Polyethylene glycols enhance the thermostability of β-cyclodextrin glycosyltransferase from Bacillus circulans
• PEG 400 enhances the activity of β-cyclodextrin glycosyltransferase by 20%. • PEG 1000 prolongs the half-life of this enzyme at 60°C by 6.5-fold. • Fluorescence spectroscopy shows that PEGs protect tertiary structure. • Circular dichroism shows that PEGs protect secondary structure.
Gespeichert in:
| Autor*in: |
Li, Caiming [verfasserIn] |
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| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
2014 |
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| Schlagwörter: |
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| Umfang: |
6 |
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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.] |
|---|---|
| Übergeordnetes Werk: |
volume:164 ; year:2014 ; day:1 ; month:12 ; pages:17-22 ; extent:6 |
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| DOI / URN: |
10.1016/j.foodchem.2014.05.013 |
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Enthalten in Temperature and the field dependence of the magnetization close to order–disorder phase transitions in DMMn and the chromium-doped DMMn New York, NY [u.a.] volume:164 year:2014 day:1 month:12 pages:17-22 extent:6 |
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• PEG 400 enhances the activity of β-cyclodextrin glycosyltransferase by 20%. • PEG 1000 prolongs the half-life of this enzyme at 60°C by 6.5-fold. • Fluorescence spectroscopy shows that PEGs protect tertiary structure. • Circular dichroism shows that PEGs protect secondary structure. |
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• PEG 400 enhances the activity of β-cyclodextrin glycosyltransferase by 20%. • PEG 1000 prolongs the half-life of this enzyme at 60°C by 6.5-fold. • Fluorescence spectroscopy shows that PEGs protect tertiary structure. • Circular dichroism shows that PEGs protect secondary structure. |
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