STUDIES ON GLUCOSE DEHYDROGENASE OF ASPERGILLUS ORYZAE .3. GENERAL ENZYMATIC PROPERTIES
STUDIES ON GLUCOSE DEHYDROGENASE OF ASPERGILLUS ORYZAE .3. GENERAL ENZYMATIC PROPERTIES
复制标题
DOI:
10.1016/0005-2744(67)90218-5
复制
发表时间:
1967-01-01
期刊:
影响因子:
--
通讯作者:
BAK, TG
中科院分区:
文献类型:
--
作者:
BAK, TG
Glucose dehydrogenase, highly purified, from Aspergillus oryzae catalyzed the oxidation of D-glucose, 2-deoxy-D-glucose, D-xylose, D-fructose, and D-mannose by certain redox dyes such as 2,6-dlchloro-phenollndophenol (DCIP) and qulnones such as [beta]-naphthoquinone. Molecular oxygen could also be utilized as acceptor, though at an extremely slow rate. The oxidation product of D-glucose was identified as D-glucono-8-lactone. The oxidation of glucose by DCIP was maximal at pH 6.5 and 45[degree]. The apparent Km values for D-glucose and DCIP were 0.025 M arid 0.1 mM, respectively. Kinetic studies ruled out the involvement of a ternary complex in the enzyme catalysis. Spectro-photometrlc titration of the enzyme with glucose did not give any indication of the formation of flavin semiqulnone during the catalysis. The dehydrogenatlon of glucose by the enzyme was shown to be Irreversible, since glucono-[delta] -lactone failed to reoxldlze the reduced flavin of the enzyme.