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Kinetic properties of polyphenoloxidase in organic solvents A study in Brij 96‐cyclohexane reverse micelles
Author(s) -
Sa´nchez-Ferrer Alvaro,
Bru Roque,
Garci´a-Carmona Francisco
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80461-7
Subject(s) - chemistry , cyclohexane , micelle , aqueous solution , pulmonary surfactant , kinetics , reaction rate constant , chromatography , nuclear chemistry , organic chemistry , biochemistry , physics , quantum mechanics
Polyphenoloxidase entrapped in Brij 96‐cyclohexame reverse micelles showed both cresolase activity towards monophenols and catecholase activity towards diphenols. The kinetic parameters, such as apparent K m , temperature effect and pH profile, were determined for catecholase activity, the findings being very close to those found in aqueous systems. The enzyme activity was dependent on the molecular ratio of water to surfactant (ω o ), obtaining a maximum activity at ω o =10. The stability of the system with time increased with the water content until ω o =10, and then decreased. An inverse relation was found between activity and water volume fraction (θ) when ω o was held constant. In this situation V max was constant while K m varied proportionally with θ.