Access the full text.
Sign up today, get DeepDyve free for 14 days.
O. Lowry, N. Rosebrough, A. Farr, R. Randall (1951)
Protein measurement with the Folin phenol reagent.The Journal of biological chemistry, 193 1
L. Phillips, M. Caldwell (1951)
A Study of the Purification and Properties of a Glucose-forming Amylase from Rhizopus delemar, Gluc Amylase1Journal of the American Chemical Society, 73
Alan Traher, J. Kittrell (1974)
Immobilization of catalase on nickel‐silica aluminaBiotechnology and Bioengineering, 16
D. Sawyer, J. Bagger (1959)
The Lactone-Acid-Salt Equilibria for D-Glucono-δ-lactone and the Hydrolysis Kinetics for this LactoneJournal of the American Chemical Society, 81
N. Nelson (1944)
A PHOTOMETRIC ADAPTATION OF THE SOMOGYI METHOD FOR THE DETERMINATION OF GLUCOSEJournal of Biological Chemistry, 153
F. Duke, M. Weibel, D. Page, V. Bulgrin, J. Luthy (1969)
Glucose oxidase mechanism. Enzyme activation by substrateJournal of the American Chemical Society, 91
H. Weetall (1970)
Storage stability of water-insoluble enzymes convalently coupled to organic and inorganic carriers.Biochimica et biophysica acta, 212 1
M. Jermyn (1960)
Studies on the glucono-δ-lactonase of Psudomonas fluorescensBiochimica et Biophysica Acta, 37
Q. Gibson, B. Swoboda, V. Massey (1964)
KINETICS AND MECHANISM OF ACTION OF GLUCOSE OXIDASE.The Journal of biological chemistry, 239
S. O'neill, P. Dunnill, M. Lilly (1971)
A comparative study of immobilized amyloglucosidase in a packed bed reactor and a continuous feed stirred tank reactorBiotechnology and Bioengineering, 13
J. Pazur, K. Kleppe (1964)
THE OXIDATION OF GLUCOSE AND RELATED COMPOUNDS BY GLUCOSE OXIDASE FROM ASPERGILLUS NIGER.Biochemistry, 3
R. Altomare, P. Greenfield, J. Kittrell (1974)
Letter: Inactivation of immobilized fungal catalase by hydrogen peroxide.Biotechnology and bioengineering, 16 12
W. Evans, D. Payne (1963)
Quantitative determination of glucose and maltose in enzyme reaction mixturesAnalyst, 88
R. Messing (1974)
Simultaneously immobilized glucose oxidase and catalase in controlled‐pore titaniaBiotechnology and Bioengineering, 16
M. Weibel, H. Bright (1971)
The glucose oxidase mechanism. Interpretation of the pH dependence.The Journal of biological chemistry, 246 9
O. Lien (1959)
Determination of Gluconolactone, Galactonolactone, and Their Free Acids by Hydroxamate MethodAnalytical Chemistry, 31
K. Kleppe (1966)
The effect of hydrogen peroxide on glucose oxidase from Aspergillus niger.Biochemistry, 5 1
K. Mansford (1963)
The determination of maltotetraose in starch conversion productsAnalyst, 88
D. Hsieh, R. Silver, R. Mateles (1969)
Use of the glucose oxidase system to measure oxygen transfer ratesBiotechnology and Bioengineering, 11
The kinetic behavior of a system of multiple enzyme in solution has been studied in a variable volume batch reactor at pH 5, controlled dissolved oxygen concentration, and T = 30°C. The enzymes used were glucoamylase (R. delemar), glucose oxidase (A. niger), and gluconolactonase (A. niger), all of which are important commercial biocatalysts, and a disaccharide was employed as the starting substrate. This study includes the basic kinetic properties of individual enzymes and interactions between components of the reaction mixture. Classical Michaelis–Menten single substrate or two substrate kinetic with parameters based on initial rate data predict correctly the batch time course of the sequential reaction network.
Biotechnology and Bioengineering – Wiley
Published: Feb 1, 1977
Read and print from thousands of top scholarly journals.
Already have an account? Log in
Bookmark this article. You can see your Bookmarks on your DeepDyve Library.
To save an article, log in first, or sign up for a DeepDyve account if you don’t already have one.
Copy and paste the desired citation format or use the link below to download a file formatted for EndNote
Access the full text.
Sign up today, get DeepDyve free for 14 days.
All DeepDyve websites use cookies to improve your online experience. They were placed on your computer when you launched this website. You can change your cookie settings through your browser.