Triacetin → Hydrogen Peroxide
反応式
[CH3:1][C:2](=[O:15])[O:3][CH2:4][CH:5]([CH2:10][O:11][C:12](=[O:14])[CH3:13])[O:6][C:7](=[O:9])[CH3:8].C([O-])([O-])=O.C([O-])([O-])=O.OO.OO.OO.[Na+].[Na+].[Na+].[Na+].C([O:37][OH:38])(=O)C>>[CH3:13][C:12](=[O:14])[O:11][CH2:10][CH:5]([CH2:4][O:3][C:2](=[O:15])[CH3:1])[O:6][C:7](=[O:9])[CH3:8].[OH:37][OH:38]参加物
5
実験手順
The procedures described in Example 44 and Example 45 were repeated using total protein from a heat-treated, centrifuged cell extract supernatant from a transformant expressing perhydrolase (SEQ ID NO. 82) from Thermotoga lettingae (KLP18/pSW220, Example 42) or a transformant expressing perhydrolase (SEQ ID NO. 90) from Thermotoga petrophila (KLP18/pSW222, Example 43), except that sodium percarbonate (˜25 wt % H2O2) was substituted for aqueous hydrogen peroxide to produce an initial concentration of either 100 mM or 250 mM hydrogen peroxide. Reactions containing triacetin, sodium percarbonate and heat-treated, centrifuged cell extract supernatant in 50 mM sodium bicarbonate buffer (2 mL total volume, pH 8.1) were run at 24° C. A control reaction for each reaction condition was run to determine the concentration of peracetic acid produced by chemical perhydrolysis of triacetin by hydrogen peroxide in the absence of added extract protein. The concentration of peracetic acid in the reaction mixtures was determined according to the method of Karst et al. described in Example 2. The peracetic acid concentrations produced in 1 min, 5 min and 30 min are listed in Table 31.