High-level synthesis of endochitinase ChiA74 in Escherichia coli K12 and its promising potential for use in biotechnology
Abstract In the present study, we expressed the chiA74 gene of Bacillus thuringiensis in Escherichia coli K12 and demonstrated that the active ChiA74 enzyme was produced at a high level in this strain. The ChiA74 enzymatic activity (in units per milliliter) was approximately 500 % greater in E. coli...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Castañeda-Ramírez, J. Cristóbal [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2013 |
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| Schlagwörter: |
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| Anmerkung: |
© Institute of Microbiology, Academy of Sciences of the Czech Republic, v.v.i. 2013 |
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| Übergeordnetes Werk: |
Enthalten in: Folia microbiologica - [S.l.] : Springer, 1956, 58(2013), 6 vom: 12. Feb., Seite 455-462 |
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| Übergeordnetes Werk: |
volume:58 ; year:2013 ; number:6 ; day:12 ; month:02 ; pages:455-462 |
| Links: |
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| DOI / URN: |
10.1007/s12223-013-0229-7 |
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| Katalog-ID: |
SPR025456903 |
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| 100 | 1 | |a Castañeda-Ramírez, J. Cristóbal |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a High-level synthesis of endochitinase ChiA74 in Escherichia coli K12 and its promising potential for use in biotechnology |
| 264 | 1 | |c 2013 | |
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| 520 | |a Abstract In the present study, we expressed the chiA74 gene of Bacillus thuringiensis in Escherichia coli K12 and demonstrated that the active ChiA74 enzyme was produced at a high level in this strain. The ChiA74 enzymatic activity (in units per milliliter) was approximately 500 % greater in E. coli K12 when compared to that produced in E. coli DH5α. Moreover, we showed that, when using our protocol, ChiA74 preparations obtained from recombinant E. coli K12 did not contain live bacteria, although transformable DNA (erm, bla genes) was detected. Nucleic acids were subsequently easily eliminated when samples were treated with magnesium. Importantly, ChiA74 was secreted by E. coli K12 and the active enzyme was shown to generate chitin-derived oligosaccharides (C-OGS) with degrees of polymerization of 2, 3, 4, 5, and 6. From an applied perspective, the C-OGS showed activity against various pathogenic bacteria. In addition, we demonstrated that ChiA74 was not toxic to Hek 293 and 3T3 L1 cells, i.e., the enzyme did not induce apoptosis or affect normal cellular cycle and also did not produce abnormal changes in cell morphology. The potential biotechnological use of producing endochitinase of B. thuringiensis in a microorganism recognized as safe (i.e., E. coli K12) is discussed. | ||
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| 650 | 4 | |a Colloidal Chitin |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Chymosin |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a chiA74 Gene |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Endochitinase Activity |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a de la Fuente-Salcido, Norma M. |4 aut | |
| 700 | 1 | |a Salcedo-Hernández, Rubén |4 aut | |
| 700 | 1 | |a León-Galván, Fabiola |4 aut | |
| 700 | 1 | |a Bideshi, Dennis K. |4 aut | |
| 700 | 1 | |a Barboza-Corona, J. Eleazar |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Folia microbiologica |d [S.l.] : Springer, 1956 |g 58(2013), 6 vom: 12. Feb., Seite 455-462 |w (DE-627)502926317 |w (DE-600)2209844-6 |x 1874-9356 |7 nnns |
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10.1007/s12223-013-0229-7 doi (DE-627)SPR025456903 (SPR)s12223-013-0229-7-e DE-627 ger DE-627 rakwb eng Castañeda-Ramírez, J. Cristóbal verfasserin aut High-level synthesis of endochitinase ChiA74 in Escherichia coli K12 and its promising potential for use in biotechnology 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Institute of Microbiology, Academy of Sciences of the Czech Republic, v.v.i. 2013 Abstract In the present study, we expressed the chiA74 gene of Bacillus thuringiensis in Escherichia coli K12 and demonstrated that the active ChiA74 enzyme was produced at a high level in this strain. The ChiA74 enzymatic activity (in units per milliliter) was approximately 500 % greater in E. coli K12 when compared to that produced in E. coli DH5α. Moreover, we showed that, when using our protocol, ChiA74 preparations obtained from recombinant E. coli K12 did not contain live bacteria, although transformable DNA (erm, bla genes) was detected. Nucleic acids were subsequently easily eliminated when samples were treated with magnesium. Importantly, ChiA74 was secreted by E. coli K12 and the active enzyme was shown to generate chitin-derived oligosaccharides (C-OGS) with degrees of polymerization of 2, 3, 4, 5, and 6. From an applied perspective, the C-OGS showed activity against various pathogenic bacteria. In addition, we demonstrated that ChiA74 was not toxic to Hek 293 and 3T3 L1 cells, i.e., the enzyme did not induce apoptosis or affect normal cellular cycle and also did not produce abnormal changes in cell morphology. The potential biotechnological use of producing endochitinase of B. thuringiensis in a microorganism recognized as safe (i.e., E. coli K12) is discussed. Chitinase (dpeaa)DE-He213 Colloidal Chitin (dpeaa)DE-He213 Chymosin (dpeaa)DE-He213 chiA74 Gene (dpeaa)DE-He213 Endochitinase Activity (dpeaa)DE-He213 de la Fuente-Salcido, Norma M. aut Salcedo-Hernández, Rubén aut León-Galván, Fabiola aut Bideshi, Dennis K. aut Barboza-Corona, J. Eleazar aut Enthalten in Folia microbiologica [S.l.] : Springer, 1956 58(2013), 6 vom: 12. Feb., Seite 455-462 (DE-627)502926317 (DE-600)2209844-6 1874-9356 nnns volume:58 year:2013 number:6 day:12 month:02 pages:455-462 https://dx.doi.org/10.1007/s12223-013-0229-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 58 2013 6 12 02 455-462 |
| spelling |
10.1007/s12223-013-0229-7 doi (DE-627)SPR025456903 (SPR)s12223-013-0229-7-e DE-627 ger DE-627 rakwb eng Castañeda-Ramírez, J. Cristóbal verfasserin aut High-level synthesis of endochitinase ChiA74 in Escherichia coli K12 and its promising potential for use in biotechnology 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Institute of Microbiology, Academy of Sciences of the Czech Republic, v.v.i. 2013 Abstract In the present study, we expressed the chiA74 gene of Bacillus thuringiensis in Escherichia coli K12 and demonstrated that the active ChiA74 enzyme was produced at a high level in this strain. The ChiA74 enzymatic activity (in units per milliliter) was approximately 500 % greater in E. coli K12 when compared to that produced in E. coli DH5α. Moreover, we showed that, when using our protocol, ChiA74 preparations obtained from recombinant E. coli K12 did not contain live bacteria, although transformable DNA (erm, bla genes) was detected. Nucleic acids were subsequently easily eliminated when samples were treated with magnesium. Importantly, ChiA74 was secreted by E. coli K12 and the active enzyme was shown to generate chitin-derived oligosaccharides (C-OGS) with degrees of polymerization of 2, 3, 4, 5, and 6. From an applied perspective, the C-OGS showed activity against various pathogenic bacteria. In addition, we demonstrated that ChiA74 was not toxic to Hek 293 and 3T3 L1 cells, i.e., the enzyme did not induce apoptosis or affect normal cellular cycle and also did not produce abnormal changes in cell morphology. The potential biotechnological use of producing endochitinase of B. thuringiensis in a microorganism recognized as safe (i.e., E. coli K12) is discussed. Chitinase (dpeaa)DE-He213 Colloidal Chitin (dpeaa)DE-He213 Chymosin (dpeaa)DE-He213 chiA74 Gene (dpeaa)DE-He213 Endochitinase Activity (dpeaa)DE-He213 de la Fuente-Salcido, Norma M. aut Salcedo-Hernández, Rubén aut León-Galván, Fabiola aut Bideshi, Dennis K. aut Barboza-Corona, J. Eleazar aut Enthalten in Folia microbiologica [S.l.] : Springer, 1956 58(2013), 6 vom: 12. Feb., Seite 455-462 (DE-627)502926317 (DE-600)2209844-6 1874-9356 nnns volume:58 year:2013 number:6 day:12 month:02 pages:455-462 https://dx.doi.org/10.1007/s12223-013-0229-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 58 2013 6 12 02 455-462 |
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10.1007/s12223-013-0229-7 doi (DE-627)SPR025456903 (SPR)s12223-013-0229-7-e DE-627 ger DE-627 rakwb eng Castañeda-Ramírez, J. Cristóbal verfasserin aut High-level synthesis of endochitinase ChiA74 in Escherichia coli K12 and its promising potential for use in biotechnology 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Institute of Microbiology, Academy of Sciences of the Czech Republic, v.v.i. 2013 Abstract In the present study, we expressed the chiA74 gene of Bacillus thuringiensis in Escherichia coli K12 and demonstrated that the active ChiA74 enzyme was produced at a high level in this strain. The ChiA74 enzymatic activity (in units per milliliter) was approximately 500 % greater in E. coli K12 when compared to that produced in E. coli DH5α. Moreover, we showed that, when using our protocol, ChiA74 preparations obtained from recombinant E. coli K12 did not contain live bacteria, although transformable DNA (erm, bla genes) was detected. Nucleic acids were subsequently easily eliminated when samples were treated with magnesium. Importantly, ChiA74 was secreted by E. coli K12 and the active enzyme was shown to generate chitin-derived oligosaccharides (C-OGS) with degrees of polymerization of 2, 3, 4, 5, and 6. From an applied perspective, the C-OGS showed activity against various pathogenic bacteria. In addition, we demonstrated that ChiA74 was not toxic to Hek 293 and 3T3 L1 cells, i.e., the enzyme did not induce apoptosis or affect normal cellular cycle and also did not produce abnormal changes in cell morphology. The potential biotechnological use of producing endochitinase of B. thuringiensis in a microorganism recognized as safe (i.e., E. coli K12) is discussed. Chitinase (dpeaa)DE-He213 Colloidal Chitin (dpeaa)DE-He213 Chymosin (dpeaa)DE-He213 chiA74 Gene (dpeaa)DE-He213 Endochitinase Activity (dpeaa)DE-He213 de la Fuente-Salcido, Norma M. aut Salcedo-Hernández, Rubén aut León-Galván, Fabiola aut Bideshi, Dennis K. aut Barboza-Corona, J. Eleazar aut Enthalten in Folia microbiologica [S.l.] : Springer, 1956 58(2013), 6 vom: 12. Feb., Seite 455-462 (DE-627)502926317 (DE-600)2209844-6 1874-9356 nnns volume:58 year:2013 number:6 day:12 month:02 pages:455-462 https://dx.doi.org/10.1007/s12223-013-0229-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 58 2013 6 12 02 455-462 |
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10.1007/s12223-013-0229-7 doi (DE-627)SPR025456903 (SPR)s12223-013-0229-7-e DE-627 ger DE-627 rakwb eng Castañeda-Ramírez, J. Cristóbal verfasserin aut High-level synthesis of endochitinase ChiA74 in Escherichia coli K12 and its promising potential for use in biotechnology 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Institute of Microbiology, Academy of Sciences of the Czech Republic, v.v.i. 2013 Abstract In the present study, we expressed the chiA74 gene of Bacillus thuringiensis in Escherichia coli K12 and demonstrated that the active ChiA74 enzyme was produced at a high level in this strain. The ChiA74 enzymatic activity (in units per milliliter) was approximately 500 % greater in E. coli K12 when compared to that produced in E. coli DH5α. Moreover, we showed that, when using our protocol, ChiA74 preparations obtained from recombinant E. coli K12 did not contain live bacteria, although transformable DNA (erm, bla genes) was detected. Nucleic acids were subsequently easily eliminated when samples were treated with magnesium. Importantly, ChiA74 was secreted by E. coli K12 and the active enzyme was shown to generate chitin-derived oligosaccharides (C-OGS) with degrees of polymerization of 2, 3, 4, 5, and 6. From an applied perspective, the C-OGS showed activity against various pathogenic bacteria. In addition, we demonstrated that ChiA74 was not toxic to Hek 293 and 3T3 L1 cells, i.e., the enzyme did not induce apoptosis or affect normal cellular cycle and also did not produce abnormal changes in cell morphology. The potential biotechnological use of producing endochitinase of B. thuringiensis in a microorganism recognized as safe (i.e., E. coli K12) is discussed. Chitinase (dpeaa)DE-He213 Colloidal Chitin (dpeaa)DE-He213 Chymosin (dpeaa)DE-He213 chiA74 Gene (dpeaa)DE-He213 Endochitinase Activity (dpeaa)DE-He213 de la Fuente-Salcido, Norma M. aut Salcedo-Hernández, Rubén aut León-Galván, Fabiola aut Bideshi, Dennis K. aut Barboza-Corona, J. Eleazar aut Enthalten in Folia microbiologica [S.l.] : Springer, 1956 58(2013), 6 vom: 12. Feb., Seite 455-462 (DE-627)502926317 (DE-600)2209844-6 1874-9356 nnns volume:58 year:2013 number:6 day:12 month:02 pages:455-462 https://dx.doi.org/10.1007/s12223-013-0229-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 58 2013 6 12 02 455-462 |
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10.1007/s12223-013-0229-7 doi (DE-627)SPR025456903 (SPR)s12223-013-0229-7-e DE-627 ger DE-627 rakwb eng Castañeda-Ramírez, J. Cristóbal verfasserin aut High-level synthesis of endochitinase ChiA74 in Escherichia coli K12 and its promising potential for use in biotechnology 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Institute of Microbiology, Academy of Sciences of the Czech Republic, v.v.i. 2013 Abstract In the present study, we expressed the chiA74 gene of Bacillus thuringiensis in Escherichia coli K12 and demonstrated that the active ChiA74 enzyme was produced at a high level in this strain. The ChiA74 enzymatic activity (in units per milliliter) was approximately 500 % greater in E. coli K12 when compared to that produced in E. coli DH5α. Moreover, we showed that, when using our protocol, ChiA74 preparations obtained from recombinant E. coli K12 did not contain live bacteria, although transformable DNA (erm, bla genes) was detected. Nucleic acids were subsequently easily eliminated when samples were treated with magnesium. Importantly, ChiA74 was secreted by E. coli K12 and the active enzyme was shown to generate chitin-derived oligosaccharides (C-OGS) with degrees of polymerization of 2, 3, 4, 5, and 6. From an applied perspective, the C-OGS showed activity against various pathogenic bacteria. In addition, we demonstrated that ChiA74 was not toxic to Hek 293 and 3T3 L1 cells, i.e., the enzyme did not induce apoptosis or affect normal cellular cycle and also did not produce abnormal changes in cell morphology. The potential biotechnological use of producing endochitinase of B. thuringiensis in a microorganism recognized as safe (i.e., E. coli K12) is discussed. Chitinase (dpeaa)DE-He213 Colloidal Chitin (dpeaa)DE-He213 Chymosin (dpeaa)DE-He213 chiA74 Gene (dpeaa)DE-He213 Endochitinase Activity (dpeaa)DE-He213 de la Fuente-Salcido, Norma M. aut Salcedo-Hernández, Rubén aut León-Galván, Fabiola aut Bideshi, Dennis K. aut Barboza-Corona, J. Eleazar aut Enthalten in Folia microbiologica [S.l.] : Springer, 1956 58(2013), 6 vom: 12. Feb., Seite 455-462 (DE-627)502926317 (DE-600)2209844-6 1874-9356 nnns volume:58 year:2013 number:6 day:12 month:02 pages:455-462 https://dx.doi.org/10.1007/s12223-013-0229-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 58 2013 6 12 02 455-462 |
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Enthalten in Folia microbiologica 58(2013), 6 vom: 12. Feb., Seite 455-462 volume:58 year:2013 number:6 day:12 month:02 pages:455-462 |
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Enthalten in Folia microbiologica 58(2013), 6 vom: 12. Feb., Seite 455-462 volume:58 year:2013 number:6 day:12 month:02 pages:455-462 |
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Chitinase Colloidal Chitin Chymosin chiA74 Gene Endochitinase Activity |
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Castañeda-Ramírez, J. Cristóbal @@aut@@ de la Fuente-Salcido, Norma M. @@aut@@ Salcedo-Hernández, Rubén @@aut@@ León-Galván, Fabiola @@aut@@ Bideshi, Dennis K. @@aut@@ Barboza-Corona, J. Eleazar @@aut@@ |
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The ChiA74 enzymatic activity (in units per milliliter) was approximately 500 % greater in E. coli K12 when compared to that produced in E. coli DH5α. Moreover, we showed that, when using our protocol, ChiA74 preparations obtained from recombinant E. coli K12 did not contain live bacteria, although transformable DNA (erm, bla genes) was detected. Nucleic acids were subsequently easily eliminated when samples were treated with magnesium. Importantly, ChiA74 was secreted by E. coli K12 and the active enzyme was shown to generate chitin-derived oligosaccharides (C-OGS) with degrees of polymerization of 2, 3, 4, 5, and 6. From an applied perspective, the C-OGS showed activity against various pathogenic bacteria. In addition, we demonstrated that ChiA74 was not toxic to Hek 293 and 3T3 L1 cells, i.e., the enzyme did not induce apoptosis or affect normal cellular cycle and also did not produce abnormal changes in cell morphology. 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Castañeda-Ramírez, J. Cristóbal |
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Castañeda-Ramírez, J. Cristóbal misc Chitinase misc Colloidal Chitin misc Chymosin misc chiA74 Gene misc Endochitinase Activity High-level synthesis of endochitinase ChiA74 in Escherichia coli K12 and its promising potential for use in biotechnology |
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High-level synthesis of endochitinase ChiA74 in Escherichia coli K12 and its promising potential for use in biotechnology Chitinase (dpeaa)DE-He213 Colloidal Chitin (dpeaa)DE-He213 Chymosin (dpeaa)DE-He213 chiA74 Gene (dpeaa)DE-He213 Endochitinase Activity (dpeaa)DE-He213 |
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High-level synthesis of endochitinase ChiA74 in Escherichia coli K12 and its promising potential for use in biotechnology |
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Castañeda-Ramírez, J. Cristóbal de la Fuente-Salcido, Norma M. Salcedo-Hernández, Rubén León-Galván, Fabiola Bideshi, Dennis K. Barboza-Corona, J. Eleazar |
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high-level synthesis of endochitinase chia74 in escherichia coli k12 and its promising potential for use in biotechnology |
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High-level synthesis of endochitinase ChiA74 in Escherichia coli K12 and its promising potential for use in biotechnology |
| abstract |
Abstract In the present study, we expressed the chiA74 gene of Bacillus thuringiensis in Escherichia coli K12 and demonstrated that the active ChiA74 enzyme was produced at a high level in this strain. The ChiA74 enzymatic activity (in units per milliliter) was approximately 500 % greater in E. coli K12 when compared to that produced in E. coli DH5α. Moreover, we showed that, when using our protocol, ChiA74 preparations obtained from recombinant E. coli K12 did not contain live bacteria, although transformable DNA (erm, bla genes) was detected. Nucleic acids were subsequently easily eliminated when samples were treated with magnesium. Importantly, ChiA74 was secreted by E. coli K12 and the active enzyme was shown to generate chitin-derived oligosaccharides (C-OGS) with degrees of polymerization of 2, 3, 4, 5, and 6. From an applied perspective, the C-OGS showed activity against various pathogenic bacteria. In addition, we demonstrated that ChiA74 was not toxic to Hek 293 and 3T3 L1 cells, i.e., the enzyme did not induce apoptosis or affect normal cellular cycle and also did not produce abnormal changes in cell morphology. The potential biotechnological use of producing endochitinase of B. thuringiensis in a microorganism recognized as safe (i.e., E. coli K12) is discussed. © Institute of Microbiology, Academy of Sciences of the Czech Republic, v.v.i. 2013 |
| abstractGer |
Abstract In the present study, we expressed the chiA74 gene of Bacillus thuringiensis in Escherichia coli K12 and demonstrated that the active ChiA74 enzyme was produced at a high level in this strain. The ChiA74 enzymatic activity (in units per milliliter) was approximately 500 % greater in E. coli K12 when compared to that produced in E. coli DH5α. Moreover, we showed that, when using our protocol, ChiA74 preparations obtained from recombinant E. coli K12 did not contain live bacteria, although transformable DNA (erm, bla genes) was detected. Nucleic acids were subsequently easily eliminated when samples were treated with magnesium. Importantly, ChiA74 was secreted by E. coli K12 and the active enzyme was shown to generate chitin-derived oligosaccharides (C-OGS) with degrees of polymerization of 2, 3, 4, 5, and 6. From an applied perspective, the C-OGS showed activity against various pathogenic bacteria. In addition, we demonstrated that ChiA74 was not toxic to Hek 293 and 3T3 L1 cells, i.e., the enzyme did not induce apoptosis or affect normal cellular cycle and also did not produce abnormal changes in cell morphology. The potential biotechnological use of producing endochitinase of B. thuringiensis in a microorganism recognized as safe (i.e., E. coli K12) is discussed. © Institute of Microbiology, Academy of Sciences of the Czech Republic, v.v.i. 2013 |
| abstract_unstemmed |
Abstract In the present study, we expressed the chiA74 gene of Bacillus thuringiensis in Escherichia coli K12 and demonstrated that the active ChiA74 enzyme was produced at a high level in this strain. The ChiA74 enzymatic activity (in units per milliliter) was approximately 500 % greater in E. coli K12 when compared to that produced in E. coli DH5α. Moreover, we showed that, when using our protocol, ChiA74 preparations obtained from recombinant E. coli K12 did not contain live bacteria, although transformable DNA (erm, bla genes) was detected. Nucleic acids were subsequently easily eliminated when samples were treated with magnesium. Importantly, ChiA74 was secreted by E. coli K12 and the active enzyme was shown to generate chitin-derived oligosaccharides (C-OGS) with degrees of polymerization of 2, 3, 4, 5, and 6. From an applied perspective, the C-OGS showed activity against various pathogenic bacteria. In addition, we demonstrated that ChiA74 was not toxic to Hek 293 and 3T3 L1 cells, i.e., the enzyme did not induce apoptosis or affect normal cellular cycle and also did not produce abnormal changes in cell morphology. The potential biotechnological use of producing endochitinase of B. thuringiensis in a microorganism recognized as safe (i.e., E. coli K12) is discussed. © Institute of Microbiology, Academy of Sciences of the Czech Republic, v.v.i. 2013 |
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High-level synthesis of endochitinase ChiA74 in Escherichia coli K12 and its promising potential for use in biotechnology |
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https://dx.doi.org/10.1007/s12223-013-0229-7 |
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de la Fuente-Salcido, Norma M. Salcedo-Hernández, Rubén León-Galván, Fabiola Bideshi, Dennis K. Barboza-Corona, J. Eleazar |
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de la Fuente-Salcido, Norma M. Salcedo-Hernández, Rubén León-Galván, Fabiola Bideshi, Dennis K. Barboza-Corona, J. Eleazar |
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| score |
7.401532 |