Bioscience Biotechnology and Biochemistry · 2000 · 29 citations · 21 references
Life SciencesBiochemistryMicrobiologyBiocatalysisEnzymologyMicrobial MetabolismCarbohydrate MetabolismEnzyme KineticsFood FermentationStarch ChemistrySugar ProcessingEnzyme ActivityEnzyme Activity RetentionEnzyme-assisted ProcessingHigh-fructose Corn Syrup MetabolismStarch ConversionStarch UtilizationSugar Metabolism During Fermentation
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 degrees C for 30 hr. The enzyme had sufficients activity at 60 degrees C, pH 5.5, (which is the reaction condition for a single-step process with a glucoamylase from A. niger), and at 58 degrees 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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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Ulrich K. Laemmli · Nature · 1970 · 251.6K citations