Expression, purification, and immobilization of His-tagged d-amino acid oxidase of Trigonopsis variabilis in Pichia pastoris
Abstract High-level expression of d-amino acid oxidase (DAO) has been reported in Pichia pastoris by integrating the DAO gene under the control of the alcohol oxidase promoter ($ P_{AOX1} $). However, the time taken to reach peak product concentration is usually long (∼43 h), and cultivation require...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Zheng, Huabao [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2006 |
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| Schlagwörter: |
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| Anmerkung: |
© Springer-Verlag 2005 |
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| Übergeordnetes Werk: |
Enthalten in: Applied microbiology and biotechnology - Berlin : Springer, 1975, 70(2006), 6 vom: 01. Mai, Seite 683-689 |
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| Übergeordnetes Werk: |
volume:70 ; year:2006 ; number:6 ; day:01 ; month:05 ; pages:683-689 |
| Links: |
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| DOI / URN: |
10.1007/s00253-005-0158-8 |
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| Katalog-ID: |
SPR002940485 |
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| 100 | 1 | |a Zheng, Huabao |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Expression, purification, and immobilization of His-tagged d-amino acid oxidase of Trigonopsis variabilis in Pichia pastoris |
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| 520 | |a Abstract High-level expression of d-amino acid oxidase (DAO) has been reported in Pichia pastoris by integrating the DAO gene under the control of the alcohol oxidase promoter ($ P_{AOX1} $). However, the time taken to reach peak product concentration is usually long (∼43 h), and cultivation requires tight regulation of methanol feeding. In this paper, we describe the expression of His-tagged DAO (HDAO) in P. pastoris using the glyceraldehydes-3-phosphate dehydrogenase promoter ($ P_{GAP} $). The maximal level of HDAO expression using the $ P_{GAP} $ integrant is attained in 13 h and is equal to that obtained using the $ P_{AOX1} $ integrant in 43 h. We also explored the possibility of secreting HDAO in P. pastoris. In-frame fusion of Saccharomyces cerevisiae α-factor secretion signal under a $ P_{GAP} $ or $ P_{AOX1} $ resulted in low-level secretion of active HDAO, which was not of practical use. The intracellularly expressed HDAO under $ P_{GAP} $ was purified by agar-based affinity support and then immobilized on Amberzyme oxirane resin. The immobilized HDAO, with specific activity of 75 U $ g^{−1} $ (wet weight), could be recycled more than 14 times without significant loss of activity. The data suggest that intracellular production of HDAO under $ P_{GAP} $, followed by affinity purification and immobilization on oxirane resin, may serve as an effective process for the manufacture of immobilized DAO for industrial application. | ||
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| 700 | 1 | |a Wang, Xiaolan |4 aut | |
| 700 | 1 | |a Chen, Jun |4 aut | |
| 700 | 1 | |a Zhu, Ke |4 aut | |
| 700 | 1 | |a Zhao, Yuhua |4 aut | |
| 700 | 1 | |a Yang, Yunliu |4 aut | |
| 700 | 1 | |a Yang, Sheng |4 aut | |
| 700 | 1 | |a Jiang, Weihong |4 aut | |
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10.1007/s00253-005-0158-8 doi (DE-627)SPR002940485 (SPR)s00253-005-0158-8-e DE-627 ger DE-627 rakwb eng Zheng, Huabao verfasserin aut Expression, purification, and immobilization of His-tagged d-amino acid oxidase of Trigonopsis variabilis in Pichia pastoris 2006 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2005 Abstract High-level expression of d-amino acid oxidase (DAO) has been reported in Pichia pastoris by integrating the DAO gene under the control of the alcohol oxidase promoter ($ P_{AOX1} $). However, the time taken to reach peak product concentration is usually long (∼43 h), and cultivation requires tight regulation of methanol feeding. In this paper, we describe the expression of His-tagged DAO (HDAO) in P. pastoris using the glyceraldehydes-3-phosphate dehydrogenase promoter ($ P_{GAP} $). The maximal level of HDAO expression using the $ P_{GAP} $ integrant is attained in 13 h and is equal to that obtained using the $ P_{AOX1} $ integrant in 43 h. We also explored the possibility of secreting HDAO in P. pastoris. In-frame fusion of Saccharomyces cerevisiae α-factor secretion signal under a $ P_{GAP} $ or $ P_{AOX1} $ resulted in low-level secretion of active HDAO, which was not of practical use. The intracellularly expressed HDAO under $ P_{GAP} $ was purified by agar-based affinity support and then immobilized on Amberzyme oxirane resin. The immobilized HDAO, with specific activity of 75 U $ g^{−1} $ (wet weight), could be recycled more than 14 times without significant loss of activity. The data suggest that intracellular production of HDAO under $ P_{GAP} $, followed by affinity purification and immobilization on oxirane resin, may serve as an effective process for the manufacture of immobilized DAO for industrial application. Oxirane (dpeaa)DE-He213 Yeast Nitrogen Base (dpeaa)DE-He213 Integrative Vector (dpeaa)DE-He213 Basal Salt Medium (dpeaa)DE-He213 Yeast Extract Peptone Dextrose Medium (dpeaa)DE-He213 Wang, Xiaolan aut Chen, Jun aut Zhu, Ke aut Zhao, Yuhua aut Yang, Yunliu aut Yang, Sheng aut Jiang, Weihong aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 70(2006), 6 vom: 01. Mai, Seite 683-689 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:70 year:2006 number:6 day:01 month:05 pages:683-689 https://dx.doi.org/10.1007/s00253-005-0158-8 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_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_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 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_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 70 2006 6 01 05 683-689 |
| spelling |
10.1007/s00253-005-0158-8 doi (DE-627)SPR002940485 (SPR)s00253-005-0158-8-e DE-627 ger DE-627 rakwb eng Zheng, Huabao verfasserin aut Expression, purification, and immobilization of His-tagged d-amino acid oxidase of Trigonopsis variabilis in Pichia pastoris 2006 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2005 Abstract High-level expression of d-amino acid oxidase (DAO) has been reported in Pichia pastoris by integrating the DAO gene under the control of the alcohol oxidase promoter ($ P_{AOX1} $). However, the time taken to reach peak product concentration is usually long (∼43 h), and cultivation requires tight regulation of methanol feeding. In this paper, we describe the expression of His-tagged DAO (HDAO) in P. pastoris using the glyceraldehydes-3-phosphate dehydrogenase promoter ($ P_{GAP} $). The maximal level of HDAO expression using the $ P_{GAP} $ integrant is attained in 13 h and is equal to that obtained using the $ P_{AOX1} $ integrant in 43 h. We also explored the possibility of secreting HDAO in P. pastoris. In-frame fusion of Saccharomyces cerevisiae α-factor secretion signal under a $ P_{GAP} $ or $ P_{AOX1} $ resulted in low-level secretion of active HDAO, which was not of practical use. The intracellularly expressed HDAO under $ P_{GAP} $ was purified by agar-based affinity support and then immobilized on Amberzyme oxirane resin. The immobilized HDAO, with specific activity of 75 U $ g^{−1} $ (wet weight), could be recycled more than 14 times without significant loss of activity. The data suggest that intracellular production of HDAO under $ P_{GAP} $, followed by affinity purification and immobilization on oxirane resin, may serve as an effective process for the manufacture of immobilized DAO for industrial application. Oxirane (dpeaa)DE-He213 Yeast Nitrogen Base (dpeaa)DE-He213 Integrative Vector (dpeaa)DE-He213 Basal Salt Medium (dpeaa)DE-He213 Yeast Extract Peptone Dextrose Medium (dpeaa)DE-He213 Wang, Xiaolan aut Chen, Jun aut Zhu, Ke aut Zhao, Yuhua aut Yang, Yunliu aut Yang, Sheng aut Jiang, Weihong aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 70(2006), 6 vom: 01. Mai, Seite 683-689 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:70 year:2006 number:6 day:01 month:05 pages:683-689 https://dx.doi.org/10.1007/s00253-005-0158-8 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_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_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 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_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 70 2006 6 01 05 683-689 |
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10.1007/s00253-005-0158-8 doi (DE-627)SPR002940485 (SPR)s00253-005-0158-8-e DE-627 ger DE-627 rakwb eng Zheng, Huabao verfasserin aut Expression, purification, and immobilization of His-tagged d-amino acid oxidase of Trigonopsis variabilis in Pichia pastoris 2006 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2005 Abstract High-level expression of d-amino acid oxidase (DAO) has been reported in Pichia pastoris by integrating the DAO gene under the control of the alcohol oxidase promoter ($ P_{AOX1} $). However, the time taken to reach peak product concentration is usually long (∼43 h), and cultivation requires tight regulation of methanol feeding. In this paper, we describe the expression of His-tagged DAO (HDAO) in P. pastoris using the glyceraldehydes-3-phosphate dehydrogenase promoter ($ P_{GAP} $). The maximal level of HDAO expression using the $ P_{GAP} $ integrant is attained in 13 h and is equal to that obtained using the $ P_{AOX1} $ integrant in 43 h. We also explored the possibility of secreting HDAO in P. pastoris. In-frame fusion of Saccharomyces cerevisiae α-factor secretion signal under a $ P_{GAP} $ or $ P_{AOX1} $ resulted in low-level secretion of active HDAO, which was not of practical use. The intracellularly expressed HDAO under $ P_{GAP} $ was purified by agar-based affinity support and then immobilized on Amberzyme oxirane resin. The immobilized HDAO, with specific activity of 75 U $ g^{−1} $ (wet weight), could be recycled more than 14 times without significant loss of activity. The data suggest that intracellular production of HDAO under $ P_{GAP} $, followed by affinity purification and immobilization on oxirane resin, may serve as an effective process for the manufacture of immobilized DAO for industrial application. Oxirane (dpeaa)DE-He213 Yeast Nitrogen Base (dpeaa)DE-He213 Integrative Vector (dpeaa)DE-He213 Basal Salt Medium (dpeaa)DE-He213 Yeast Extract Peptone Dextrose Medium (dpeaa)DE-He213 Wang, Xiaolan aut Chen, Jun aut Zhu, Ke aut Zhao, Yuhua aut Yang, Yunliu aut Yang, Sheng aut Jiang, Weihong aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 70(2006), 6 vom: 01. Mai, Seite 683-689 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:70 year:2006 number:6 day:01 month:05 pages:683-689 https://dx.doi.org/10.1007/s00253-005-0158-8 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_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_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 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_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 70 2006 6 01 05 683-689 |
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10.1007/s00253-005-0158-8 doi (DE-627)SPR002940485 (SPR)s00253-005-0158-8-e DE-627 ger DE-627 rakwb eng Zheng, Huabao verfasserin aut Expression, purification, and immobilization of His-tagged d-amino acid oxidase of Trigonopsis variabilis in Pichia pastoris 2006 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2005 Abstract High-level expression of d-amino acid oxidase (DAO) has been reported in Pichia pastoris by integrating the DAO gene under the control of the alcohol oxidase promoter ($ P_{AOX1} $). However, the time taken to reach peak product concentration is usually long (∼43 h), and cultivation requires tight regulation of methanol feeding. In this paper, we describe the expression of His-tagged DAO (HDAO) in P. pastoris using the glyceraldehydes-3-phosphate dehydrogenase promoter ($ P_{GAP} $). The maximal level of HDAO expression using the $ P_{GAP} $ integrant is attained in 13 h and is equal to that obtained using the $ P_{AOX1} $ integrant in 43 h. We also explored the possibility of secreting HDAO in P. pastoris. In-frame fusion of Saccharomyces cerevisiae α-factor secretion signal under a $ P_{GAP} $ or $ P_{AOX1} $ resulted in low-level secretion of active HDAO, which was not of practical use. The intracellularly expressed HDAO under $ P_{GAP} $ was purified by agar-based affinity support and then immobilized on Amberzyme oxirane resin. The immobilized HDAO, with specific activity of 75 U $ g^{−1} $ (wet weight), could be recycled more than 14 times without significant loss of activity. The data suggest that intracellular production of HDAO under $ P_{GAP} $, followed by affinity purification and immobilization on oxirane resin, may serve as an effective process for the manufacture of immobilized DAO for industrial application. Oxirane (dpeaa)DE-He213 Yeast Nitrogen Base (dpeaa)DE-He213 Integrative Vector (dpeaa)DE-He213 Basal Salt Medium (dpeaa)DE-He213 Yeast Extract Peptone Dextrose Medium (dpeaa)DE-He213 Wang, Xiaolan aut Chen, Jun aut Zhu, Ke aut Zhao, Yuhua aut Yang, Yunliu aut Yang, Sheng aut Jiang, Weihong aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 70(2006), 6 vom: 01. Mai, Seite 683-689 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:70 year:2006 number:6 day:01 month:05 pages:683-689 https://dx.doi.org/10.1007/s00253-005-0158-8 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_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_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 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_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 70 2006 6 01 05 683-689 |
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10.1007/s00253-005-0158-8 doi (DE-627)SPR002940485 (SPR)s00253-005-0158-8-e DE-627 ger DE-627 rakwb eng Zheng, Huabao verfasserin aut Expression, purification, and immobilization of His-tagged d-amino acid oxidase of Trigonopsis variabilis in Pichia pastoris 2006 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Springer-Verlag 2005 Abstract High-level expression of d-amino acid oxidase (DAO) has been reported in Pichia pastoris by integrating the DAO gene under the control of the alcohol oxidase promoter ($ P_{AOX1} $). However, the time taken to reach peak product concentration is usually long (∼43 h), and cultivation requires tight regulation of methanol feeding. In this paper, we describe the expression of His-tagged DAO (HDAO) in P. pastoris using the glyceraldehydes-3-phosphate dehydrogenase promoter ($ P_{GAP} $). The maximal level of HDAO expression using the $ P_{GAP} $ integrant is attained in 13 h and is equal to that obtained using the $ P_{AOX1} $ integrant in 43 h. We also explored the possibility of secreting HDAO in P. pastoris. In-frame fusion of Saccharomyces cerevisiae α-factor secretion signal under a $ P_{GAP} $ or $ P_{AOX1} $ resulted in low-level secretion of active HDAO, which was not of practical use. The intracellularly expressed HDAO under $ P_{GAP} $ was purified by agar-based affinity support and then immobilized on Amberzyme oxirane resin. The immobilized HDAO, with specific activity of 75 U $ g^{−1} $ (wet weight), could be recycled more than 14 times without significant loss of activity. The data suggest that intracellular production of HDAO under $ P_{GAP} $, followed by affinity purification and immobilization on oxirane resin, may serve as an effective process for the manufacture of immobilized DAO for industrial application. Oxirane (dpeaa)DE-He213 Yeast Nitrogen Base (dpeaa)DE-He213 Integrative Vector (dpeaa)DE-He213 Basal Salt Medium (dpeaa)DE-He213 Yeast Extract Peptone Dextrose Medium (dpeaa)DE-He213 Wang, Xiaolan aut Chen, Jun aut Zhu, Ke aut Zhao, Yuhua aut Yang, Yunliu aut Yang, Sheng aut Jiang, Weihong aut Enthalten in Applied microbiology and biotechnology Berlin : Springer, 1975 70(2006), 6 vom: 01. Mai, Seite 683-689 (DE-627)265509564 (DE-600)1464336-4 1432-0614 nnns volume:70 year:2006 number:6 day:01 month:05 pages:683-689 https://dx.doi.org/10.1007/s00253-005-0158-8 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_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_165 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_381 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_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2110 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2153 GBV_ILN_2188 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 70 2006 6 01 05 683-689 |
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Enthalten in Applied microbiology and biotechnology 70(2006), 6 vom: 01. Mai, Seite 683-689 volume:70 year:2006 number:6 day:01 month:05 pages:683-689 |
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Enthalten in Applied microbiology and biotechnology 70(2006), 6 vom: 01. Mai, Seite 683-689 volume:70 year:2006 number:6 day:01 month:05 pages:683-689 |
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Zheng, Huabao @@aut@@ Wang, Xiaolan @@aut@@ Chen, Jun @@aut@@ Zhu, Ke @@aut@@ Zhao, Yuhua @@aut@@ Yang, Yunliu @@aut@@ Yang, Sheng @@aut@@ Jiang, Weihong @@aut@@ |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">SPR002940485</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230519170944.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">201001s2006 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1007/s00253-005-0158-8</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)SPR002940485</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(SPR)s00253-005-0158-8-e</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Zheng, Huabao</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Expression, purification, and immobilization of His-tagged d-amino acid oxidase of Trigonopsis variabilis in Pichia pastoris</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2006</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">© Springer-Verlag 2005</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract High-level expression of d-amino acid oxidase (DAO) has been reported in Pichia pastoris by integrating the DAO gene under the control of the alcohol oxidase promoter ($ P_{AOX1} $). However, the time taken to reach peak product concentration is usually long (∼43 h), and cultivation requires tight regulation of methanol feeding. In this paper, we describe the expression of His-tagged DAO (HDAO) in P. pastoris using the glyceraldehydes-3-phosphate dehydrogenase promoter ($ P_{GAP} $). The maximal level of HDAO expression using the $ P_{GAP} $ integrant is attained in 13 h and is equal to that obtained using the $ P_{AOX1} $ integrant in 43 h. We also explored the possibility of secreting HDAO in P. pastoris. In-frame fusion of Saccharomyces cerevisiae α-factor secretion signal under a $ P_{GAP} $ or $ P_{AOX1} $ resulted in low-level secretion of active HDAO, which was not of practical use. The intracellularly expressed HDAO under $ P_{GAP} $ was purified by agar-based affinity support and then immobilized on Amberzyme oxirane resin. The immobilized HDAO, with specific activity of 75 U $ g^{−1} $ (wet weight), could be recycled more than 14 times without significant loss of activity. 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Zheng, Huabao |
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Zheng, Huabao misc Oxirane misc Yeast Nitrogen Base misc Integrative Vector misc Basal Salt Medium misc Yeast Extract Peptone Dextrose Medium Expression, purification, and immobilization of His-tagged d-amino acid oxidase of Trigonopsis variabilis in Pichia pastoris |
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Expression, purification, and immobilization of His-tagged d-amino acid oxidase of Trigonopsis variabilis in Pichia pastoris Oxirane (dpeaa)DE-He213 Yeast Nitrogen Base (dpeaa)DE-He213 Integrative Vector (dpeaa)DE-He213 Basal Salt Medium (dpeaa)DE-He213 Yeast Extract Peptone Dextrose Medium (dpeaa)DE-He213 |
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Expression, purification, and immobilization of His-tagged d-amino acid oxidase of Trigonopsis variabilis in Pichia pastoris |
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Expression, purification, and immobilization of His-tagged d-amino acid oxidase of Trigonopsis variabilis in Pichia pastoris |
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Zheng, Huabao |
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Zheng, Huabao Wang, Xiaolan Chen, Jun Zhu, Ke Zhao, Yuhua Yang, Yunliu Yang, Sheng Jiang, Weihong |
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expression, purification, and immobilization of his-tagged d-amino acid oxidase of trigonopsis variabilis in pichia pastoris |
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Expression, purification, and immobilization of His-tagged d-amino acid oxidase of Trigonopsis variabilis in Pichia pastoris |
| abstract |
Abstract High-level expression of d-amino acid oxidase (DAO) has been reported in Pichia pastoris by integrating the DAO gene under the control of the alcohol oxidase promoter ($ P_{AOX1} $). However, the time taken to reach peak product concentration is usually long (∼43 h), and cultivation requires tight regulation of methanol feeding. In this paper, we describe the expression of His-tagged DAO (HDAO) in P. pastoris using the glyceraldehydes-3-phosphate dehydrogenase promoter ($ P_{GAP} $). The maximal level of HDAO expression using the $ P_{GAP} $ integrant is attained in 13 h and is equal to that obtained using the $ P_{AOX1} $ integrant in 43 h. We also explored the possibility of secreting HDAO in P. pastoris. In-frame fusion of Saccharomyces cerevisiae α-factor secretion signal under a $ P_{GAP} $ or $ P_{AOX1} $ resulted in low-level secretion of active HDAO, which was not of practical use. The intracellularly expressed HDAO under $ P_{GAP} $ was purified by agar-based affinity support and then immobilized on Amberzyme oxirane resin. The immobilized HDAO, with specific activity of 75 U $ g^{−1} $ (wet weight), could be recycled more than 14 times without significant loss of activity. The data suggest that intracellular production of HDAO under $ P_{GAP} $, followed by affinity purification and immobilization on oxirane resin, may serve as an effective process for the manufacture of immobilized DAO for industrial application. © Springer-Verlag 2005 |
| abstractGer |
Abstract High-level expression of d-amino acid oxidase (DAO) has been reported in Pichia pastoris by integrating the DAO gene under the control of the alcohol oxidase promoter ($ P_{AOX1} $). However, the time taken to reach peak product concentration is usually long (∼43 h), and cultivation requires tight regulation of methanol feeding. In this paper, we describe the expression of His-tagged DAO (HDAO) in P. pastoris using the glyceraldehydes-3-phosphate dehydrogenase promoter ($ P_{GAP} $). The maximal level of HDAO expression using the $ P_{GAP} $ integrant is attained in 13 h and is equal to that obtained using the $ P_{AOX1} $ integrant in 43 h. We also explored the possibility of secreting HDAO in P. pastoris. In-frame fusion of Saccharomyces cerevisiae α-factor secretion signal under a $ P_{GAP} $ or $ P_{AOX1} $ resulted in low-level secretion of active HDAO, which was not of practical use. The intracellularly expressed HDAO under $ P_{GAP} $ was purified by agar-based affinity support and then immobilized on Amberzyme oxirane resin. The immobilized HDAO, with specific activity of 75 U $ g^{−1} $ (wet weight), could be recycled more than 14 times without significant loss of activity. The data suggest that intracellular production of HDAO under $ P_{GAP} $, followed by affinity purification and immobilization on oxirane resin, may serve as an effective process for the manufacture of immobilized DAO for industrial application. © Springer-Verlag 2005 |
| abstract_unstemmed |
Abstract High-level expression of d-amino acid oxidase (DAO) has been reported in Pichia pastoris by integrating the DAO gene under the control of the alcohol oxidase promoter ($ P_{AOX1} $). However, the time taken to reach peak product concentration is usually long (∼43 h), and cultivation requires tight regulation of methanol feeding. In this paper, we describe the expression of His-tagged DAO (HDAO) in P. pastoris using the glyceraldehydes-3-phosphate dehydrogenase promoter ($ P_{GAP} $). The maximal level of HDAO expression using the $ P_{GAP} $ integrant is attained in 13 h and is equal to that obtained using the $ P_{AOX1} $ integrant in 43 h. We also explored the possibility of secreting HDAO in P. pastoris. In-frame fusion of Saccharomyces cerevisiae α-factor secretion signal under a $ P_{GAP} $ or $ P_{AOX1} $ resulted in low-level secretion of active HDAO, which was not of practical use. The intracellularly expressed HDAO under $ P_{GAP} $ was purified by agar-based affinity support and then immobilized on Amberzyme oxirane resin. The immobilized HDAO, with specific activity of 75 U $ g^{−1} $ (wet weight), could be recycled more than 14 times without significant loss of activity. The data suggest that intracellular production of HDAO under $ P_{GAP} $, followed by affinity purification and immobilization on oxirane resin, may serve as an effective process for the manufacture of immobilized DAO for industrial application. © Springer-Verlag 2005 |
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| container_issue |
6 |
| title_short |
Expression, purification, and immobilization of His-tagged d-amino acid oxidase of Trigonopsis variabilis in Pichia pastoris |
| url |
https://dx.doi.org/10.1007/s00253-005-0158-8 |
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Wang, Xiaolan Chen, Jun Zhu, Ke Zhao, Yuhua Yang, Yunliu Yang, Sheng Jiang, Weihong |
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Wang, Xiaolan Chen, Jun Zhu, Ke Zhao, Yuhua Yang, Yunliu Yang, Sheng Jiang, Weihong |
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| doi_str |
10.1007/s00253-005-0158-8 |
| up_date |
2024-07-03T16:12:46.332Z |
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|
| score |
7.400895 |