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Xylose isomerase : ウィキペディア英語版 | Xylose isomerase
In enzymology, a xylose isomerase () is an enzyme that catalyzes the interconversion of D-xylose and D-xylulose. This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The isomerase has now been observed in nearly a hundred species of bacteria. Xylose-isomerases are also commonly called glucose-isomerases due to their extensive use in the industry to produce high fructose corn syrup from glucose.〔 The systematic name of this enzyme class is D-xylose aldose-ketose-isomerase. Other names in common use include D-xylose isomerase, D-xylose ketoisomerase, and D-xylose ketol-isomerase. ==History== The activity of D-xylose isomerase was first observed by Mitsuhashi and Lampen in 1953 in the bacterium ''Lactobacillus pentosus''. Artificial production through transformed ''E.coli'' have also been successful. D-xylose isomerase was first crystallized was from the ''Lactobacillus brevis'' strain.〔 In 1957, the D-xylose isomerase activity on D-glucose conversion to D-fructose was noted by Kooi and Marshall. It is now known that isomerases have broad substrate specificity. Most pentoses and some hexoses are all substrates for D-xylose isomerase. Some examples include: D-ribose, L-arabinose, L-rhanmose, and D-allose. Conversion of glucose to fructose by xylose isomerase was first patented in the 1960s, however, the process was not industrially viable as the enzymes were suspended in solution, and recycling the enzyme was problematic.〔 An immobile xylose isomerase that was fixed on a solid surface was first developed in Japan by Takanashi.〔 Due to the development of this technology and its application to produce enriched fructose corn syrup(EFCS), sucrose in United States' soft drinks have been almost completely been substituted by EFCS's.〔
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