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A method for assaying the rhamnosidase activity of naringinase

✍ Scribed by Carmen Romero; Arturo Manjón; Josefa Bastida; JoséL. Iborra

Publisher
Elsevier Science
Year
1985
Tongue
English
Weight
469 KB
Volume
149
Category
Article
ISSN
0003-2697

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✦ Synopsis

The use of the p-nitrophenyl-cu-L-rhamnopyranoside for the specific measurement of the (Yrhamnosidase activity of naringinase, by calorimetrically following the appearance of p-nitrophenolate anion, is proposed. Use of this synthetic substrate did not change the pH, temperature, or ionic strength optima of the enzyme. It did, however, result in (a) a decrease of the Michaelis constant of the enzyme, allowing the V ,,,= to be measured, this being impossible to accomplish with naringin, (b) an increase in the sensitivity of the assay to the presence of inhibitors in the reaction media, (c) an increase in the sensitivity which enabled measurement of low levels of naringinase due to the high absorptivity of p-nitrophenolate, and (d) a quick and cheap method of evaluating the cu-rhamnosidase activity of naringinase. 0 1985 Academic Pre~$ Inc.

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