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Katsumi Nakao

Researcher at Yamaguchi University

Publications -  70
Citations -  1356

Katsumi Nakao is an academic researcher from Yamaguchi University. The author has contributed to research in topics: Glucose oxidase & Lipase. The author has an hindex of 21, co-authored 70 publications receiving 1282 citations.

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Competitive inhibition by hydrogen peroxide produced in glucose oxidation catalyzed by glucose oxidase

TL;DR: In this article, it was shown that the inhibition of free glucose oxidase catalyzed reaction with an appreciable amount of hydrogen peroxide produced is almost equal to the apparent Michaelis constant with respect to oxygen KM.
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Effects of ultrasonic intensity and reactor scale on kinetics of enzymatic saccharification of various waste papers in continuously irradiated stirred tanks

TL;DR: The previous kinetic model was found to be applicable to analyze and simulate the saccharification of each waste paper in the different ultrasonic reactors and neither the apparent Michaelis constant, product inhibition constant nor glucose formation equilibrium constant was influenced by the specific ultrasonic intensity.
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Characterization and immobilization of liposome-bound cellulase for hydrolysis of insoluble cellulose.

TL;DR: The results showed that the immobilized liposome-bound cellulase had the higher remaining cellulase activity and reusability than the conventionally immobilized cellulase for the hydrolysis of either soluble or insoluble cellulose.
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A Kinetic Study on Air Oxidation of Glucose Catalyzed by Immobilized Glucose Oxidase for Production of Calcium Gluconate

TL;DR: The kinetic studies on air oxidation of glucose catalyzed by free and immobilized glucose oxidase were carried out in the gluconate buffer solution and the values of the constant KI were found to be almost equal to those of the Michaelis constant KM.
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Stabilization of quaternary structure and activity of bovine liver catalase through encapsulation in liposomes

TL;DR: In this paper, catalase was encapsulated in an aqueous phase of the phospholipid vesicle (liposome) to improve the stability of its tetrameric structure and activity.