INVESTIGADORES
STEGE Patricia Wanda
congresos y reuniones científicas
Título:
Micellar electrokinetic chromathography pre capillary enzyme assay applied to determinate phosphatase activity in semiarid soil.
Autor/es:
PATRICIA W. STEGE; GERMÁN A. MESSINA; GUILLERMO BIANCHI; ROBERTO A. OLSINA
Lugar:
Florianópolis (SC), Brasil
Reunión:
Congreso; COLACRO XII - Congresso Latino-Americano de Cromatografia e Técnicas Relacionadas.; 2008
Resumen:
Nanomaterial-Assisted Signal Enhancement of Hybridization for DNA
Biosensors: A Review
<!--
/* Font Definitions */
@font-face
{font-family:"Cambria Math";
panose-1:2 4 5 3 5 4 6 3 2 4;
mso-font-charset:0;
mso-generic-font-family:roman;
mso-font-pitch:variable;
mso-font-signature:-1610611985 1107304683 0 0 415 0;}
@font-face
{font-family:Calibri;
panose-1:2 15 5 2 2 2 4 3 2 4;
mso-font-charset:0;
mso-generic-font-family:swiss;
mso-font-pitch:variable;
mso-font-signature:-520092929 1073786111 9 0 415 0;}
/* Style Definitions */
p.MsoNormal, li.MsoNormal, div.MsoNormal
{mso-style-unhide:no;
mso-style-qformat:yes;
mso-style-parent:"";
margin:0cm;
margin-bottom:.0001pt;
mso-pagination:widow-orphan;
font-size:12.0pt;
font-family:"Times New Roman","serif";
mso-fareast-font-family:"Times New Roman";
mso-ansi-language:EN-GB;}
p.MsoBodyText, li.MsoBodyText, div.MsoBodyText
{mso-style-unhide:no;
mso-style-link:"Texto independiente Car";
margin:0cm;
margin-bottom:.0001pt;
text-align:center;
mso-pagination:widow-orphan;
font-size:12.0pt;
mso-bidi-font-size:10.0pt;
font-family:"Times New Roman","serif";
mso-fareast-font-family:"Times New Roman";
font-weight:bold;
mso-bidi-font-weight:normal;}
span.TextoindependienteCar
{mso-style-name:"Texto independiente Car";
mso-style-unhide:no;
mso-style-locked:yes;
mso-style-link:"Texto independiente";
mso-ansi-font-size:12.0pt;
font-weight:bold;
mso-bidi-font-weight:normal;}
.MsoChpDefault
{mso-style-type:export-only;
mso-default-props:yes;
font-size:10.0pt;
mso-ansi-font-size:10.0pt;
mso-bidi-font-size:10.0pt;}
@page WordSection1
{size:612.0pt 792.0pt;
margin:70.85pt 3.0cm 70.85pt 3.0cm;
mso-header-margin:36.0pt;
mso-footer-margin:36.0pt;
mso-paper-source:0;}
div.WordSection1
{page:WordSection1;}
-->
Sustainability of agricultural systems has become an important issue all
over the world. Many of the issues of sustainability are related to the quality
of soil and the changes through time. Intensive cultivation leads to a rapid
decline in organic matter and in nutrient levels besides affecting physical
and biologycal properties of soil. Phosphorus
(P) is an essential plant nutrient that must be added to most soils to maintain
plant growth and sustain crop yields. Organic phosphorus compounds in soil can
constitute 30 50 % of total phosphorus. The assimilation of this phosphorus
by plants and microorganisms is preceded by soil enzymes. Phosphatases enzymes
play a major role in the processes of mineralization (dephosphorylation) of
organic P substrates. Enzyme activities are indicators of soil quality because:
i) they are strongly connected with important soil properties such as organic
matter, physical properties and microbial activity or biomass; ii) they respond
earlier than other soil properties; and iii) they involve relatively simple
methods compared to other soil quality bioindicators. In the present study we
propose a precise and accurate method to determine the alkaline and acid
phosphatase activity in soil using adenosine monophosphate, wich is a natural
compound, as a substrate. The adenosine released by the enzymatic reaction was
cuantified by MEKC method. The background electrolyte consisted in 20 mM phosphate buffer (pH 8)
10 mM
sodium dodecyl sulphate and 10% acetonitrile. The LOD and LOQ were 2.27 10-4
and 6.4 10-4 mg mL-1, respectively. The values for
the activities of alkaline and acid phosphatase were 44.5±3.5 and 21.7±2.3 µmol
of free adenosine g-1 h-1 respectively. These are the first studies on the
determination of the activity of alkaline and acid phosphatase using MEKC. The
CE method has demonstrated to be reliable to evaluate enzymatic activity,
representing a suitable and convenient alternative to the spectrophotometric
method. The most important advantage of MEKC is that it allows the use of
natural substrate in the enzymatic activity. Moreover, compared to LC methods,
capillary electrophoresis methods have some advantages. One of them is using a
smaller volume of samples, and also producing less amount of waste, which is a
very important point in this time of the Green Analytical Chemistry (GAC).