The optimization of synthesis conditions for laccase entrapment in mesoporous silica microparticles by response surface methodology

Immobilization of Trametes versicolor laccase on different PGMA‐based polymeric microspheres using response surface methodology: Optimization of conditions

“…The coefficients of determination were determined for both models as R PGMA = 0.90 and R PGMA–NH2 = 0.89, which are very good for biological systems and indicate that 90% and 89%, respectively, of the response variability could be predicted by the model. These after mentioned values of R 2 are in the range of previously published optimization process for laccase immobilization using RSM, indicating that the regression model provides a high correlation between independent variables and the response . Therefore, the adjusted model is adequate to predict the experimental data for immobilization for both carriers.…”

“…The assay consisted of mixing 0.5 m M ABTS and a suitable volume of free or immobilized laccases in a citric acid–Na 2 HPO 4 buffer solution to a total reaction volume of 1 mL. Enzyme activity was reported in U L −1 and was calculated using the following equation, derived from the Beer‐Lambert law: where Δ A is the change in absorbance at 420 nm, V is the reaction volume (L), ɛ is molar extinction coefficient (M −1 cm −1 ), l is the optical path (1 cm), and Δ t is the reaction time (min). One unit of enzyme activity (U) is defined as the amount of enzyme required to oxidize 1 μmol of ABTS per min.…”

“…For that reason, support characteristics, such as the shape, morphology, and reactive groups, as well as the immobilization conditions should be considered. There are many factors that could affect the immobilization efficiency (IE) . An alternative to study the effect of several variables that affect responses to obtain optimum conditions for enzyme immobilization is the use of response surface methodology (RSM).…”

Effects of morphology and pore size of mesoporous silicas on the efficiency of an immobilized enzyme

“…[23][24][25][26][27][28] In general, the results have shown that adsorption, covalent bonding and entrapment mechanisms all provide an effective means of stabilizing enzymes on inorganic, organic or polymeric matrices by increasing the rigidity of the matrix and reducing the unfolding and deactivating possibility. [29][30][31][32] Diaz and Mansor examined the MS entrapment of three different enzymes, namely cytochrome C, papain and trypsin 33,34 It was shown that the trypsin retained a signicant activity for more than one week in the immobilized state, but was totally deactivated aer just 24 h in the free (i.e., solution) state. Wang and Caruso entrapped catalase, peroxidase, cytochrome C, and lysozyme enzymes in MS supports, and showed that all four enzymes exhibited good activity and a long durability.…”

Production of Laccase by a New Myrothecium verrucaria MD-R-16 Isolated from Pigeon Pea [Cajanus cajan (L.) Millsp.] and its Application on Dye Decolorization

“…The values of R 2 and adjusted R 2 were 0.9974 and 0.9950 respectively, which were desirable determination coefficients and had advocated a high correlation between the experimental and predicted values of the response. Meanwhile, a non-significant value of lack of fit ( p > 0.05) and a highly significant level of the model ( p < 0.01) were obtained by statistical analyses, suggesting that the mode could be accurately predicted by the variation [ 38 ]. Therefore, the model can be used for further analysis.…”