Determination of aluminium in water by flow injection with fluorimetric detection by using salicylaldehyde carbohydrazone as reagent in a micellar medium

The Analyst ◽  
1994 ◽  
Vol 119 (6) ◽  
pp. 1221-1223 ◽  
Author(s):  
F. Sánchez Rojas ◽  
E. Cristófol Alcaraz ◽  
J. M. Cano Pavón
Keyword(s):  
Flow Injection ◽  
Micellar Medium ◽  
Fluorimetric Detection

Determination of zinc by flow injection with fluorimetric detection in a micellar medium

1996 ◽  
Vol 355 (1) ◽  
pp. 88-91 ◽  
Author(s):  
N. Gañán Gutiérrez ◽  
F. Sánchez Rojas ◽  
J. M. Cano Pavón
Keyword(s):  
Flow Injection ◽  
Micellar Medium ◽  
Fluorimetric Detection

Exploitation of micellar medium for photochemical-spectrofluorimetric flow-injection determination of fenvalerate

1999 ◽  
Vol 34 (2) ◽  
pp. 143-148 ◽  
Author(s):  
Nelson Maniasso ◽  
Elias A.G. Zagatto ◽  
Salette Reis ◽  
João L.M. Santos ◽  
José L.F.C. Lima
Keyword(s):  
Flow Injection ◽  
Micellar Medium

Determination of the Depolymerisation Kinetics of Amylose, Amylopectin and Maltodextrin by Aspergillus niger Glucoamylase Using a 2-p-toluidinylnaphthalene-6-sulfonate/Flow-injection Analysis System with Fluorimetric Detection

2005 ◽  
Vol 11 (2) ◽  
pp. 139-147 ◽  
Author(s):  
N. Batlle ◽  
J. V. Carbonell ◽  
J. M. Sendra
Keyword(s):  
Aspergillus Niger ◽  
Exponential Decay ◽  
Flow Injection ◽  
Flow Injection Analysis ◽  
Decay Curve ◽  
Fluorimetric Detection ◽  
Flow Injection Analysis System ◽  
Analysis System ◽  
Kinetics Of

This work describes the determination of depolymerisation kinetics of amylose, amylopectin and maltodextrin by Aspergillus niger glucoamylase using a flow-injection analysis system with fluorimetric detection and 2- p-toluidinylnaphthalene-2-sulfonate as the fluorescent probe. Experimental data corresponding to the time evolution of the concentration of detectable substrate were fitted to a single exponential decay curve in the case of amylose (linear substrate) and to a double exponential decay curve in the case of amylopectin and maltodextrin (ramified substrates). For all the substrates assayed, the depolymerisation rates at time zero correlated well with the initial substrate and enzyme concentrations through the Michaelis-Menten hyperbola. Therefore, this methodology allowed the determination of glucoamylase activity using any of these substrates. The determined value of the enzymic constant K m was lower for amylose than for amylopectin and maltodextrin, thus reflecting the higher difficulty of glucoamylase to hydrolyse the (1,6) when compared to the (1,4) linkages. In contrast, the values obtained for the rate constant k3 were very similar for all the substrates assayed.

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