Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1376894 | Bioorganic & Medicinal Chemistry Letters | 2008 | 5 Pages |
A β-galactosidase (from Aspergillus oryzae) preparation viz. EPRP (enzyme precipitated and rinsed with propanol), obtained by the removal of bulk water by precipitation with n-propanol, showed higher biological activity than the lyophilized powder. FT-IR study confirmed that EPRP had retained the α-helical content of the native structure better than the lyophilized form. Use of this formulation of β-galactosidase under low water conditions (temperature 55 °C, reaction time of 4 h) gave enantioselectivity, E > 1000 for the stereoselective synthesis of (R)-(1-phenylethyl)-β-d-galactopyranoside, starting from racemic 1-phenylethanol and d-galactose. For racemic 2-octanol also, EPRP worked better. Under similar conditions, (R)-(2-octyl)-β-d-galactopyranoside was formed with an enantioselectivity, E = 38.
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