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Molecules 2017, 22(12), 2136;

Monitoring the Activity of Immobilized Lipase with Quinizarin Diester Fluoro-Chromogenic Probe

Instituto de Química de São Carlos, Universidade de São Paulo, São Carlos 13566-590, SP, Brazil
Author to whom correspondence should be addressed.
Received: 1 November 2017 / Revised: 23 November 2017 / Accepted: 1 December 2017 / Published: 4 December 2017
(This article belongs to the Special Issue Lipases and Lipases Modification)
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Quinizarin diester is used as a fluoro-chromogenic substrate of the activity of lipase supported in poly(methylmetacrylate) beads (CALB, Novozym® 435) dispersed in organic solvents. The monoester and diester of quinizarin are both non-fluorescent species contrasting with the enzymatic product quinizarin that shows optical absorption in the visible region and strong fluorescence signal. The enzymatic conversion is accomplished by spectroscopic measurements and it follows a sigmoid curve from which the mean reaction time of the enzymatic process can be determined. This parameter indicates the enzyme activity of the immobilized lipase. Its dependency with the amount of lipase allowed the determination of the ratio of the catalytic rate and the Michaelis constant (kc/Km) and the experimental value found was (1.0 ± 0.1) × 10−2 mg−1/min in the case of quinizarin diacetate. View Full-Text
Keywords: fluorochromic substrate; quinizarin diester; lipase assay; enzyme kinetics fluorochromic substrate; quinizarin diester; lipase assay; enzyme kinetics

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Aparecida Sabatini, C.; Massucatto dos Santos, D.; Matos de Oliveira da Silva, S.; Henrique Gehlen, M. Monitoring the Activity of Immobilized Lipase with Quinizarin Diester Fluoro-Chromogenic Probe. Molecules 2017, 22, 2136.

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