Codon optimization, promoter and expression system selection that achieved high-level production of Yarrowia lipolytica lipase in Pichia pastoris
Lipase (EC 3.1.1.3) stands amongst the most important and promising biocatalysts for industrial applications. In this study, in order to realize a high-level expression of the Yarrowia lipolytica lipase gene in Pichia pastoris, we optimized the codon of LIP2 by de novo gene design and synthesis, whi...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Zhou, Wen-Jing [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2015 |
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| Rechteinformationen: |
Nutzungsrecht: Copyright © 2014 Elsevier Inc. All rights reserved. |
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| Schlagwörter: |
Recombinant Proteins - genetics |
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| Übergeordnetes Werk: |
Enthalten in: Enzyme and microbial technology - Amsterdam [u.a.] : Elsevier, 1979, 71(2015), Seite 66-72 |
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| Übergeordnetes Werk: |
volume:71 ; year:2015 ; pages:66-72 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.enzmictec.2014.10.007 |
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| 520 | |a Lipase (EC 3.1.1.3) stands amongst the most important and promising biocatalysts for industrial applications. In this study, in order to realize a high-level expression of the Yarrowia lipolytica lipase gene in Pichia pastoris, we optimized the codon of LIP2 by de novo gene design and synthesis, which significantly improved the lipase expression when compared to the native lip2 gene. We also comparatively analyzed the effects of the promoter types (PAOX1 and PFLD1) and the Pichia expression systems, including the newly developed PichiaPink system, on lipase production and obtained the optimal recombinants. Bench-top scale fermentation studies indicated that the recombinant carrying the codon-optimized lipase gene syn-lip under the control of promoter PAOX1 has a significantly higher lipase production capacity in the fermenter than other types of recombinants. After undergoing methanol inducible expression for 96h, the wet cell weight of Pichia, the lipase activity and the protein content in the fermentation broth reached their highest values of 262g/L, 38,500U/mL and 2.82g/L, respectively. This study has not only greatly facilitated the bioapplication of lipase in industrial fields but the strategies utilized, such as de novo gene design and synthesis, the comparative analysis among promoters and different generations of Pichia expression systems will also be useful as references for future work in this field. | ||
| 540 | |a Nutzungsrecht: Copyright © 2014 Elsevier Inc. All rights reserved. | ||
| 650 | 4 | |a Recombinant Proteins - genetics | |
| 650 | 4 | |a Yarrowia - genetics | |
| 650 | 4 | |a Recombinant Proteins - metabolism | |
| 650 | 4 | |a RNA, Fungal - chemistry | |
| 650 | 4 | |a Fungal Proteins - metabolism | |
| 650 | 4 | |a Pichia - genetics | |
| 650 | 4 | |a Fungal Proteins - genetics | |
| 650 | 4 | |a Codon - genetics | |
| 650 | 4 | |a Lipase - metabolism | |
| 650 | 4 | |a RNA, Fungal - genetics | |
| 650 | 4 | |a RNA, Messenger - genetics | |
| 650 | 4 | |a Yarrowia - enzymology | |
| 650 | 4 | |a Lipase - genetics | |
| 650 | 4 | |a RNA, Messenger - chemistry | |
| 650 | 4 | |a Pichia - enzymology | |
| 700 | 1 | |a Yang, Jiang-Ke |4 oth | |
| 700 | 1 | |a Mao, Lin |4 oth | |
| 700 | 1 | |a Miao, Li-Hong |4 oth | |
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10.1016/j.enzmictec.2014.10.007 doi PQ20160617 (DE-627)OLC1967990727 (DE-599)GBVOLC1967990727 (PRQ)c1670-e3ad448ca84b53b01c5fc88630a987532e5d2c609af8fc79c69d986629815730 (KEY)0090193820150000071000000066codonoptimizationpromoterandexpressionsystemselect DE-627 ger DE-627 rakwb eng 570 610 DNB 42.30 bkl 58.30 bkl Zhou, Wen-Jing verfasserin aut Codon optimization, promoter and expression system selection that achieved high-level production of Yarrowia lipolytica lipase in Pichia pastoris 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Lipase (EC 3.1.1.3) stands amongst the most important and promising biocatalysts for industrial applications. In this study, in order to realize a high-level expression of the Yarrowia lipolytica lipase gene in Pichia pastoris, we optimized the codon of LIP2 by de novo gene design and synthesis, which significantly improved the lipase expression when compared to the native lip2 gene. We also comparatively analyzed the effects of the promoter types (PAOX1 and PFLD1) and the Pichia expression systems, including the newly developed PichiaPink system, on lipase production and obtained the optimal recombinants. Bench-top scale fermentation studies indicated that the recombinant carrying the codon-optimized lipase gene syn-lip under the control of promoter PAOX1 has a significantly higher lipase production capacity in the fermenter than other types of recombinants. After undergoing methanol inducible expression for 96h, the wet cell weight of Pichia, the lipase activity and the protein content in the fermentation broth reached their highest values of 262g/L, 38,500U/mL and 2.82g/L, respectively. This study has not only greatly facilitated the bioapplication of lipase in industrial fields but the strategies utilized, such as de novo gene design and synthesis, the comparative analysis among promoters and different generations of Pichia expression systems will also be useful as references for future work in this field. Nutzungsrecht: Copyright © 2014 Elsevier Inc. All rights reserved. Recombinant Proteins - genetics Yarrowia - genetics Recombinant Proteins - metabolism RNA, Fungal - chemistry Fungal Proteins - metabolism Pichia - genetics Fungal Proteins - genetics Codon - genetics Lipase - metabolism RNA, Fungal - genetics RNA, Messenger - genetics Yarrowia - enzymology Lipase - genetics RNA, Messenger - chemistry Pichia - enzymology Yang, Jiang-Ke oth Mao, Lin oth Miao, Li-Hong oth Enthalten in Enzyme and microbial technology Amsterdam [u.a.] : Elsevier, 1979 71(2015), Seite 66-72 (DE-627)130025216 (DE-600)423729-8 (DE-576)015567141 0141-0229 nnns volume:71 year:2015 pages:66-72 http://dx.doi.org/10.1016/j.enzmictec.2014.10.007 Volltext http://www.ncbi.nlm.nih.gov/pubmed/25765312 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_21 GBV_ILN_70 42.30 AVZ 58.30 AVZ AR 71 2015 66-72 |
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10.1016/j.enzmictec.2014.10.007 doi PQ20160617 (DE-627)OLC1967990727 (DE-599)GBVOLC1967990727 (PRQ)c1670-e3ad448ca84b53b01c5fc88630a987532e5d2c609af8fc79c69d986629815730 (KEY)0090193820150000071000000066codonoptimizationpromoterandexpressionsystemselect DE-627 ger DE-627 rakwb eng 570 610 DNB 42.30 bkl 58.30 bkl Zhou, Wen-Jing verfasserin aut Codon optimization, promoter and expression system selection that achieved high-level production of Yarrowia lipolytica lipase in Pichia pastoris 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Lipase (EC 3.1.1.3) stands amongst the most important and promising biocatalysts for industrial applications. In this study, in order to realize a high-level expression of the Yarrowia lipolytica lipase gene in Pichia pastoris, we optimized the codon of LIP2 by de novo gene design and synthesis, which significantly improved the lipase expression when compared to the native lip2 gene. We also comparatively analyzed the effects of the promoter types (PAOX1 and PFLD1) and the Pichia expression systems, including the newly developed PichiaPink system, on lipase production and obtained the optimal recombinants. Bench-top scale fermentation studies indicated that the recombinant carrying the codon-optimized lipase gene syn-lip under the control of promoter PAOX1 has a significantly higher lipase production capacity in the fermenter than other types of recombinants. After undergoing methanol inducible expression for 96h, the wet cell weight of Pichia, the lipase activity and the protein content in the fermentation broth reached their highest values of 262g/L, 38,500U/mL and 2.82g/L, respectively. This study has not only greatly facilitated the bioapplication of lipase in industrial fields but the strategies utilized, such as de novo gene design and synthesis, the comparative analysis among promoters and different generations of Pichia expression systems will also be useful as references for future work in this field. Nutzungsrecht: Copyright © 2014 Elsevier Inc. All rights reserved. Recombinant Proteins - genetics Yarrowia - genetics Recombinant Proteins - metabolism RNA, Fungal - chemistry Fungal Proteins - metabolism Pichia - genetics Fungal Proteins - genetics Codon - genetics Lipase - metabolism RNA, Fungal - genetics RNA, Messenger - genetics Yarrowia - enzymology Lipase - genetics RNA, Messenger - chemistry Pichia - enzymology Yang, Jiang-Ke oth Mao, Lin oth Miao, Li-Hong oth Enthalten in Enzyme and microbial technology Amsterdam [u.a.] : Elsevier, 1979 71(2015), Seite 66-72 (DE-627)130025216 (DE-600)423729-8 (DE-576)015567141 0141-0229 nnns volume:71 year:2015 pages:66-72 http://dx.doi.org/10.1016/j.enzmictec.2014.10.007 Volltext http://www.ncbi.nlm.nih.gov/pubmed/25765312 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_21 GBV_ILN_70 42.30 AVZ 58.30 AVZ AR 71 2015 66-72 |
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10.1016/j.enzmictec.2014.10.007 doi PQ20160617 (DE-627)OLC1967990727 (DE-599)GBVOLC1967990727 (PRQ)c1670-e3ad448ca84b53b01c5fc88630a987532e5d2c609af8fc79c69d986629815730 (KEY)0090193820150000071000000066codonoptimizationpromoterandexpressionsystemselect DE-627 ger DE-627 rakwb eng 570 610 DNB 42.30 bkl 58.30 bkl Zhou, Wen-Jing verfasserin aut Codon optimization, promoter and expression system selection that achieved high-level production of Yarrowia lipolytica lipase in Pichia pastoris 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Lipase (EC 3.1.1.3) stands amongst the most important and promising biocatalysts for industrial applications. In this study, in order to realize a high-level expression of the Yarrowia lipolytica lipase gene in Pichia pastoris, we optimized the codon of LIP2 by de novo gene design and synthesis, which significantly improved the lipase expression when compared to the native lip2 gene. We also comparatively analyzed the effects of the promoter types (PAOX1 and PFLD1) and the Pichia expression systems, including the newly developed PichiaPink system, on lipase production and obtained the optimal recombinants. Bench-top scale fermentation studies indicated that the recombinant carrying the codon-optimized lipase gene syn-lip under the control of promoter PAOX1 has a significantly higher lipase production capacity in the fermenter than other types of recombinants. After undergoing methanol inducible expression for 96h, the wet cell weight of Pichia, the lipase activity and the protein content in the fermentation broth reached their highest values of 262g/L, 38,500U/mL and 2.82g/L, respectively. This study has not only greatly facilitated the bioapplication of lipase in industrial fields but the strategies utilized, such as de novo gene design and synthesis, the comparative analysis among promoters and different generations of Pichia expression systems will also be useful as references for future work in this field. Nutzungsrecht: Copyright © 2014 Elsevier Inc. All rights reserved. Recombinant Proteins - genetics Yarrowia - genetics Recombinant Proteins - metabolism RNA, Fungal - chemistry Fungal Proteins - metabolism Pichia - genetics Fungal Proteins - genetics Codon - genetics Lipase - metabolism RNA, Fungal - genetics RNA, Messenger - genetics Yarrowia - enzymology Lipase - genetics RNA, Messenger - chemistry Pichia - enzymology Yang, Jiang-Ke oth Mao, Lin oth Miao, Li-Hong oth Enthalten in Enzyme and microbial technology Amsterdam [u.a.] : Elsevier, 1979 71(2015), Seite 66-72 (DE-627)130025216 (DE-600)423729-8 (DE-576)015567141 0141-0229 nnns volume:71 year:2015 pages:66-72 http://dx.doi.org/10.1016/j.enzmictec.2014.10.007 Volltext http://www.ncbi.nlm.nih.gov/pubmed/25765312 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_21 GBV_ILN_70 42.30 AVZ 58.30 AVZ AR 71 2015 66-72 |
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10.1016/j.enzmictec.2014.10.007 doi PQ20160617 (DE-627)OLC1967990727 (DE-599)GBVOLC1967990727 (PRQ)c1670-e3ad448ca84b53b01c5fc88630a987532e5d2c609af8fc79c69d986629815730 (KEY)0090193820150000071000000066codonoptimizationpromoterandexpressionsystemselect DE-627 ger DE-627 rakwb eng 570 610 DNB 42.30 bkl 58.30 bkl Zhou, Wen-Jing verfasserin aut Codon optimization, promoter and expression system selection that achieved high-level production of Yarrowia lipolytica lipase in Pichia pastoris 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Lipase (EC 3.1.1.3) stands amongst the most important and promising biocatalysts for industrial applications. In this study, in order to realize a high-level expression of the Yarrowia lipolytica lipase gene in Pichia pastoris, we optimized the codon of LIP2 by de novo gene design and synthesis, which significantly improved the lipase expression when compared to the native lip2 gene. We also comparatively analyzed the effects of the promoter types (PAOX1 and PFLD1) and the Pichia expression systems, including the newly developed PichiaPink system, on lipase production and obtained the optimal recombinants. Bench-top scale fermentation studies indicated that the recombinant carrying the codon-optimized lipase gene syn-lip under the control of promoter PAOX1 has a significantly higher lipase production capacity in the fermenter than other types of recombinants. After undergoing methanol inducible expression for 96h, the wet cell weight of Pichia, the lipase activity and the protein content in the fermentation broth reached their highest values of 262g/L, 38,500U/mL and 2.82g/L, respectively. This study has not only greatly facilitated the bioapplication of lipase in industrial fields but the strategies utilized, such as de novo gene design and synthesis, the comparative analysis among promoters and different generations of Pichia expression systems will also be useful as references for future work in this field. Nutzungsrecht: Copyright © 2014 Elsevier Inc. All rights reserved. Recombinant Proteins - genetics Yarrowia - genetics Recombinant Proteins - metabolism RNA, Fungal - chemistry Fungal Proteins - metabolism Pichia - genetics Fungal Proteins - genetics Codon - genetics Lipase - metabolism RNA, Fungal - genetics RNA, Messenger - genetics Yarrowia - enzymology Lipase - genetics RNA, Messenger - chemistry Pichia - enzymology Yang, Jiang-Ke oth Mao, Lin oth Miao, Li-Hong oth Enthalten in Enzyme and microbial technology Amsterdam [u.a.] : Elsevier, 1979 71(2015), Seite 66-72 (DE-627)130025216 (DE-600)423729-8 (DE-576)015567141 0141-0229 nnns volume:71 year:2015 pages:66-72 http://dx.doi.org/10.1016/j.enzmictec.2014.10.007 Volltext http://www.ncbi.nlm.nih.gov/pubmed/25765312 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_21 GBV_ILN_70 42.30 AVZ 58.30 AVZ AR 71 2015 66-72 |
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10.1016/j.enzmictec.2014.10.007 doi PQ20160617 (DE-627)OLC1967990727 (DE-599)GBVOLC1967990727 (PRQ)c1670-e3ad448ca84b53b01c5fc88630a987532e5d2c609af8fc79c69d986629815730 (KEY)0090193820150000071000000066codonoptimizationpromoterandexpressionsystemselect DE-627 ger DE-627 rakwb eng 570 610 DNB 42.30 bkl 58.30 bkl Zhou, Wen-Jing verfasserin aut Codon optimization, promoter and expression system selection that achieved high-level production of Yarrowia lipolytica lipase in Pichia pastoris 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Lipase (EC 3.1.1.3) stands amongst the most important and promising biocatalysts for industrial applications. In this study, in order to realize a high-level expression of the Yarrowia lipolytica lipase gene in Pichia pastoris, we optimized the codon of LIP2 by de novo gene design and synthesis, which significantly improved the lipase expression when compared to the native lip2 gene. We also comparatively analyzed the effects of the promoter types (PAOX1 and PFLD1) and the Pichia expression systems, including the newly developed PichiaPink system, on lipase production and obtained the optimal recombinants. Bench-top scale fermentation studies indicated that the recombinant carrying the codon-optimized lipase gene syn-lip under the control of promoter PAOX1 has a significantly higher lipase production capacity in the fermenter than other types of recombinants. After undergoing methanol inducible expression for 96h, the wet cell weight of Pichia, the lipase activity and the protein content in the fermentation broth reached their highest values of 262g/L, 38,500U/mL and 2.82g/L, respectively. This study has not only greatly facilitated the bioapplication of lipase in industrial fields but the strategies utilized, such as de novo gene design and synthesis, the comparative analysis among promoters and different generations of Pichia expression systems will also be useful as references for future work in this field. Nutzungsrecht: Copyright © 2014 Elsevier Inc. All rights reserved. Recombinant Proteins - genetics Yarrowia - genetics Recombinant Proteins - metabolism RNA, Fungal - chemistry Fungal Proteins - metabolism Pichia - genetics Fungal Proteins - genetics Codon - genetics Lipase - metabolism RNA, Fungal - genetics RNA, Messenger - genetics Yarrowia - enzymology Lipase - genetics RNA, Messenger - chemistry Pichia - enzymology Yang, Jiang-Ke oth Mao, Lin oth Miao, Li-Hong oth Enthalten in Enzyme and microbial technology Amsterdam [u.a.] : Elsevier, 1979 71(2015), Seite 66-72 (DE-627)130025216 (DE-600)423729-8 (DE-576)015567141 0141-0229 nnns volume:71 year:2015 pages:66-72 http://dx.doi.org/10.1016/j.enzmictec.2014.10.007 Volltext http://www.ncbi.nlm.nih.gov/pubmed/25765312 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_21 GBV_ILN_70 42.30 AVZ 58.30 AVZ AR 71 2015 66-72 |
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codon optimization, promoter and expression system selection that achieved high-level production of yarrowia lipolytica lipase in pichia pastoris |
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Codon optimization, promoter and expression system selection that achieved high-level production of Yarrowia lipolytica lipase in Pichia pastoris |
| abstract |
Lipase (EC 3.1.1.3) stands amongst the most important and promising biocatalysts for industrial applications. In this study, in order to realize a high-level expression of the Yarrowia lipolytica lipase gene in Pichia pastoris, we optimized the codon of LIP2 by de novo gene design and synthesis, which significantly improved the lipase expression when compared to the native lip2 gene. We also comparatively analyzed the effects of the promoter types (PAOX1 and PFLD1) and the Pichia expression systems, including the newly developed PichiaPink system, on lipase production and obtained the optimal recombinants. Bench-top scale fermentation studies indicated that the recombinant carrying the codon-optimized lipase gene syn-lip under the control of promoter PAOX1 has a significantly higher lipase production capacity in the fermenter than other types of recombinants. After undergoing methanol inducible expression for 96h, the wet cell weight of Pichia, the lipase activity and the protein content in the fermentation broth reached their highest values of 262g/L, 38,500U/mL and 2.82g/L, respectively. This study has not only greatly facilitated the bioapplication of lipase in industrial fields but the strategies utilized, such as de novo gene design and synthesis, the comparative analysis among promoters and different generations of Pichia expression systems will also be useful as references for future work in this field. |
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Lipase (EC 3.1.1.3) stands amongst the most important and promising biocatalysts for industrial applications. In this study, in order to realize a high-level expression of the Yarrowia lipolytica lipase gene in Pichia pastoris, we optimized the codon of LIP2 by de novo gene design and synthesis, which significantly improved the lipase expression when compared to the native lip2 gene. We also comparatively analyzed the effects of the promoter types (PAOX1 and PFLD1) and the Pichia expression systems, including the newly developed PichiaPink system, on lipase production and obtained the optimal recombinants. Bench-top scale fermentation studies indicated that the recombinant carrying the codon-optimized lipase gene syn-lip under the control of promoter PAOX1 has a significantly higher lipase production capacity in the fermenter than other types of recombinants. After undergoing methanol inducible expression for 96h, the wet cell weight of Pichia, the lipase activity and the protein content in the fermentation broth reached their highest values of 262g/L, 38,500U/mL and 2.82g/L, respectively. This study has not only greatly facilitated the bioapplication of lipase in industrial fields but the strategies utilized, such as de novo gene design and synthesis, the comparative analysis among promoters and different generations of Pichia expression systems will also be useful as references for future work in this field. |
| abstract_unstemmed |
Lipase (EC 3.1.1.3) stands amongst the most important and promising biocatalysts for industrial applications. In this study, in order to realize a high-level expression of the Yarrowia lipolytica lipase gene in Pichia pastoris, we optimized the codon of LIP2 by de novo gene design and synthesis, which significantly improved the lipase expression when compared to the native lip2 gene. We also comparatively analyzed the effects of the promoter types (PAOX1 and PFLD1) and the Pichia expression systems, including the newly developed PichiaPink system, on lipase production and obtained the optimal recombinants. Bench-top scale fermentation studies indicated that the recombinant carrying the codon-optimized lipase gene syn-lip under the control of promoter PAOX1 has a significantly higher lipase production capacity in the fermenter than other types of recombinants. After undergoing methanol inducible expression for 96h, the wet cell weight of Pichia, the lipase activity and the protein content in the fermentation broth reached their highest values of 262g/L, 38,500U/mL and 2.82g/L, respectively. This study has not only greatly facilitated the bioapplication of lipase in industrial fields but the strategies utilized, such as de novo gene design and synthesis, the comparative analysis among promoters and different generations of Pichia expression systems will also be useful as references for future work in this field. |
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Codon optimization, promoter and expression system selection that achieved high-level production of Yarrowia lipolytica lipase in Pichia pastoris |
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