Abstract
Two cationic peroxidases isolated from Vaccinium myrtillus were encapsulated in reverse micelles of bis(2-ethylhexyl)sodium sulfosuccinate/isooctane. By using a central composite design, some relevant parameters for the enzymatic activity, such as surfactant and water concentration, pH, and buffer molarity, were analyzed. With the results obtained from this experimental planning, the response surface curves were established. The maximum specific activity obtained (0.19 mM/min · mM of enzyme) was approximately the same for both peroxidases, but the experimental conditions under which this value was attained differed considerably.
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Morna-Gomes, A., Serralheiro, M.L., Fevereiro, P.S. et al. Application of factorial design to the optimization of peroxidase activity in reverse micelles of bis(2-ethylhexyl)sodium sulfosuccinate/isooctane. Appl Biochem Biotechnol 82, 27–36 (1999). https://doi.org/10.1385/ABAB:82:1:27
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DOI: https://doi.org/10.1385/ABAB:82:1:27