A novel sn-1,3 specific lipase from Janibacter sp. as catalysts for the high-yield synthesis of long-medium-long type structured triacylglycerols
• Our novel sn-1,3 specific lipase MAJ1 enabled high-yield synthesis of LML-type TAGs. • The positional specificity index value of lipase MAJ1 reached 96.6. • Lipase MAJ1 exhibited a lower optimal temperature than other sn-1,3 specific lipases. • The thermal stability of lipase MAJ1 improved signifi...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Cui, Ruiguo [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2022 |
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| Schlagwörter: |
Multi-dimensional mass spectrometry-based shotgun lipidomics |
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| Übergeordnetes Werk: |
Enthalten in: Temperature and the field dependence of the magnetization close to order–disorder phase transitions in DMMn and the chromium-doped DMMn - Yurtseven, H. ELSEVIER, 2018, New York, NY [u.a.] |
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| Übergeordnetes Werk: |
volume:366 ; year:2022 ; day:1 ; month:01 ; pages:0 |
| Links: |
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| DOI / URN: |
10.1016/j.foodchem.2021.130523 |
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| 520 | |a • Our novel sn-1,3 specific lipase MAJ1 enabled high-yield synthesis of LML-type TAGs. • The positional specificity index value of lipase MAJ1 reached 96.6. • Lipase MAJ1 exhibited a lower optimal temperature than other sn-1,3 specific lipases. • The thermal stability of lipase MAJ1 improved significantly after immobilization. • The TAG positional isomers were qualified and quantified by MDMS-SL. | ||
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10.1016/j.foodchem.2021.130523 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001983.pica (DE-627)ELV055151663 (ELSEVIER)S0308-8146(21)01529-6 DE-627 ger DE-627 rakwb eng 540 VZ 35.00 bkl Cui, Ruiguo verfasserin aut A novel sn-1,3 specific lipase from Janibacter sp. as catalysts for the high-yield synthesis of long-medium-long type structured triacylglycerols 2022 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier • Our novel sn-1,3 specific lipase MAJ1 enabled high-yield synthesis of LML-type TAGs. • The positional specificity index value of lipase MAJ1 reached 96.6. • Lipase MAJ1 exhibited a lower optimal temperature than other sn-1,3 specific lipases. • The thermal stability of lipase MAJ1 improved significantly after immobilization. • The TAG positional isomers were qualified and quantified by MDMS-SL. Sn-1,3 specific lipase Elsevier Structured triacylglycerols Elsevier Interesterification Elsevier Multi-dimensional mass spectrometry-based shotgun lipidomics Elsevier Long-medium-long type structured triacylglycerols Elsevier Xu, Long oth Lan, Dongming oth Yang, Bo oth Wang, Yonghua oth Enthalten in Elsevier Yurtseven, H. ELSEVIER Temperature and the field dependence of the magnetization close to order–disorder phase transitions in DMMn and the chromium-doped DMMn 2018 New York, NY [u.a.] (DE-627)ELV000463221 volume:366 year:2022 day:1 month:01 pages:0 https://doi.org/10.1016/j.foodchem.2021.130523 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 35.00 Chemie: Allgemeines VZ AR 366 2022 1 0101 0 |
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10.1016/j.foodchem.2021.130523 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001983.pica (DE-627)ELV055151663 (ELSEVIER)S0308-8146(21)01529-6 DE-627 ger DE-627 rakwb eng 540 VZ 35.00 bkl Cui, Ruiguo verfasserin aut A novel sn-1,3 specific lipase from Janibacter sp. as catalysts for the high-yield synthesis of long-medium-long type structured triacylglycerols 2022 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier • Our novel sn-1,3 specific lipase MAJ1 enabled high-yield synthesis of LML-type TAGs. • The positional specificity index value of lipase MAJ1 reached 96.6. • Lipase MAJ1 exhibited a lower optimal temperature than other sn-1,3 specific lipases. • The thermal stability of lipase MAJ1 improved significantly after immobilization. • The TAG positional isomers were qualified and quantified by MDMS-SL. Sn-1,3 specific lipase Elsevier Structured triacylglycerols Elsevier Interesterification Elsevier Multi-dimensional mass spectrometry-based shotgun lipidomics Elsevier Long-medium-long type structured triacylglycerols Elsevier Xu, Long oth Lan, Dongming oth Yang, Bo oth Wang, Yonghua oth Enthalten in Elsevier Yurtseven, H. ELSEVIER Temperature and the field dependence of the magnetization close to order–disorder phase transitions in DMMn and the chromium-doped DMMn 2018 New York, NY [u.a.] (DE-627)ELV000463221 volume:366 year:2022 day:1 month:01 pages:0 https://doi.org/10.1016/j.foodchem.2021.130523 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 35.00 Chemie: Allgemeines VZ AR 366 2022 1 0101 0 |
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10.1016/j.foodchem.2021.130523 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001983.pica (DE-627)ELV055151663 (ELSEVIER)S0308-8146(21)01529-6 DE-627 ger DE-627 rakwb eng 540 VZ 35.00 bkl Cui, Ruiguo verfasserin aut A novel sn-1,3 specific lipase from Janibacter sp. as catalysts for the high-yield synthesis of long-medium-long type structured triacylglycerols 2022 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier • Our novel sn-1,3 specific lipase MAJ1 enabled high-yield synthesis of LML-type TAGs. • The positional specificity index value of lipase MAJ1 reached 96.6. • Lipase MAJ1 exhibited a lower optimal temperature than other sn-1,3 specific lipases. • The thermal stability of lipase MAJ1 improved significantly after immobilization. • The TAG positional isomers were qualified and quantified by MDMS-SL. Sn-1,3 specific lipase Elsevier Structured triacylglycerols Elsevier Interesterification Elsevier Multi-dimensional mass spectrometry-based shotgun lipidomics Elsevier Long-medium-long type structured triacylglycerols Elsevier Xu, Long oth Lan, Dongming oth Yang, Bo oth Wang, Yonghua oth Enthalten in Elsevier Yurtseven, H. ELSEVIER Temperature and the field dependence of the magnetization close to order–disorder phase transitions in DMMn and the chromium-doped DMMn 2018 New York, NY [u.a.] (DE-627)ELV000463221 volume:366 year:2022 day:1 month:01 pages:0 https://doi.org/10.1016/j.foodchem.2021.130523 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 35.00 Chemie: Allgemeines VZ AR 366 2022 1 0101 0 |
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10.1016/j.foodchem.2021.130523 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001983.pica (DE-627)ELV055151663 (ELSEVIER)S0308-8146(21)01529-6 DE-627 ger DE-627 rakwb eng 540 VZ 35.00 bkl Cui, Ruiguo verfasserin aut A novel sn-1,3 specific lipase from Janibacter sp. as catalysts for the high-yield synthesis of long-medium-long type structured triacylglycerols 2022 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier • Our novel sn-1,3 specific lipase MAJ1 enabled high-yield synthesis of LML-type TAGs. • The positional specificity index value of lipase MAJ1 reached 96.6. • Lipase MAJ1 exhibited a lower optimal temperature than other sn-1,3 specific lipases. • The thermal stability of lipase MAJ1 improved significantly after immobilization. • The TAG positional isomers were qualified and quantified by MDMS-SL. Sn-1,3 specific lipase Elsevier Structured triacylglycerols Elsevier Interesterification Elsevier Multi-dimensional mass spectrometry-based shotgun lipidomics Elsevier Long-medium-long type structured triacylglycerols Elsevier Xu, Long oth Lan, Dongming oth Yang, Bo oth Wang, Yonghua oth Enthalten in Elsevier Yurtseven, H. ELSEVIER Temperature and the field dependence of the magnetization close to order–disorder phase transitions in DMMn and the chromium-doped DMMn 2018 New York, NY [u.a.] (DE-627)ELV000463221 volume:366 year:2022 day:1 month:01 pages:0 https://doi.org/10.1016/j.foodchem.2021.130523 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 35.00 Chemie: Allgemeines VZ AR 366 2022 1 0101 0 |
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10.1016/j.foodchem.2021.130523 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001983.pica (DE-627)ELV055151663 (ELSEVIER)S0308-8146(21)01529-6 DE-627 ger DE-627 rakwb eng 540 VZ 35.00 bkl Cui, Ruiguo verfasserin aut A novel sn-1,3 specific lipase from Janibacter sp. as catalysts for the high-yield synthesis of long-medium-long type structured triacylglycerols 2022 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier • Our novel sn-1,3 specific lipase MAJ1 enabled high-yield synthesis of LML-type TAGs. • The positional specificity index value of lipase MAJ1 reached 96.6. • Lipase MAJ1 exhibited a lower optimal temperature than other sn-1,3 specific lipases. • The thermal stability of lipase MAJ1 improved significantly after immobilization. • The TAG positional isomers were qualified and quantified by MDMS-SL. Sn-1,3 specific lipase Elsevier Structured triacylglycerols Elsevier Interesterification Elsevier Multi-dimensional mass spectrometry-based shotgun lipidomics Elsevier Long-medium-long type structured triacylglycerols Elsevier Xu, Long oth Lan, Dongming oth Yang, Bo oth Wang, Yonghua oth Enthalten in Elsevier Yurtseven, H. ELSEVIER Temperature and the field dependence of the magnetization close to order–disorder phase transitions in DMMn and the chromium-doped DMMn 2018 New York, NY [u.a.] (DE-627)ELV000463221 volume:366 year:2022 day:1 month:01 pages:0 https://doi.org/10.1016/j.foodchem.2021.130523 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 35.00 Chemie: Allgemeines VZ AR 366 2022 1 0101 0 |
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a novel sn-1,3 specific lipase from janibacter sp. as catalysts for the high-yield synthesis of long-medium-long type structured triacylglycerols |
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A novel sn-1,3 specific lipase from Janibacter sp. as catalysts for the high-yield synthesis of long-medium-long type structured triacylglycerols |
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• Our novel sn-1,3 specific lipase MAJ1 enabled high-yield synthesis of LML-type TAGs. • The positional specificity index value of lipase MAJ1 reached 96.6. • Lipase MAJ1 exhibited a lower optimal temperature than other sn-1,3 specific lipases. • The thermal stability of lipase MAJ1 improved significantly after immobilization. • The TAG positional isomers were qualified and quantified by MDMS-SL. |
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• Our novel sn-1,3 specific lipase MAJ1 enabled high-yield synthesis of LML-type TAGs. • The positional specificity index value of lipase MAJ1 reached 96.6. • Lipase MAJ1 exhibited a lower optimal temperature than other sn-1,3 specific lipases. • The thermal stability of lipase MAJ1 improved significantly after immobilization. • The TAG positional isomers were qualified and quantified by MDMS-SL. |
| abstract_unstemmed |
• Our novel sn-1,3 specific lipase MAJ1 enabled high-yield synthesis of LML-type TAGs. • The positional specificity index value of lipase MAJ1 reached 96.6. • Lipase MAJ1 exhibited a lower optimal temperature than other sn-1,3 specific lipases. • The thermal stability of lipase MAJ1 improved significantly after immobilization. • The TAG positional isomers were qualified and quantified by MDMS-SL. |
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| title_short |
A novel sn-1,3 specific lipase from Janibacter sp. as catalysts for the high-yield synthesis of long-medium-long type structured triacylglycerols |
| url |
https://doi.org/10.1016/j.foodchem.2021.130523 |
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| author2 |
Xu, Long Lan, Dongming Yang, Bo Wang, Yonghua |
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Xu, Long Lan, Dongming Yang, Bo Wang, Yonghua |
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10.1016/j.foodchem.2021.130523 |
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2024-07-06T16:45:31.739Z |
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