Recombinant production and biochemical characterization of a hypothetical acidic shell matrix protein in Escherichia coli for the preparation of protein-based $ CaCO_{3} $ biominerals
Abstract The biological structure of shells consists of highly organized calcium carbonate ($ CaCO_{3} $) crystals, which have remarkable mechanical and biological properties compared to the pure mineral form of $ CaCO_{3} $. It has been known that the organization of these biominerals is controlled...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Son, Chaeyeon [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2016 |
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| Schlagwörter: |
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| Anmerkung: |
© Korean Institute of Chemical Engineers, Seoul, Korea 2016 |
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| Übergeordnetes Werk: |
Enthalten in: The Korean journal of chemical engineering - Seoul : Inst., 1984, 33(2016), 8 vom: 03. Juni, Seite 2406-2410 |
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| Übergeordnetes Werk: |
volume:33 ; year:2016 ; number:8 ; day:03 ; month:06 ; pages:2406-2410 |
| Links: |
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| DOI / URN: |
10.1007/s11814-016-0091-9 |
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SPR022517006 |
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| 100 | 1 | |a Son, Chaeyeon |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Recombinant production and biochemical characterization of a hypothetical acidic shell matrix protein in Escherichia coli for the preparation of protein-based $ CaCO_{3} $ biominerals |
| 264 | 1 | |c 2016 | |
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| 520 | |a Abstract The biological structure of shells consists of highly organized calcium carbonate ($ CaCO_{3} $) crystals, which have remarkable mechanical and biological properties compared to the pure mineral form of $ CaCO_{3} $. It has been known that the organization of these biominerals is controlled by a relatively tiny amount of organic components such as shell matrix proteins. Here, we successfully produced a recombinant hypothetical acidic shell matrix protein in Escherichia coli, although the protein is composed of highly repetitive and biased amino acid sequences. About 15mg/L purified protein with greater than 95% purity was obtained in the 400 mL lab scale flask culture. The protein was able to efficiently form a complex with calcium ions, and spherulitic calcite crystals were synthesized in the presence of the recombinant protein. We expect that biomineralization using the recombinant protein could not only overcome the limited amount of protein available for biomineralization studies and biomineral preparation in practical aspects, but also provide opportunities to enable biomimetic synthesis of notable bio-composites based on organic-inorganic complexation. | ||
| 650 | 4 | |a Biomineralization |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Calcium Carbonate |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Shell Matrix Protein |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Glycine-rich Protein |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Recombinant |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Song, Wooho |4 aut | |
| 700 | 1 | |a Hwang, Dong Soo |4 aut | |
| 700 | 1 | |a Hong, Yong-Ki |4 aut | |
| 700 | 1 | |a Joo, Jin |4 aut | |
| 700 | 1 | |a Choi, Yoo Seong |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t The Korean journal of chemical engineering |d Seoul : Inst., 1984 |g 33(2016), 8 vom: 03. Juni, Seite 2406-2410 |w (DE-627)391337246 |w (DE-600)2152566-3 |x 1975-7220 |7 nnns |
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10.1007/s11814-016-0091-9 doi (DE-627)SPR022517006 (SPR)s11814-016-0091-9-e DE-627 ger DE-627 rakwb eng Son, Chaeyeon verfasserin aut Recombinant production and biochemical characterization of a hypothetical acidic shell matrix protein in Escherichia coli for the preparation of protein-based $ CaCO_{3} $ biominerals 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Korean Institute of Chemical Engineers, Seoul, Korea 2016 Abstract The biological structure of shells consists of highly organized calcium carbonate ($ CaCO_{3} $) crystals, which have remarkable mechanical and biological properties compared to the pure mineral form of $ CaCO_{3} $. It has been known that the organization of these biominerals is controlled by a relatively tiny amount of organic components such as shell matrix proteins. Here, we successfully produced a recombinant hypothetical acidic shell matrix protein in Escherichia coli, although the protein is composed of highly repetitive and biased amino acid sequences. About 15mg/L purified protein with greater than 95% purity was obtained in the 400 mL lab scale flask culture. The protein was able to efficiently form a complex with calcium ions, and spherulitic calcite crystals were synthesized in the presence of the recombinant protein. We expect that biomineralization using the recombinant protein could not only overcome the limited amount of protein available for biomineralization studies and biomineral preparation in practical aspects, but also provide opportunities to enable biomimetic synthesis of notable bio-composites based on organic-inorganic complexation. Biomineralization (dpeaa)DE-He213 Calcium Carbonate (dpeaa)DE-He213 Shell Matrix Protein (dpeaa)DE-He213 Glycine-rich Protein (dpeaa)DE-He213 Recombinant (dpeaa)DE-He213 Song, Wooho aut Hwang, Dong Soo aut Hong, Yong-Ki aut Joo, Jin aut Choi, Yoo Seong aut Enthalten in The Korean journal of chemical engineering Seoul : Inst., 1984 33(2016), 8 vom: 03. Juni, Seite 2406-2410 (DE-627)391337246 (DE-600)2152566-3 1975-7220 nnns volume:33 year:2016 number:8 day:03 month:06 pages:2406-2410 https://dx.doi.org/10.1007/s11814-016-0091-9 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_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_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 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 33 2016 8 03 06 2406-2410 |
| spelling |
10.1007/s11814-016-0091-9 doi (DE-627)SPR022517006 (SPR)s11814-016-0091-9-e DE-627 ger DE-627 rakwb eng Son, Chaeyeon verfasserin aut Recombinant production and biochemical characterization of a hypothetical acidic shell matrix protein in Escherichia coli for the preparation of protein-based $ CaCO_{3} $ biominerals 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Korean Institute of Chemical Engineers, Seoul, Korea 2016 Abstract The biological structure of shells consists of highly organized calcium carbonate ($ CaCO_{3} $) crystals, which have remarkable mechanical and biological properties compared to the pure mineral form of $ CaCO_{3} $. It has been known that the organization of these biominerals is controlled by a relatively tiny amount of organic components such as shell matrix proteins. Here, we successfully produced a recombinant hypothetical acidic shell matrix protein in Escherichia coli, although the protein is composed of highly repetitive and biased amino acid sequences. About 15mg/L purified protein with greater than 95% purity was obtained in the 400 mL lab scale flask culture. The protein was able to efficiently form a complex with calcium ions, and spherulitic calcite crystals were synthesized in the presence of the recombinant protein. We expect that biomineralization using the recombinant protein could not only overcome the limited amount of protein available for biomineralization studies and biomineral preparation in practical aspects, but also provide opportunities to enable biomimetic synthesis of notable bio-composites based on organic-inorganic complexation. Biomineralization (dpeaa)DE-He213 Calcium Carbonate (dpeaa)DE-He213 Shell Matrix Protein (dpeaa)DE-He213 Glycine-rich Protein (dpeaa)DE-He213 Recombinant (dpeaa)DE-He213 Song, Wooho aut Hwang, Dong Soo aut Hong, Yong-Ki aut Joo, Jin aut Choi, Yoo Seong aut Enthalten in The Korean journal of chemical engineering Seoul : Inst., 1984 33(2016), 8 vom: 03. Juni, Seite 2406-2410 (DE-627)391337246 (DE-600)2152566-3 1975-7220 nnns volume:33 year:2016 number:8 day:03 month:06 pages:2406-2410 https://dx.doi.org/10.1007/s11814-016-0091-9 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_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_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 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 33 2016 8 03 06 2406-2410 |
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10.1007/s11814-016-0091-9 doi (DE-627)SPR022517006 (SPR)s11814-016-0091-9-e DE-627 ger DE-627 rakwb eng Son, Chaeyeon verfasserin aut Recombinant production and biochemical characterization of a hypothetical acidic shell matrix protein in Escherichia coli for the preparation of protein-based $ CaCO_{3} $ biominerals 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Korean Institute of Chemical Engineers, Seoul, Korea 2016 Abstract The biological structure of shells consists of highly organized calcium carbonate ($ CaCO_{3} $) crystals, which have remarkable mechanical and biological properties compared to the pure mineral form of $ CaCO_{3} $. It has been known that the organization of these biominerals is controlled by a relatively tiny amount of organic components such as shell matrix proteins. Here, we successfully produced a recombinant hypothetical acidic shell matrix protein in Escherichia coli, although the protein is composed of highly repetitive and biased amino acid sequences. About 15mg/L purified protein with greater than 95% purity was obtained in the 400 mL lab scale flask culture. The protein was able to efficiently form a complex with calcium ions, and spherulitic calcite crystals were synthesized in the presence of the recombinant protein. We expect that biomineralization using the recombinant protein could not only overcome the limited amount of protein available for biomineralization studies and biomineral preparation in practical aspects, but also provide opportunities to enable biomimetic synthesis of notable bio-composites based on organic-inorganic complexation. Biomineralization (dpeaa)DE-He213 Calcium Carbonate (dpeaa)DE-He213 Shell Matrix Protein (dpeaa)DE-He213 Glycine-rich Protein (dpeaa)DE-He213 Recombinant (dpeaa)DE-He213 Song, Wooho aut Hwang, Dong Soo aut Hong, Yong-Ki aut Joo, Jin aut Choi, Yoo Seong aut Enthalten in The Korean journal of chemical engineering Seoul : Inst., 1984 33(2016), 8 vom: 03. Juni, Seite 2406-2410 (DE-627)391337246 (DE-600)2152566-3 1975-7220 nnns volume:33 year:2016 number:8 day:03 month:06 pages:2406-2410 https://dx.doi.org/10.1007/s11814-016-0091-9 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_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_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 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 33 2016 8 03 06 2406-2410 |
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10.1007/s11814-016-0091-9 doi (DE-627)SPR022517006 (SPR)s11814-016-0091-9-e DE-627 ger DE-627 rakwb eng Son, Chaeyeon verfasserin aut Recombinant production and biochemical characterization of a hypothetical acidic shell matrix protein in Escherichia coli for the preparation of protein-based $ CaCO_{3} $ biominerals 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Korean Institute of Chemical Engineers, Seoul, Korea 2016 Abstract The biological structure of shells consists of highly organized calcium carbonate ($ CaCO_{3} $) crystals, which have remarkable mechanical and biological properties compared to the pure mineral form of $ CaCO_{3} $. It has been known that the organization of these biominerals is controlled by a relatively tiny amount of organic components such as shell matrix proteins. Here, we successfully produced a recombinant hypothetical acidic shell matrix protein in Escherichia coli, although the protein is composed of highly repetitive and biased amino acid sequences. About 15mg/L purified protein with greater than 95% purity was obtained in the 400 mL lab scale flask culture. The protein was able to efficiently form a complex with calcium ions, and spherulitic calcite crystals were synthesized in the presence of the recombinant protein. We expect that biomineralization using the recombinant protein could not only overcome the limited amount of protein available for biomineralization studies and biomineral preparation in practical aspects, but also provide opportunities to enable biomimetic synthesis of notable bio-composites based on organic-inorganic complexation. Biomineralization (dpeaa)DE-He213 Calcium Carbonate (dpeaa)DE-He213 Shell Matrix Protein (dpeaa)DE-He213 Glycine-rich Protein (dpeaa)DE-He213 Recombinant (dpeaa)DE-He213 Song, Wooho aut Hwang, Dong Soo aut Hong, Yong-Ki aut Joo, Jin aut Choi, Yoo Seong aut Enthalten in The Korean journal of chemical engineering Seoul : Inst., 1984 33(2016), 8 vom: 03. Juni, Seite 2406-2410 (DE-627)391337246 (DE-600)2152566-3 1975-7220 nnns volume:33 year:2016 number:8 day:03 month:06 pages:2406-2410 https://dx.doi.org/10.1007/s11814-016-0091-9 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_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_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 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 33 2016 8 03 06 2406-2410 |
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10.1007/s11814-016-0091-9 doi (DE-627)SPR022517006 (SPR)s11814-016-0091-9-e DE-627 ger DE-627 rakwb eng Son, Chaeyeon verfasserin aut Recombinant production and biochemical characterization of a hypothetical acidic shell matrix protein in Escherichia coli for the preparation of protein-based $ CaCO_{3} $ biominerals 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Korean Institute of Chemical Engineers, Seoul, Korea 2016 Abstract The biological structure of shells consists of highly organized calcium carbonate ($ CaCO_{3} $) crystals, which have remarkable mechanical and biological properties compared to the pure mineral form of $ CaCO_{3} $. It has been known that the organization of these biominerals is controlled by a relatively tiny amount of organic components such as shell matrix proteins. Here, we successfully produced a recombinant hypothetical acidic shell matrix protein in Escherichia coli, although the protein is composed of highly repetitive and biased amino acid sequences. About 15mg/L purified protein with greater than 95% purity was obtained in the 400 mL lab scale flask culture. The protein was able to efficiently form a complex with calcium ions, and spherulitic calcite crystals were synthesized in the presence of the recombinant protein. We expect that biomineralization using the recombinant protein could not only overcome the limited amount of protein available for biomineralization studies and biomineral preparation in practical aspects, but also provide opportunities to enable biomimetic synthesis of notable bio-composites based on organic-inorganic complexation. Biomineralization (dpeaa)DE-He213 Calcium Carbonate (dpeaa)DE-He213 Shell Matrix Protein (dpeaa)DE-He213 Glycine-rich Protein (dpeaa)DE-He213 Recombinant (dpeaa)DE-He213 Song, Wooho aut Hwang, Dong Soo aut Hong, Yong-Ki aut Joo, Jin aut Choi, Yoo Seong aut Enthalten in The Korean journal of chemical engineering Seoul : Inst., 1984 33(2016), 8 vom: 03. Juni, Seite 2406-2410 (DE-627)391337246 (DE-600)2152566-3 1975-7220 nnns volume:33 year:2016 number:8 day:03 month:06 pages:2406-2410 https://dx.doi.org/10.1007/s11814-016-0091-9 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_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_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 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 33 2016 8 03 06 2406-2410 |
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Enthalten in The Korean journal of chemical engineering 33(2016), 8 vom: 03. Juni, Seite 2406-2410 volume:33 year:2016 number:8 day:03 month:06 pages:2406-2410 |
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Biomineralization Calcium Carbonate Shell Matrix Protein Glycine-rich Protein Recombinant |
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Son, Chaeyeon @@aut@@ Song, Wooho @@aut@@ Hwang, Dong Soo @@aut@@ Hong, Yong-Ki @@aut@@ Joo, Jin @@aut@@ Choi, Yoo Seong @@aut@@ |
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Son, Chaeyeon |
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Son, Chaeyeon misc Biomineralization misc Calcium Carbonate misc Shell Matrix Protein misc Glycine-rich Protein misc Recombinant Recombinant production and biochemical characterization of a hypothetical acidic shell matrix protein in Escherichia coli for the preparation of protein-based $ CaCO_{3} $ biominerals |
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Recombinant production and biochemical characterization of a hypothetical acidic shell matrix protein in Escherichia coli for the preparation of protein-based $ CaCO_{3} $ biominerals Biomineralization (dpeaa)DE-He213 Calcium Carbonate (dpeaa)DE-He213 Shell Matrix Protein (dpeaa)DE-He213 Glycine-rich Protein (dpeaa)DE-He213 Recombinant (dpeaa)DE-He213 |
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misc Biomineralization misc Calcium Carbonate misc Shell Matrix Protein misc Glycine-rich Protein misc Recombinant |
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Recombinant production and biochemical characterization of a hypothetical acidic shell matrix protein in Escherichia coli for the preparation of protein-based $ CaCO_{3} $ biominerals |
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Recombinant production and biochemical characterization of a hypothetical acidic shell matrix protein in Escherichia coli for the preparation of protein-based $ CaCO_{3} $ biominerals |
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Son, Chaeyeon Song, Wooho Hwang, Dong Soo Hong, Yong-Ki Joo, Jin Choi, Yoo Seong |
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recombinant production and biochemical characterization of a hypothetical acidic shell matrix protein in escherichia coli for the preparation of protein-based $ caco_{3} $ biominerals |
| title_auth |
Recombinant production and biochemical characterization of a hypothetical acidic shell matrix protein in Escherichia coli for the preparation of protein-based $ CaCO_{3} $ biominerals |
| abstract |
Abstract The biological structure of shells consists of highly organized calcium carbonate ($ CaCO_{3} $) crystals, which have remarkable mechanical and biological properties compared to the pure mineral form of $ CaCO_{3} $. It has been known that the organization of these biominerals is controlled by a relatively tiny amount of organic components such as shell matrix proteins. Here, we successfully produced a recombinant hypothetical acidic shell matrix protein in Escherichia coli, although the protein is composed of highly repetitive and biased amino acid sequences. About 15mg/L purified protein with greater than 95% purity was obtained in the 400 mL lab scale flask culture. The protein was able to efficiently form a complex with calcium ions, and spherulitic calcite crystals were synthesized in the presence of the recombinant protein. We expect that biomineralization using the recombinant protein could not only overcome the limited amount of protein available for biomineralization studies and biomineral preparation in practical aspects, but also provide opportunities to enable biomimetic synthesis of notable bio-composites based on organic-inorganic complexation. © Korean Institute of Chemical Engineers, Seoul, Korea 2016 |
| abstractGer |
Abstract The biological structure of shells consists of highly organized calcium carbonate ($ CaCO_{3} $) crystals, which have remarkable mechanical and biological properties compared to the pure mineral form of $ CaCO_{3} $. It has been known that the organization of these biominerals is controlled by a relatively tiny amount of organic components such as shell matrix proteins. Here, we successfully produced a recombinant hypothetical acidic shell matrix protein in Escherichia coli, although the protein is composed of highly repetitive and biased amino acid sequences. About 15mg/L purified protein with greater than 95% purity was obtained in the 400 mL lab scale flask culture. The protein was able to efficiently form a complex with calcium ions, and spherulitic calcite crystals were synthesized in the presence of the recombinant protein. We expect that biomineralization using the recombinant protein could not only overcome the limited amount of protein available for biomineralization studies and biomineral preparation in practical aspects, but also provide opportunities to enable biomimetic synthesis of notable bio-composites based on organic-inorganic complexation. © Korean Institute of Chemical Engineers, Seoul, Korea 2016 |
| abstract_unstemmed |
Abstract The biological structure of shells consists of highly organized calcium carbonate ($ CaCO_{3} $) crystals, which have remarkable mechanical and biological properties compared to the pure mineral form of $ CaCO_{3} $. It has been known that the organization of these biominerals is controlled by a relatively tiny amount of organic components such as shell matrix proteins. Here, we successfully produced a recombinant hypothetical acidic shell matrix protein in Escherichia coli, although the protein is composed of highly repetitive and biased amino acid sequences. About 15mg/L purified protein with greater than 95% purity was obtained in the 400 mL lab scale flask culture. The protein was able to efficiently form a complex with calcium ions, and spherulitic calcite crystals were synthesized in the presence of the recombinant protein. We expect that biomineralization using the recombinant protein could not only overcome the limited amount of protein available for biomineralization studies and biomineral preparation in practical aspects, but also provide opportunities to enable biomimetic synthesis of notable bio-composites based on organic-inorganic complexation. © Korean Institute of Chemical Engineers, Seoul, Korea 2016 |
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Recombinant production and biochemical characterization of a hypothetical acidic shell matrix protein in Escherichia coli for the preparation of protein-based $ CaCO_{3} $ biominerals |
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https://dx.doi.org/10.1007/s11814-016-0091-9 |
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Song, Wooho Hwang, Dong Soo Hong, Yong-Ki Joo, Jin Choi, Yoo Seong |
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10.1007/s11814-016-0091-9 |
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2024-07-03T13:23:22.121Z |
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| score |
7.3981886 |