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A steady-state kineties study of myrosinase with direct ultraviolet spectrophotometric assay

✍ Scribed by S. Palmieri; O. Leoni; R. Iori

Publisher: Elsevier Science
Year: 1982
Tongue: English
Weight: 317 KB
Volume: 123
Category: Article
ISSN: 0003-2697
DOI: 10.1016/0003-2697(82)90452-3

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✦ Synopsis

Plant myrosinase (EC 3.2.3.1) catalyzes the hydrolysis of mustard oil glucosides to isothiocyanate, glucose, and sulfate. We have developed a spectrophotometric assay for myrosinase activity with sinigrin as substrate which measures the decomposition of the allylglucosinolate by the decrease in absorbance at 227 nm. The assay was linear both with time and with enzyme concentration. In addition, the assay appears useful for continuous monitoring of the enzyme activity, determination of initial rates of reaction, and detailed kinetic studies of myrosinase. The method appears to be suitable for the analysis of crude plant myrosinase preparations during the enzyme purification and also for determining the myrosinase activity in aqueous extracts of cruciferous material.

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✍ C.Nick Pace; Andres Buonanno; Jeannie Simmons-Hansen 📂 Article 📅 1980 🏛 Elsevier Science 🌐 English ⚖ 361 KB

A direct spectrophotometric assay for arginase developed by R. L. Ward and P. A. Srere t 1967. At~crl. Biochem. 18, 102) is extended so that it can be used at pH 7.5 or 9.5. at higher substrate concentrations, for assaying crude sources of arginase. and for steady-state kinetic studies of the enzyme