Using three enzyme sensors (tyrosinase, catalase and glucose oxidase), capable of functioning also in non-aqueous solvents, we found new correlations between classical indicators, e.g. the log P value of several organic solvents and new empirical indicators such as 'maximum current variation' (MCV) and above all the 'current variation rate' (CVR), the values of which may be monitored with the biosensor considered dipping directly into the organic solvent. The trend of the immobilised specific activity of the tyrosinase enzyme dipping into different organic solvents was evaluated and compared with that determined by the spectrophotometric method. Lastly, an investigation was performed to experimentally verify the relation between hydrophobicity of the solvent and its ability to draw back the water from the enzyme microenvironment using the Karl Fischer method and thermogravimetric analysis to estimate the residual water in the enzyme microenvironment after having treated the enzyme with the organic solvent, then allowing it to dry. (C) 1998 Elsevier Science B.V. All rights reserved.
Further development of catalase, tyrosinase and glucose oxidase based organic phase enzyme electrode response as a function of organic solvent properties / Campanella, Luigi; Favero, Gabriele; Sammartino, Maria Pia; Tomassetti, Mauro. - In: TALANTA. - ISSN 0039-9140. - 46:4(1998), pp. 595-606. [10.1016/s0039-9140(97)00311-1]
Further development of catalase, tyrosinase and glucose oxidase based organic phase enzyme electrode response as a function of organic solvent properties
CAMPANELLA, Luigi;FAVERO, Gabriele;SAMMARTINO, Maria Pia;TOMASSETTI, Mauro
1998
Abstract
Using three enzyme sensors (tyrosinase, catalase and glucose oxidase), capable of functioning also in non-aqueous solvents, we found new correlations between classical indicators, e.g. the log P value of several organic solvents and new empirical indicators such as 'maximum current variation' (MCV) and above all the 'current variation rate' (CVR), the values of which may be monitored with the biosensor considered dipping directly into the organic solvent. The trend of the immobilised specific activity of the tyrosinase enzyme dipping into different organic solvents was evaluated and compared with that determined by the spectrophotometric method. Lastly, an investigation was performed to experimentally verify the relation between hydrophobicity of the solvent and its ability to draw back the water from the enzyme microenvironment using the Karl Fischer method and thermogravimetric analysis to estimate the residual water in the enzyme microenvironment after having treated the enzyme with the organic solvent, then allowing it to dry. (C) 1998 Elsevier Science B.V. All rights reserved.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.