2000 Volume 64 Issue 5 Pages 940-947
The glucose isomerase from Streptomyces olivaceoviridis E-86 was purified by chromatographic procedures, showing one single protein band in the SDS-PAGE. The enzyme had high acid stability, and there was no loss in enzyme activity at pH 5.0 after incubation at 60°C for 30 hr. The enzyme had sufficients activity at 60°C, pH 5.5, (which is the reaction condition for a single-step process with a glucoamylase from A. niger), and at 58°C, pH 6.0, (condition with a glucoamylase from R. niveus). By using this acid-stable glucose isomerase, a single-step process to produce high-fructose corn sweetener (HFCS) from liquefied starch was formed without any reductant or other reagents for enzyme stabilization. The HFCS produced was about fifty percent fructose and less than 1.5% unknown oligosaccharides.
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