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...
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Autor*in:	Zheng, Huabao [verfasserIn] Wang, Xiaolan Chen, Jun Zhu, Ke Zhao, Yuhua Yang, Yunliu Yang, Sheng Jiang, Weihong

Format:	Artikel
Sprache:	Englisch

Erschienen:	2006

Schlagwörter:	Oxirane Yeast Nitrogen Base Integrative Vector Basal Salt Medium Yeast Extract Peptone Dextrose Medium

Anmerkung:	© Springer-Verlag 2005

Übergeordnetes Werk:	Enthalten in: Applied microbiology and biotechnology - Springer Berlin Heidelberg, 1984, 70(2006), 6 vom: 01. Mai, Seite 683-689
Übergeordnetes Werk:	volume:70 ; year:2006 ; number:6 ; day:01 ; month:05 ; pages:683-689

Links:	Volltext

DOI / URN:	10.1007/s00253-005-0158-8

Katalog-ID:	OLC2050705964

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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} $, followed by affinity purification and immobilization on oxirane resin, may serve as an effective process for the manufacture of immobilized DAO for industrial application.
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allfields	10.1007/s00253-005-0158-8 doi (DE-627)OLC2050705964 (DE-He213)s00253-005-0158-8-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Zheng, Huabao verfasserin aut Expression, purification, and immobilization of His-tagged d-amino acid oxidase of Trigonopsis variabilis in Pichia pastoris 2006 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2005 Abstract High-level expression of d-amino acid oxidase (DAO) has been reported in Pichia pastoris by integrating the DAO gene under the control of the alcohol oxidase promoter ($ 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} $, followed by affinity purification and immobilization on oxirane resin, may serve as an effective process for the manufacture of immobilized DAO for industrial application. Oxirane Yeast Nitrogen Base Integrative Vector Basal Salt Medium Yeast Extract Peptone Dextrose Medium Wang, Xiaolan aut Chen, Jun aut Zhu, Ke aut Zhao, Yuhua aut Yang, Yunliu aut Yang, Sheng aut Jiang, Weihong aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 70(2006), 6 vom: 01. Mai, Seite 683-689 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:70 year:2006 number:6 day:01 month:05 pages:683-689 https://doi.org/10.1007/s00253-005-0158-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 70 2006 6 01 05 683-689
spelling	10.1007/s00253-005-0158-8 doi (DE-627)OLC2050705964 (DE-He213)s00253-005-0158-8-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Zheng, Huabao verfasserin aut Expression, purification, and immobilization of His-tagged d-amino acid oxidase of Trigonopsis variabilis in Pichia pastoris 2006 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2005 Abstract High-level expression of d-amino acid oxidase (DAO) has been reported in Pichia pastoris by integrating the DAO gene under the control of the alcohol oxidase promoter ($ 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} $, followed by affinity purification and immobilization on oxirane resin, may serve as an effective process for the manufacture of immobilized DAO for industrial application. Oxirane Yeast Nitrogen Base Integrative Vector Basal Salt Medium Yeast Extract Peptone Dextrose Medium Wang, Xiaolan aut Chen, Jun aut Zhu, Ke aut Zhao, Yuhua aut Yang, Yunliu aut Yang, Sheng aut Jiang, Weihong aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 70(2006), 6 vom: 01. Mai, Seite 683-689 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:70 year:2006 number:6 day:01 month:05 pages:683-689 https://doi.org/10.1007/s00253-005-0158-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 70 2006 6 01 05 683-689
allfields_unstemmed	10.1007/s00253-005-0158-8 doi (DE-627)OLC2050705964 (DE-He213)s00253-005-0158-8-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Zheng, Huabao verfasserin aut Expression, purification, and immobilization of His-tagged d-amino acid oxidase of Trigonopsis variabilis in Pichia pastoris 2006 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2005 Abstract High-level expression of d-amino acid oxidase (DAO) has been reported in Pichia pastoris by integrating the DAO gene under the control of the alcohol oxidase promoter ($ 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} $, followed by affinity purification and immobilization on oxirane resin, may serve as an effective process for the manufacture of immobilized DAO for industrial application. Oxirane Yeast Nitrogen Base Integrative Vector Basal Salt Medium Yeast Extract Peptone Dextrose Medium Wang, Xiaolan aut Chen, Jun aut Zhu, Ke aut Zhao, Yuhua aut Yang, Yunliu aut Yang, Sheng aut Jiang, Weihong aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 70(2006), 6 vom: 01. Mai, Seite 683-689 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:70 year:2006 number:6 day:01 month:05 pages:683-689 https://doi.org/10.1007/s00253-005-0158-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 70 2006 6 01 05 683-689
allfieldsGer	10.1007/s00253-005-0158-8 doi (DE-627)OLC2050705964 (DE-He213)s00253-005-0158-8-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Zheng, Huabao verfasserin aut Expression, purification, and immobilization of His-tagged d-amino acid oxidase of Trigonopsis variabilis in Pichia pastoris 2006 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2005 Abstract High-level expression of d-amino acid oxidase (DAO) has been reported in Pichia pastoris by integrating the DAO gene under the control of the alcohol oxidase promoter ($ 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} $, followed by affinity purification and immobilization on oxirane resin, may serve as an effective process for the manufacture of immobilized DAO for industrial application. Oxirane Yeast Nitrogen Base Integrative Vector Basal Salt Medium Yeast Extract Peptone Dextrose Medium Wang, Xiaolan aut Chen, Jun aut Zhu, Ke aut Zhao, Yuhua aut Yang, Yunliu aut Yang, Sheng aut Jiang, Weihong aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 70(2006), 6 vom: 01. Mai, Seite 683-689 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:70 year:2006 number:6 day:01 month:05 pages:683-689 https://doi.org/10.1007/s00253-005-0158-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 70 2006 6 01 05 683-689
allfieldsSound	10.1007/s00253-005-0158-8 doi (DE-627)OLC2050705964 (DE-He213)s00253-005-0158-8-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Zheng, Huabao verfasserin aut Expression, purification, and immobilization of His-tagged d-amino acid oxidase of Trigonopsis variabilis in Pichia pastoris 2006 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2005 Abstract High-level expression of d-amino acid oxidase (DAO) has been reported in Pichia pastoris by integrating the DAO gene under the control of the alcohol oxidase promoter ($ 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 Yeast Nitrogen Base Integrative Vector Basal Salt Medium Yeast Extract Peptone Dextrose Medium 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 Springer Berlin Heidelberg, 1984 70(2006), 6 vom: 01. Mai, Seite 683-689 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:70 year:2006 number:6 day:01 month:05 pages:683-689 https://doi.org/10.1007/s00253-005-0158-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 70 2006 6 01 05 683-689
language	English
source	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
sourceStr	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
format_phy_str_mv	Article
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topic_facet	Oxirane Yeast Nitrogen Base Integrative Vector Basal Salt Medium Yeast Extract Peptone Dextrose Medium
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container_title	Applied microbiology and biotechnology
authorswithroles_txt_mv	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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author	Zheng, Huabao
spellingShingle	Zheng, Huabao ddc 570 ssgn 12 fid BIODIV 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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topic_title	570 VZ 12 ssgn BIODIV DE-30 fid Expression, purification, and immobilization of His-tagged d-amino acid oxidase of Trigonopsis variabilis in Pichia pastoris Oxirane Yeast Nitrogen Base Integrative Vector Basal Salt Medium Yeast Extract Peptone Dextrose Medium
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title	Expression, purification, and immobilization of His-tagged d-amino acid oxidase of Trigonopsis variabilis in Pichia pastoris
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title_full	Expression, purification, and immobilization of His-tagged d-amino acid oxidase of Trigonopsis variabilis in Pichia pastoris
author_sort	Zheng, Huabao
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author_browse	Zheng, Huabao Wang, Xiaolan Chen, Jun Zhu, Ke Zhao, Yuhua Yang, Yunliu Yang, Sheng Jiang, Weihong
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title_sort	expression, purification, and immobilization of his-tagged d-amino acid oxidase of trigonopsis variabilis in pichia pastoris
title_auth	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
collection_details	GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307
container_issue	6
title_short	Expression, purification, and immobilization of His-tagged d-amino acid oxidase of Trigonopsis variabilis in Pichia pastoris
url	https://doi.org/10.1007/s00253-005-0158-8
remote_bool	false
author2	Wang, Xiaolan Chen, Jun Zhu, Ke Zhao, Yuhua Yang, Yunliu Yang, Sheng Jiang, Weihong
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up_date	2024-07-04T02:38:24.018Z
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