Improving the thermostability and activity of lipoxygenase from Anabaena sp. PCC 7120 by directed evolution and site-directed mutagenesis
Highlights • A mutant lipoxygenase (LOX) was selected through a directed evolution approach. • The mutant enzyme had greater LOX activity and thermostability than the wild-type. • Thermostability doubled. • Amino acid 305 was critical for improving catalytic activity and thermostability. • The role...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Guo, Fangfang [verfasserIn] |
|---|
| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
2014 |
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| Schlagwörter: |
|---|
| Umfang: |
8 |
|---|
| Übergeordnetes Werk: |
Enthalten in: CME Activities Calendar - 2014, Amsterdam [u.a.] |
|---|---|
| Übergeordnetes Werk: |
volume:107 ; year:2014 ; pages:23-30 ; extent:8 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.molcatb.2014.05.016 |
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| 520 | |a Highlights • A mutant lipoxygenase (LOX) was selected through a directed evolution approach. • The mutant enzyme had greater LOX activity and thermostability than the wild-type. • Thermostability doubled. • Amino acid 305 was critical for improving catalytic activity and thermostability. • The role of amino acid 305 was confirmed by site-saturation mutagenesis. | ||
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10.1016/j.molcatb.2014.05.016 doi GBVA2014002000026.pica (DE-627)ELV022412948 (ELSEVIER)S1381-1177(14)00166-0 DE-627 ger DE-627 rakwb eng 540 540 DE-600 610 VZ 610 VZ 44.85 bkl Guo, Fangfang verfasserin aut Improving the thermostability and activity of lipoxygenase from Anabaena sp. PCC 7120 by directed evolution and site-directed mutagenesis 2014 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Highlights • A mutant lipoxygenase (LOX) was selected through a directed evolution approach. • The mutant enzyme had greater LOX activity and thermostability than the wild-type. • Thermostability doubled. • Amino acid 305 was critical for improving catalytic activity and thermostability. • The role of amino acid 305 was confirmed by site-saturation mutagenesis. Thermostability Elsevier Directed evolution Elsevier Activity Elsevier Recombinant lipoxygenase Elsevier Anabaena sp. PCC 7120 Elsevier Zhang, Chong oth Bie, Xiaomei oth Zhao, Haizhen oth Diao, Hanwen oth Lu, Fengxia oth Lu, Zhaoxin oth Enthalten in Elsevier Science CME Activities Calendar 2014 Amsterdam [u.a.] (DE-627)ELV011989025 volume:107 year:2014 pages:23-30 extent:8 https://doi.org/10.1016/j.molcatb.2014.05.016 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 44.85 Kardiologie Angiologie VZ AR 107 2014 23-30 8 045F 540 |
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Improving the thermostability and activity of lipoxygenase from Anabaena sp. PCC 7120 by directed evolution and site-directed mutagenesis |
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Highlights • A mutant lipoxygenase (LOX) was selected through a directed evolution approach. • The mutant enzyme had greater LOX activity and thermostability than the wild-type. • Thermostability doubled. • Amino acid 305 was critical for improving catalytic activity and thermostability. • The role of amino acid 305 was confirmed by site-saturation mutagenesis. |
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Highlights • A mutant lipoxygenase (LOX) was selected through a directed evolution approach. • The mutant enzyme had greater LOX activity and thermostability than the wild-type. • Thermostability doubled. • Amino acid 305 was critical for improving catalytic activity and thermostability. • The role of amino acid 305 was confirmed by site-saturation mutagenesis. |
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Highlights • A mutant lipoxygenase (LOX) was selected through a directed evolution approach. • The mutant enzyme had greater LOX activity and thermostability than the wild-type. • Thermostability doubled. • Amino acid 305 was critical for improving catalytic activity and thermostability. • The role of amino acid 305 was confirmed by site-saturation mutagenesis. |
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