Production of glucose isomerase in a recombinant strain of Streptomyces lividans
1998
Wang, F. | Whitaker, R.D. | Batt, C.A.
D-Xylose isomerase, also known as D-glucose isomerase, is an intracellular enzyme found in a number of micro-organisms. It catalyzes the reversible isomerization of D-xylose to D-xylulose as well as D-glucose to D-fructose. Since the 1970s, this enzyme has been utilized to produce high-fructose corn syrup from hydrolyzed cornstarch (Chen 1990; Bhosale et al. 1996). All bacteria that normally produce this enzyme require depletion of glucose and/or the addition of xylose to express xylose isomerase although constitutive mutants have been isolated (Chen 1990). Streptomyces murinus DSM 3253 was found to produce about 1.5 times more xylose isomerase without the need for xylose than did the fully induced wild-type (Skoet and Guertler 1987). Streptomyces thermoviolaceus NRRL 15615 that was isolated after ethyl methanesulfonate mutagenesis produced 2.5-fold higher xylose isomerase constitutively, as compared to the fully induced parental strain (S. thermoviolaceus, ATCC 19283; Hafner 1985). S. coelicolor NRRL 15398, an ethyl methanesulfonate-induced mutant, produced relatively the same amount of enzyme in the absence of xylose as did its parent strain (S. coelicolor ATCC 21666) in xylose medium (Hafner and Jackson 1985).
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