Downscaling a multicommuted flow injection analysis system for the photometric determination of iodate in table salt

2010 ◽  
Vol 668 (1) ◽  
pp. 3-7 ◽  
Author(s):  
Sivanildo S. Borges ◽  
Jailson de Souza Peixoto ◽  
Mário A. Feres ◽  
Boaventura F. Reis
Keyword(s):  
Flow Injection ◽  
Flow Injection Analysis ◽  
Photometric Determination ◽  
Table Salt ◽  
Flow Injection Analysis System ◽  
Analysis System

scholarly journals Fabrication of a Nitrate Selective Electrode for Determination of Nitrate in Fertilizers by Using Flow Injection Analysis System

2016 ◽  
Vol 20 ◽  
pp. 73-75 ◽  
Author(s):  
Sumonmarn Chaneam ◽  
Waritta Taweetong ◽  
Kampanart Kaewyai ◽  
Pheeraphon Thienwong ◽  
Aekgaraj Takaew ◽  
...  
Keyword(s):  
Flow Injection ◽  
Flow Injection Analysis ◽  
Selective Electrode ◽  
Flow Injection Analysis System ◽  
Analysis System

Computer-controlled flow-injection analysis system for on-line determination of distribution ratios

1988 ◽  
Vol 60 (14) ◽  
pp. 1390-1393 ◽  
Author(s):  
Howard L. Nekimken ◽  
Barbara F. Smith ◽  
Gordon D. Jarvinen ◽  
E. J. Peterson ◽  
Marianne M. Jones
Keyword(s):  
Flow Injection ◽  
Flow Injection Analysis ◽  
Flow Injection Analysis System ◽  
On Line ◽  
Computer Controlled ◽  
Controlled Flow ◽  
Analysis System

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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