1985 Volume 49 Issue 7 Pages 2113-2118
Synthesis of trehalose from maltose by a coupled enzyme system with trehalose phosphorylase and maltose phosphorylase has been studied. Trehalose phosphorylase was partially purified from Euglena gracilis and maltose phosphorylase was obtained from Lactobacillus brevis. The optimum pH of the reaction was 6.5-7.0 and the reaction rate was faster in the rection mixture containing a low concentration of phosphate. The final ratio of conversion (the ratio of trehalose to maltose) in the pH range between 6.0 and 8.0 was about 60%.
Immobilized maltose and trehalose phosphorylase in κ-carageenan could be used without any appreciable loss of activity for batch reactions at least 10 times.
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