A method for assaying the rhamnosidase activity of naringinase.

@article{Romero1985AMF,
  title={A method for assaying the rhamnosidase activity of naringinase.},
  author={Carlos Santiago Romero and Arturo Manj{\'o}n and Jaume Bastida and Jos{\'e} Luis Iborra},
  journal={Analytical biochemistry},
  year={1985},
  volume={149 2},
  pages={566-71}
}
The use of the p-nitrophenyl-alpha-L-rhamnopyranoside for the specific measurement of the alpha-rhamnosidase activity of naringinase, by colorimetrically 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 Vmax to be measured, this being impossible to accomplish with naringin, (b… CONTINUE READING

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