology
  doi: 10.1046/j.1365-2672.1999.00484.x
  contributor:
    fullname: Chitte
– volume: 102
  start-page: 509
  year: 2007
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0090
  publication-title: Journal of Applied Microbiology
  doi: 10.1111/j.1365-2672.2006.03080.x
  contributor:
    fullname: Yoshioka
– volume: 205
  start-page: 221
  issue: 2
  year: 2001
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0155
  publication-title: FEMS Microbiology Letters
  doi: 10.1111/j.1574-6968.2001.tb10951.x
  contributor:
    fullname: Rozs
– volume: 118
  start-page: 173
  issue: 1
  year: 1981
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0130
  publication-title: Analytical Biochemistry
  doi: 10.1016/0003-2697(81)90175-5
  contributor:
    fullname: Doi
– volume: 96
  start-page: 1703
  year: 2005
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0015
  publication-title: Bioresource Technology
  doi: 10.1016/j.biortech.2004.12.026
  contributor:
    fullname: Bertsch
– volume: 18
  start-page: 563
  year: 2002
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0045
  publication-title: Journal of Microbiology and Biotechnology
  doi: 10.1023/A:1016341702908
  contributor:
    fullname: Noronha
– volume: 72
  start-page: 248
  year: 1976
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0135
  publication-title: Analytical Biochemistry
  doi: 10.1016/0003-2697(76)90527-3
  contributor:
    fullname: Bradford
– volume: 40
  start-page: 2325
  issue: 7
  year: 2005
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0165
  publication-title: Process Biochemistry
  doi: 10.1016/j.procbio.2004.09.006
  contributor:
    fullname: El-Refai
– volume: 56
  start-page: 219
  year: 1990
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0115
  publication-title: Entomologia Experimentia et Applicata
  doi: 10.1111/j.1570-7458.1990.tb01400.x
  contributor:
    fullname: Lemos
– volume: 40
  start-page: 191
  issue: 11
  year: 2004
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0060
  publication-title: Biotechnology and Applied Biochemistry
  doi: 10.1042/BA20030228
  contributor:
    fullname: Ramnani
– volume: 56
  start-page: 1509
  issue: 6
  year: 1990
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0030
  publication-title: Applied and Environment Microbiology
  doi: 10.1128/AEM.56.6.1509-1515.1990
  contributor:
    fullname: Williams
– volume: 3
  start-page: 293
  issue: 4
  year: 1999
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0150
  publication-title: Extremophiles
  doi: 10.1007/s007920050130
  contributor:
    fullname: Takami
– volume: 98
  start-page: 1238
  year: 2007
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0065
  publication-title: Bioresource Technology
  doi: 10.1016/j.biortech.2006.05.003
  contributor:
    fullname: Nilegaonkar
– volume: 61
  start-page: 3705
  year: 1995
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0035
  publication-title: Applied and Environment Microbiology
  doi: 10.1128/AEM.61.10.3705-3710.1995
  contributor:
    fullname: Böckle
– volume: 173
  start-page: 697
  issue: 2
  year: 1991
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0110
  publication-title: Journal of Bacteriology
  doi: 10.1128/jb.173.2.697-703.1991
  contributor:
    fullname: Weisberg
– volume: 6
  start-page: 185
  year: 2002
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0070
  publication-title: Extremophiles
  doi: 10.1007/s007920100239
  contributor:
    fullname: Kluskens
– volume: 37
  start-page: 287
  issue: 3
  year: 2001
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0140
  publication-title: Process Biochemistry
  doi: 10.1016/S0032-9592(01)00206-0
  contributor:
    fullname: Kim
– volume: 162
  start-page: 329
  year: 2010
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0170
  publication-title: Applied Microbiology and Biotechnology
  contributor:
    fullname: Zouari
– volume: 86
  start-page: 239
  issue: 3
  year: 2003
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0055
  publication-title: Bioresource Technology
  doi: 10.1016/S0960-8524(02)00177-3
  contributor:
    fullname: Suntornsuk
– year: 1984
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0105
  article-title: Bacillus and cocci
  contributor:
    fullname: Liu
– volume: 69
  start-page: 404
  year: 2005
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0020
  publication-title: Applied Microbiology and Biotechnology
  doi: 10.1007/s00253-005-1993-3
  contributor:
    fullname: Bálint
– volume: 71
  start-page: 594
  issue: 1
  year: 2005
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0145
  publication-title: Applied and Environment Microbiology
  doi: 10.1128/AEM.71.1.594-596.2005
  contributor:
    fullname: Macedo
– volume: 24
  start-page: 2741
  year: 2008
  ident: 10.1016/j.ijbiomac.2013.01.002_bib0180
  publication-title: World Journal of Microbiology and Biotechnology
  doi: 10.1007/s11274-008-9782-7
  contributor:
    fullname: Balaji
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Snippet Novel keratinolytic enzyme (32kDa) secreted by a newly isolated Bacillus strain (Bacillus subtilis NRC3) cultivated in medium containing chicken feather meal...
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StartPage 169
SubjectTerms 16S rDNA
Bacillus subtilis
Bacillus subtilis - classification
Bacillus subtilis - genetics
Bacillus subtilis - isolation & purification
Bacillus subtilis - metabolism
barium
calcium
cation exchange chromatography
cations
chickens
Enzyme Activation
enzyme activity
Enzyme Stability
enzymes
feather meal
feathers
gel chromatography
Hydrogen-Ion Concentration
Hydrolysis
keratin
Kinetics
magnesium
Metallo-keratinase
PCR-based RFLP
Peptide Hydrolases - biosynthesis
Peptide Hydrolases - chemistry
Peptide Hydrolases - isolation & purification
Peptide Hydrolases - metabolism
Phylogeny
potassium
RNA, Ribosomal, 16S
SDS-PAGE
sodium
Temperature
thermal stability
Thermostability
Title Production and characterization of thermostable metallo-keratinase from newly isolated Bacillus subtilis NRC 3
URI https://dx.doi.org/10.1016/j.ijbiomac.2013.01.002
https://www.ncbi.nlm.nih.gov/pubmed/23313822
https://search.proquest.com/docview/1316054415
Volume 55
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