Improved thermostability of lipase Lip2 from Yarrowia lipolytica through disulfide bond design for preparation of medium-long-medium structured lipids
Lipase Lip2 from Yarrowia lipolytica with great potential value in the enzymatic preparation of medium-long-medium structured lipids (MLM-SLs), but the synthetic efficiency might be limited by its poor thermostability. We identified flexible regions of lipase Lip2 by molecular dynamics (MD) simulati...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Li, Lilang [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2022transfer abstract |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Assessment of urban identity through a matrix of cultural landscapes - Ziyaee, Maryam ELSEVIER, 2017, an official journal of the Swiss Society of Food Science and Technology (SGLWT/SOSSTA) and the International Union of Food Science and Technology (IUFoST), Amsterdam [u.a.] |
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| Übergeordnetes Werk: |
volume:166 ; year:2022 ; day:15 ; month:08 ; pages:0 |
| Links: |
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| DOI / URN: |
10.1016/j.lwt.2022.113786 |
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ELV058539476 |
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| 245 | 1 | 0 | |a Improved thermostability of lipase Lip2 from Yarrowia lipolytica through disulfide bond design for preparation of medium-long-medium structured lipids |
| 264 | 1 | |c 2022transfer abstract | |
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| 520 | |a Lipase Lip2 from Yarrowia lipolytica with great potential value in the enzymatic preparation of medium-long-medium structured lipids (MLM-SLs), but the synthetic efficiency might be limited by its poor thermostability. We identified flexible regions of lipase Lip2 by molecular dynamics (MD) simulation, and then disulfide bonds were engineered into these regions to enhance its thermostability. Compared with the wild type, mutant 4sN with four disulfide bonds showed a 19.22 and 27.75 °C increase in the melting temperature (T m ) and the half-loss temperature at 15 min (T15 50), respectively. The half-life of the wild type at 50 °C was 1.66 min, while that of mutant 4sN at 60 °C was 40.52 min. MD simulation showed that the thermal stability improvement in the mutant was attributed to enhanced structural rigidity. Finally, the MLM-SLs were synthesized from olive oil and caprylic acid with immobilized wild-type and mutant 4sN. Mutant 4sN displayed a 5 °C higher optimum temperature and a higher reaction rate than the wild type. Meanwhile, residual activity of mutant 4sN after 7 consecutive cycles increased by 20.84% compared to the wild type. The increased reaction rate and recyclability of lipase Lip2 provide greater potential for industrial production of MLM-SLs. | ||
| 520 | |a Lipase Lip2 from Yarrowia lipolytica with great potential value in the enzymatic preparation of medium-long-medium structured lipids (MLM-SLs), but the synthetic efficiency might be limited by its poor thermostability. We identified flexible regions of lipase Lip2 by molecular dynamics (MD) simulation, and then disulfide bonds were engineered into these regions to enhance its thermostability. Compared with the wild type, mutant 4sN with four disulfide bonds showed a 19.22 and 27.75 °C increase in the melting temperature (T m ) and the half-loss temperature at 15 min (T15 50), respectively. The half-life of the wild type at 50 °C was 1.66 min, while that of mutant 4sN at 60 °C was 40.52 min. MD simulation showed that the thermal stability improvement in the mutant was attributed to enhanced structural rigidity. Finally, the MLM-SLs were synthesized from olive oil and caprylic acid with immobilized wild-type and mutant 4sN. Mutant 4sN displayed a 5 °C higher optimum temperature and a higher reaction rate than the wild type. Meanwhile, residual activity of mutant 4sN after 7 consecutive cycles increased by 20.84% compared to the wild type. The increased reaction rate and recyclability of lipase Lip2 provide greater potential for industrial production of MLM-SLs. | ||
| 650 | 7 | |a Thermostability |2 Elsevier | |
| 650 | 7 | |a Disulfide bond |2 Elsevier | |
| 650 | 7 | |a Medium-long-medium structured triacylglycerols |2 Elsevier | |
| 650 | 7 | |a Lipase Lip2 |2 Elsevier | |
| 650 | 7 | |a Molecular dynamics simulation |2 Elsevier | |
| 700 | 1 | |a Wu, Weikun |4 oth | |
| 700 | 1 | |a Deng, Zixiao |4 oth | |
| 700 | 1 | |a Zhang, Shihai |4 oth | |
| 700 | 1 | |a Guan, Wutai |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |n Elsevier |a Ziyaee, Maryam ELSEVIER |t Assessment of urban identity through a matrix of cultural landscapes |d 2017 |d an official journal of the Swiss Society of Food Science and Technology (SGLWT/SOSSTA) and the International Union of Food Science and Technology (IUFoST) |g Amsterdam [u.a.] |w (DE-627)ELV004078675 |
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10.1016/j.lwt.2022.113786 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001859.pica (DE-627)ELV058539476 (ELSEVIER)S0023-6438(22)00721-6 DE-627 ger DE-627 rakwb eng 690 VZ 74.12 bkl 74.72 bkl Li, Lilang verfasserin aut Improved thermostability of lipase Lip2 from Yarrowia lipolytica through disulfide bond design for preparation of medium-long-medium structured lipids 2022transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Lipase Lip2 from Yarrowia lipolytica with great potential value in the enzymatic preparation of medium-long-medium structured lipids (MLM-SLs), but the synthetic efficiency might be limited by its poor thermostability. We identified flexible regions of lipase Lip2 by molecular dynamics (MD) simulation, and then disulfide bonds were engineered into these regions to enhance its thermostability. Compared with the wild type, mutant 4sN with four disulfide bonds showed a 19.22 and 27.75 °C increase in the melting temperature (T m ) and the half-loss temperature at 15 min (T15 50), respectively. The half-life of the wild type at 50 °C was 1.66 min, while that of mutant 4sN at 60 °C was 40.52 min. MD simulation showed that the thermal stability improvement in the mutant was attributed to enhanced structural rigidity. Finally, the MLM-SLs were synthesized from olive oil and caprylic acid with immobilized wild-type and mutant 4sN. Mutant 4sN displayed a 5 °C higher optimum temperature and a higher reaction rate than the wild type. Meanwhile, residual activity of mutant 4sN after 7 consecutive cycles increased by 20.84% compared to the wild type. The increased reaction rate and recyclability of lipase Lip2 provide greater potential for industrial production of MLM-SLs. Lipase Lip2 from Yarrowia lipolytica with great potential value in the enzymatic preparation of medium-long-medium structured lipids (MLM-SLs), but the synthetic efficiency might be limited by its poor thermostability. We identified flexible regions of lipase Lip2 by molecular dynamics (MD) simulation, and then disulfide bonds were engineered into these regions to enhance its thermostability. Compared with the wild type, mutant 4sN with four disulfide bonds showed a 19.22 and 27.75 °C increase in the melting temperature (T m ) and the half-loss temperature at 15 min (T15 50), respectively. The half-life of the wild type at 50 °C was 1.66 min, while that of mutant 4sN at 60 °C was 40.52 min. MD simulation showed that the thermal stability improvement in the mutant was attributed to enhanced structural rigidity. Finally, the MLM-SLs were synthesized from olive oil and caprylic acid with immobilized wild-type and mutant 4sN. Mutant 4sN displayed a 5 °C higher optimum temperature and a higher reaction rate than the wild type. Meanwhile, residual activity of mutant 4sN after 7 consecutive cycles increased by 20.84% compared to the wild type. The increased reaction rate and recyclability of lipase Lip2 provide greater potential for industrial production of MLM-SLs. Thermostability Elsevier Disulfide bond Elsevier Medium-long-medium structured triacylglycerols Elsevier Lipase Lip2 Elsevier Molecular dynamics simulation Elsevier Wu, Weikun oth Deng, Zixiao oth Zhang, Shihai oth Guan, Wutai oth Enthalten in Elsevier Ziyaee, Maryam ELSEVIER Assessment of urban identity through a matrix of cultural landscapes 2017 an official journal of the Swiss Society of Food Science and Technology (SGLWT/SOSSTA) and the International Union of Food Science and Technology (IUFoST) Amsterdam [u.a.] (DE-627)ELV004078675 volume:166 year:2022 day:15 month:08 pages:0 https://doi.org/10.1016/j.lwt.2022.113786 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO 74.12 Stadtgeographie Siedlungsgeographie VZ 74.72 Stadtplanung kommunale Planung VZ AR 166 2022 15 0815 0 |
| spelling |
10.1016/j.lwt.2022.113786 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001859.pica (DE-627)ELV058539476 (ELSEVIER)S0023-6438(22)00721-6 DE-627 ger DE-627 rakwb eng 690 VZ 74.12 bkl 74.72 bkl Li, Lilang verfasserin aut Improved thermostability of lipase Lip2 from Yarrowia lipolytica through disulfide bond design for preparation of medium-long-medium structured lipids 2022transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Lipase Lip2 from Yarrowia lipolytica with great potential value in the enzymatic preparation of medium-long-medium structured lipids (MLM-SLs), but the synthetic efficiency might be limited by its poor thermostability. We identified flexible regions of lipase Lip2 by molecular dynamics (MD) simulation, and then disulfide bonds were engineered into these regions to enhance its thermostability. Compared with the wild type, mutant 4sN with four disulfide bonds showed a 19.22 and 27.75 °C increase in the melting temperature (T m ) and the half-loss temperature at 15 min (T15 50), respectively. The half-life of the wild type at 50 °C was 1.66 min, while that of mutant 4sN at 60 °C was 40.52 min. MD simulation showed that the thermal stability improvement in the mutant was attributed to enhanced structural rigidity. Finally, the MLM-SLs were synthesized from olive oil and caprylic acid with immobilized wild-type and mutant 4sN. Mutant 4sN displayed a 5 °C higher optimum temperature and a higher reaction rate than the wild type. Meanwhile, residual activity of mutant 4sN after 7 consecutive cycles increased by 20.84% compared to the wild type. The increased reaction rate and recyclability of lipase Lip2 provide greater potential for industrial production of MLM-SLs. Lipase Lip2 from Yarrowia lipolytica with great potential value in the enzymatic preparation of medium-long-medium structured lipids (MLM-SLs), but the synthetic efficiency might be limited by its poor thermostability. We identified flexible regions of lipase Lip2 by molecular dynamics (MD) simulation, and then disulfide bonds were engineered into these regions to enhance its thermostability. Compared with the wild type, mutant 4sN with four disulfide bonds showed a 19.22 and 27.75 °C increase in the melting temperature (T m ) and the half-loss temperature at 15 min (T15 50), respectively. The half-life of the wild type at 50 °C was 1.66 min, while that of mutant 4sN at 60 °C was 40.52 min. MD simulation showed that the thermal stability improvement in the mutant was attributed to enhanced structural rigidity. Finally, the MLM-SLs were synthesized from olive oil and caprylic acid with immobilized wild-type and mutant 4sN. Mutant 4sN displayed a 5 °C higher optimum temperature and a higher reaction rate than the wild type. Meanwhile, residual activity of mutant 4sN after 7 consecutive cycles increased by 20.84% compared to the wild type. The increased reaction rate and recyclability of lipase Lip2 provide greater potential for industrial production of MLM-SLs. Thermostability Elsevier Disulfide bond Elsevier Medium-long-medium structured triacylglycerols Elsevier Lipase Lip2 Elsevier Molecular dynamics simulation Elsevier Wu, Weikun oth Deng, Zixiao oth Zhang, Shihai oth Guan, Wutai oth Enthalten in Elsevier Ziyaee, Maryam ELSEVIER Assessment of urban identity through a matrix of cultural landscapes 2017 an official journal of the Swiss Society of Food Science and Technology (SGLWT/SOSSTA) and the International Union of Food Science and Technology (IUFoST) Amsterdam [u.a.] (DE-627)ELV004078675 volume:166 year:2022 day:15 month:08 pages:0 https://doi.org/10.1016/j.lwt.2022.113786 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO 74.12 Stadtgeographie Siedlungsgeographie VZ 74.72 Stadtplanung kommunale Planung VZ AR 166 2022 15 0815 0 |
| allfields_unstemmed |
10.1016/j.lwt.2022.113786 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001859.pica (DE-627)ELV058539476 (ELSEVIER)S0023-6438(22)00721-6 DE-627 ger DE-627 rakwb eng 690 VZ 74.12 bkl 74.72 bkl Li, Lilang verfasserin aut Improved thermostability of lipase Lip2 from Yarrowia lipolytica through disulfide bond design for preparation of medium-long-medium structured lipids 2022transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Lipase Lip2 from Yarrowia lipolytica with great potential value in the enzymatic preparation of medium-long-medium structured lipids (MLM-SLs), but the synthetic efficiency might be limited by its poor thermostability. We identified flexible regions of lipase Lip2 by molecular dynamics (MD) simulation, and then disulfide bonds were engineered into these regions to enhance its thermostability. Compared with the wild type, mutant 4sN with four disulfide bonds showed a 19.22 and 27.75 °C increase in the melting temperature (T m ) and the half-loss temperature at 15 min (T15 50), respectively. The half-life of the wild type at 50 °C was 1.66 min, while that of mutant 4sN at 60 °C was 40.52 min. MD simulation showed that the thermal stability improvement in the mutant was attributed to enhanced structural rigidity. Finally, the MLM-SLs were synthesized from olive oil and caprylic acid with immobilized wild-type and mutant 4sN. Mutant 4sN displayed a 5 °C higher optimum temperature and a higher reaction rate than the wild type. Meanwhile, residual activity of mutant 4sN after 7 consecutive cycles increased by 20.84% compared to the wild type. The increased reaction rate and recyclability of lipase Lip2 provide greater potential for industrial production of MLM-SLs. Lipase Lip2 from Yarrowia lipolytica with great potential value in the enzymatic preparation of medium-long-medium structured lipids (MLM-SLs), but the synthetic efficiency might be limited by its poor thermostability. We identified flexible regions of lipase Lip2 by molecular dynamics (MD) simulation, and then disulfide bonds were engineered into these regions to enhance its thermostability. Compared with the wild type, mutant 4sN with four disulfide bonds showed a 19.22 and 27.75 °C increase in the melting temperature (T m ) and the half-loss temperature at 15 min (T15 50), respectively. The half-life of the wild type at 50 °C was 1.66 min, while that of mutant 4sN at 60 °C was 40.52 min. MD simulation showed that the thermal stability improvement in the mutant was attributed to enhanced structural rigidity. Finally, the MLM-SLs were synthesized from olive oil and caprylic acid with immobilized wild-type and mutant 4sN. Mutant 4sN displayed a 5 °C higher optimum temperature and a higher reaction rate than the wild type. Meanwhile, residual activity of mutant 4sN after 7 consecutive cycles increased by 20.84% compared to the wild type. The increased reaction rate and recyclability of lipase Lip2 provide greater potential for industrial production of MLM-SLs. Thermostability Elsevier Disulfide bond Elsevier Medium-long-medium structured triacylglycerols Elsevier Lipase Lip2 Elsevier Molecular dynamics simulation Elsevier Wu, Weikun oth Deng, Zixiao oth Zhang, Shihai oth Guan, Wutai oth Enthalten in Elsevier Ziyaee, Maryam ELSEVIER Assessment of urban identity through a matrix of cultural landscapes 2017 an official journal of the Swiss Society of Food Science and Technology (SGLWT/SOSSTA) and the International Union of Food Science and Technology (IUFoST) Amsterdam [u.a.] (DE-627)ELV004078675 volume:166 year:2022 day:15 month:08 pages:0 https://doi.org/10.1016/j.lwt.2022.113786 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO 74.12 Stadtgeographie Siedlungsgeographie VZ 74.72 Stadtplanung kommunale Planung VZ AR 166 2022 15 0815 0 |
| allfieldsGer |
10.1016/j.lwt.2022.113786 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001859.pica (DE-627)ELV058539476 (ELSEVIER)S0023-6438(22)00721-6 DE-627 ger DE-627 rakwb eng 690 VZ 74.12 bkl 74.72 bkl Li, Lilang verfasserin aut Improved thermostability of lipase Lip2 from Yarrowia lipolytica through disulfide bond design for preparation of medium-long-medium structured lipids 2022transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Lipase Lip2 from Yarrowia lipolytica with great potential value in the enzymatic preparation of medium-long-medium structured lipids (MLM-SLs), but the synthetic efficiency might be limited by its poor thermostability. We identified flexible regions of lipase Lip2 by molecular dynamics (MD) simulation, and then disulfide bonds were engineered into these regions to enhance its thermostability. Compared with the wild type, mutant 4sN with four disulfide bonds showed a 19.22 and 27.75 °C increase in the melting temperature (T m ) and the half-loss temperature at 15 min (T15 50), respectively. The half-life of the wild type at 50 °C was 1.66 min, while that of mutant 4sN at 60 °C was 40.52 min. MD simulation showed that the thermal stability improvement in the mutant was attributed to enhanced structural rigidity. Finally, the MLM-SLs were synthesized from olive oil and caprylic acid with immobilized wild-type and mutant 4sN. Mutant 4sN displayed a 5 °C higher optimum temperature and a higher reaction rate than the wild type. Meanwhile, residual activity of mutant 4sN after 7 consecutive cycles increased by 20.84% compared to the wild type. The increased reaction rate and recyclability of lipase Lip2 provide greater potential for industrial production of MLM-SLs. Lipase Lip2 from Yarrowia lipolytica with great potential value in the enzymatic preparation of medium-long-medium structured lipids (MLM-SLs), but the synthetic efficiency might be limited by its poor thermostability. We identified flexible regions of lipase Lip2 by molecular dynamics (MD) simulation, and then disulfide bonds were engineered into these regions to enhance its thermostability. Compared with the wild type, mutant 4sN with four disulfide bonds showed a 19.22 and 27.75 °C increase in the melting temperature (T m ) and the half-loss temperature at 15 min (T15 50), respectively. The half-life of the wild type at 50 °C was 1.66 min, while that of mutant 4sN at 60 °C was 40.52 min. MD simulation showed that the thermal stability improvement in the mutant was attributed to enhanced structural rigidity. Finally, the MLM-SLs were synthesized from olive oil and caprylic acid with immobilized wild-type and mutant 4sN. Mutant 4sN displayed a 5 °C higher optimum temperature and a higher reaction rate than the wild type. Meanwhile, residual activity of mutant 4sN after 7 consecutive cycles increased by 20.84% compared to the wild type. The increased reaction rate and recyclability of lipase Lip2 provide greater potential for industrial production of MLM-SLs. Thermostability Elsevier Disulfide bond Elsevier Medium-long-medium structured triacylglycerols Elsevier Lipase Lip2 Elsevier Molecular dynamics simulation Elsevier Wu, Weikun oth Deng, Zixiao oth Zhang, Shihai oth Guan, Wutai oth Enthalten in Elsevier Ziyaee, Maryam ELSEVIER Assessment of urban identity through a matrix of cultural landscapes 2017 an official journal of the Swiss Society of Food Science and Technology (SGLWT/SOSSTA) and the International Union of Food Science and Technology (IUFoST) Amsterdam [u.a.] (DE-627)ELV004078675 volume:166 year:2022 day:15 month:08 pages:0 https://doi.org/10.1016/j.lwt.2022.113786 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO 74.12 Stadtgeographie Siedlungsgeographie VZ 74.72 Stadtplanung kommunale Planung VZ AR 166 2022 15 0815 0 |
| allfieldsSound |
10.1016/j.lwt.2022.113786 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001859.pica (DE-627)ELV058539476 (ELSEVIER)S0023-6438(22)00721-6 DE-627 ger DE-627 rakwb eng 690 VZ 74.12 bkl 74.72 bkl Li, Lilang verfasserin aut Improved thermostability of lipase Lip2 from Yarrowia lipolytica through disulfide bond design for preparation of medium-long-medium structured lipids 2022transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Lipase Lip2 from Yarrowia lipolytica with great potential value in the enzymatic preparation of medium-long-medium structured lipids (MLM-SLs), but the synthetic efficiency might be limited by its poor thermostability. We identified flexible regions of lipase Lip2 by molecular dynamics (MD) simulation, and then disulfide bonds were engineered into these regions to enhance its thermostability. Compared with the wild type, mutant 4sN with four disulfide bonds showed a 19.22 and 27.75 °C increase in the melting temperature (T m ) and the half-loss temperature at 15 min (T15 50), respectively. The half-life of the wild type at 50 °C was 1.66 min, while that of mutant 4sN at 60 °C was 40.52 min. MD simulation showed that the thermal stability improvement in the mutant was attributed to enhanced structural rigidity. Finally, the MLM-SLs were synthesized from olive oil and caprylic acid with immobilized wild-type and mutant 4sN. Mutant 4sN displayed a 5 °C higher optimum temperature and a higher reaction rate than the wild type. Meanwhile, residual activity of mutant 4sN after 7 consecutive cycles increased by 20.84% compared to the wild type. The increased reaction rate and recyclability of lipase Lip2 provide greater potential for industrial production of MLM-SLs. Lipase Lip2 from Yarrowia lipolytica with great potential value in the enzymatic preparation of medium-long-medium structured lipids (MLM-SLs), but the synthetic efficiency might be limited by its poor thermostability. We identified flexible regions of lipase Lip2 by molecular dynamics (MD) simulation, and then disulfide bonds were engineered into these regions to enhance its thermostability. Compared with the wild type, mutant 4sN with four disulfide bonds showed a 19.22 and 27.75 °C increase in the melting temperature (T m ) and the half-loss temperature at 15 min (T15 50), respectively. The half-life of the wild type at 50 °C was 1.66 min, while that of mutant 4sN at 60 °C was 40.52 min. MD simulation showed that the thermal stability improvement in the mutant was attributed to enhanced structural rigidity. Finally, the MLM-SLs were synthesized from olive oil and caprylic acid with immobilized wild-type and mutant 4sN. Mutant 4sN displayed a 5 °C higher optimum temperature and a higher reaction rate than the wild type. Meanwhile, residual activity of mutant 4sN after 7 consecutive cycles increased by 20.84% compared to the wild type. The increased reaction rate and recyclability of lipase Lip2 provide greater potential for industrial production of MLM-SLs. Thermostability Elsevier Disulfide bond Elsevier Medium-long-medium structured triacylglycerols Elsevier Lipase Lip2 Elsevier Molecular dynamics simulation Elsevier Wu, Weikun oth Deng, Zixiao oth Zhang, Shihai oth Guan, Wutai oth Enthalten in Elsevier Ziyaee, Maryam ELSEVIER Assessment of urban identity through a matrix of cultural landscapes 2017 an official journal of the Swiss Society of Food Science and Technology (SGLWT/SOSSTA) and the International Union of Food Science and Technology (IUFoST) Amsterdam [u.a.] (DE-627)ELV004078675 volume:166 year:2022 day:15 month:08 pages:0 https://doi.org/10.1016/j.lwt.2022.113786 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO 74.12 Stadtgeographie Siedlungsgeographie VZ 74.72 Stadtplanung kommunale Planung VZ AR 166 2022 15 0815 0 |
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Improved thermostability of lipase Lip2 from Yarrowia lipolytica through disulfide bond design for preparation of medium-long-medium structured lipids |
| abstract |
Lipase Lip2 from Yarrowia lipolytica with great potential value in the enzymatic preparation of medium-long-medium structured lipids (MLM-SLs), but the synthetic efficiency might be limited by its poor thermostability. We identified flexible regions of lipase Lip2 by molecular dynamics (MD) simulation, and then disulfide bonds were engineered into these regions to enhance its thermostability. Compared with the wild type, mutant 4sN with four disulfide bonds showed a 19.22 and 27.75 °C increase in the melting temperature (T m ) and the half-loss temperature at 15 min (T15 50), respectively. The half-life of the wild type at 50 °C was 1.66 min, while that of mutant 4sN at 60 °C was 40.52 min. MD simulation showed that the thermal stability improvement in the mutant was attributed to enhanced structural rigidity. Finally, the MLM-SLs were synthesized from olive oil and caprylic acid with immobilized wild-type and mutant 4sN. Mutant 4sN displayed a 5 °C higher optimum temperature and a higher reaction rate than the wild type. Meanwhile, residual activity of mutant 4sN after 7 consecutive cycles increased by 20.84% compared to the wild type. The increased reaction rate and recyclability of lipase Lip2 provide greater potential for industrial production of MLM-SLs. |
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Lipase Lip2 from Yarrowia lipolytica with great potential value in the enzymatic preparation of medium-long-medium structured lipids (MLM-SLs), but the synthetic efficiency might be limited by its poor thermostability. We identified flexible regions of lipase Lip2 by molecular dynamics (MD) simulation, and then disulfide bonds were engineered into these regions to enhance its thermostability. Compared with the wild type, mutant 4sN with four disulfide bonds showed a 19.22 and 27.75 °C increase in the melting temperature (T m ) and the half-loss temperature at 15 min (T15 50), respectively. The half-life of the wild type at 50 °C was 1.66 min, while that of mutant 4sN at 60 °C was 40.52 min. MD simulation showed that the thermal stability improvement in the mutant was attributed to enhanced structural rigidity. Finally, the MLM-SLs were synthesized from olive oil and caprylic acid with immobilized wild-type and mutant 4sN. Mutant 4sN displayed a 5 °C higher optimum temperature and a higher reaction rate than the wild type. Meanwhile, residual activity of mutant 4sN after 7 consecutive cycles increased by 20.84% compared to the wild type. The increased reaction rate and recyclability of lipase Lip2 provide greater potential for industrial production of MLM-SLs. |
| abstract_unstemmed |
Lipase Lip2 from Yarrowia lipolytica with great potential value in the enzymatic preparation of medium-long-medium structured lipids (MLM-SLs), but the synthetic efficiency might be limited by its poor thermostability. We identified flexible regions of lipase Lip2 by molecular dynamics (MD) simulation, and then disulfide bonds were engineered into these regions to enhance its thermostability. Compared with the wild type, mutant 4sN with four disulfide bonds showed a 19.22 and 27.75 °C increase in the melting temperature (T m ) and the half-loss temperature at 15 min (T15 50), respectively. The half-life of the wild type at 50 °C was 1.66 min, while that of mutant 4sN at 60 °C was 40.52 min. MD simulation showed that the thermal stability improvement in the mutant was attributed to enhanced structural rigidity. Finally, the MLM-SLs were synthesized from olive oil and caprylic acid with immobilized wild-type and mutant 4sN. Mutant 4sN displayed a 5 °C higher optimum temperature and a higher reaction rate than the wild type. Meanwhile, residual activity of mutant 4sN after 7 consecutive cycles increased by 20.84% compared to the wild type. The increased reaction rate and recyclability of lipase Lip2 provide greater potential for industrial production of MLM-SLs. |
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