University of North Florida
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Stuart Chalk, Ph.D.
Department of Chemistry
University of North Florida
Phone: 1-904-620-1938
Fax: 1-904-620-3535
Email: schalk@unf.edu
Website: @unf

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Enzyme, cellobiose dehydrogenase

Citations 1

"Spectrophotometric Flow Injection Determination Of Cellobiose Dehydrogenase Activity In Fermentation Samples With 2, 6-dichlorophenolindophenol"
Anal. Chim. Acta 1986 Volume 188, Issue 1 Pages 285-288
Kaj André Holm

Abstract: Cellobiose dehydrogenase activity (range 0.25 to 1 iu mL-1) is monitored by oxidation of cellobiose to cellobionolactone. The cellobiose substrate, the 2,6-dichlorophenolindophenol(I) reagent solution in Tris buffer (pH 7.5) and the gluconolactone(II) solution in acetate buffer are mixed before addition of the enzyme. After incubation at 50°C for 20 s the absorbance is measured at 605 nm. The decrease in absorbance is a measure of enzyme activity, because I is reduced to a colorless compound. The presence of II prevents reaction of any β-glucosidase. With a sample throughput of 120 h-1, the correlation coefficient between the flow and manual procedures is 0.96 (n = 40).
Spectrophotometry Enzyme Heated reaction Method comparison