When the solubilizing activity of a microbial cellulase complex (e.g., Trichoderma viride) is determined with conventional methods based on formation of reducing sugars, the results depend on the concentration ratio of cellobiose and glucose in the reaction mixture and thus on the/3-glucosidase pres
A spectrophotometric method for determination of the solubilizing activity of cellulase complexes
β Scribed by Spas D. Spasov; Miglena E. Stefanova; Dimiter N. Kolev
- Publisher
- Springer Vienna
- Year
- 1989
- Tongue
- English
- Weight
- 168 KB
- Volume
- 120
- Category
- Article
- ISSN
- 0026-9247
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
Elastiti ptqxtrationa stainetl wit11 Cotigo red ( 1,l or Oweitt (2) xc tliv substrates cOtntnottly uwl for the rlctvrtninatioti Of c~ladolytic activity.
A sensitive and rapid spectrophotometric method for determination of glucose-6-phosphatase activity is described. Glucose formed by the enzyme is oxidized by glucose oxidase to gluconolactone and hydrogen peroxide. The latter, phenol, and 4-aminoantipyrine are converted by peroxidase to quinoneimine
A sensitive, rapid, quantitative method for the determination of the activities of the bifunctional frog epidermis enzyme, tyrosinase (E.C. 1.14.18. l), has been developed. It is a spectrophotometric method using p-coumaric acid and caffeic acid as substrates at pH 7.0. Lineweaver-Burk plots yielded