2013 年 77 巻 2 号 p. 385-388
L-Arabinose isomerase from Bacillus thermoglucosidasius KCTC 1828 (BTAI) was expressed in Escherichia coli. The optimal temperature and pH for the activity of the purified BTAI were 40 °C and pH 7.0. The Mn2+ ion was an activator of BTAI activity. The kinetic parameters of BTAI for D-galactose were a Km of 175 mM and a kcat/Km of 2.8 mM−1min−1. The conversion ratio by BTAI to D-tagatose reached 45.6% at 40 °C.
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