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[A method for determining theo-diphenoloxidase activity in the pyrocatechol oxidation reaction]
Ukrainskii Biokhimicheskii Zhurnal (1978)
|July 1, 1984
Summary
A new spectrophotometric method accurately measures catecholase activity using pyrocatechol oxidation. This simple assay quantifies diphenoloxidase enzyme function via a stable condensation product.
Area of Science:
- Biochemistry
- Enzymology
Context:
- Diphenoloxidase enzymes play crucial roles in biological processes.
- Accurate measurement of catecholase activity is essential for biochemical research.
Purpose:
- To develop a simple, sensitive, and accurate spectrophotometric method for determining catecholase activity.
- To establish optimal reaction conditions for the proposed assay.
Summary:
- The method utilizes the enzymatic oxidation of pyrocatechol to 1,2-benzoquinone (BQ) in the presence of ethylenediamine sulphate (EDA).
- A stable condensation product (P365) is formed between BQ and EDA, exhibiting strong absorption at 365 nm.
- The molar absorptivity of P365 is determined to be 15500 M-1 cm-1, with optimal conditions at pH 7.0 and 25-30°C.
Impact:
- Provides a valuable tool for quantifying diphenoloxidase activity in various biological samples.
- Offers advantages in simplicity and sensitivity compared to existing methods.
- Facilitates research in fields involving polyphenol oxidase enzymes.