Reactivity of trypsin in reverse micelles: pH-effects on the W0 versus enzyme activity profiles.

@article{Fadnavis1998ReactivityOT,
  title={Reactivity of trypsin in reverse micelles: pH-effects on the W0 versus enzyme activity profiles.},
  author={Nitin Wasantrao Fadnavis and Ramesh Babu and Ashlesha Deshpande},
  journal={Biochimie},
  year={1998},
  volume={80 12},
  pages={1025-30}
}
pH-Dependence of hydrolytic activity of trypsin has been studied in cationic reverse micellar system of cetyltrimethylammonium bromide (CTAB) in (50% v/v) chloroform/isooctane using a positively charged substrate N(alpha)-benzoyl-L-arginine ethyl ester (BAEE). The pH of the medium was varied from 4.0 to 8.5 with addition of 0.025 M citrate-phosphate buffer containing 1 mM CaCl2. Optimum pH for maximum enzyme activity, pH(opt) in reverse micelles is found to be similar to that observed in bulk… CONTINUE READING