| Budget Amount *help |
¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 1988: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1987: ¥1,500,000 (Direct Cost: ¥1,500,000)
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| Research Abstract |
1, Streptomyces xylose isomerase (XIase) was purified with the ammonium sulfate fractionation and the DEAE Sephadex column chromatography to be pure in the electrophoretic analysis. With this enzyme preparation, the kinetic parameters, Km and kO were evaluated for some saccharides, eq. glucose, -glucose and fructose. -Glucose was found to be not a substrate. For the kinetic studies, a new method on the observation of the Xiase-catalyzed-reaction was developed on the basis of optical rotation caused by the reaction, glucose fructose, which was continuously recorded on a union automatic digital polarimeter. The optical rotation stopped-flow apparatus was also developed to measure the transient phase (within 1 sec) of the Siase reaction.
2, Interaction of Asp. niger glucoamylase with maltose and isomaltose was observed with kinetic and static methods in the presence or absence of glucose and gluconolactone, and kinetic and static parameters were evaluated for prediction of the binding subsites of these saccharides.
3, Rhizopus blucoamylase and Bacillus liquefying -amylase were immobilized to formyl-cellulofine carrier. These immobilized enzyme preparations were confirmed to be useful for the production of glucose. The latter produces -glucose, which is the substrate of isomerization by XIase. Thus, it will be possible to construct a system with co-immobilized enzymes for the direct production of fructose from starch. A new method for the determination of the liquefying -amylase-catalyzed activity was also developed on the basis of the use of a commercial glucose-kit and maltohexaose as a substrate. This method is very useful for the kinetic studies of the enzyme.
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