%0 Journal Article
%T Characterization of an Exopolygalacturonase from <i>Leucoagaricus gongylophorus</i>, the Symbiotic Fungus of <i>Atta sexdens</i>
%A Paulo R. Adalberto
%A Camilla C. Golfeto
%A Ariele C. Moreira
%A Fernando G. Almeida
%A Douglas Ferreira
%A Quezia B. Cass
%A Dulce H. F. Souza
%J Advances in Enzyme Research
%P 7-19
%@ 2328-4854
%D 2016
%I Scientific Research Publishing
%R 10.4236/aer.2016.41002
%X The present study aimed to purify and characterize one polygalacturonase from <i>L. gongylophorus </i>(PGaseLg), the symbiotic fungus of <i>Atta sexdens</i>. The enzyme was isolated by salting out of crude extract followed by two chromatographic steps. PGaseLG was identified with MS analysis and molecular exclusion chromatography revealed the monomeric nature of a protein with an estimated molecular weight of about 39 kDa. PGaseLg has an optimum temperature of 60<span style=\"font-family:Verdana, Helvetica, Arial;white-space:normal;background-color:#FFFFFF;\">¡ã</span>C and optimum pH activity at 5.0. Using polygalacturonate as a substrate, the calculations of K<sub>M</sub>, V<sub>max</sub> and k<sub>cat</sub> were 0.65 mg¡¤mL<sup>-1</sup>, 1800 ¦Ìmol¡¤min<sup>-1</sup>¡¤mg<sup>-1</sup> and 35.97 s<sup>-1</sup>, respectively. The enzyme was stable for more than 3 h at 50¡ãC at pH 5.0; otherwise, at lower or higher pH values, the PGaseLg was less stable. The influence of several metals, EDTA and <i>¦Â</i>-mercaptoethanol on enzyme activity was also determined. Thin layer chromatography (TLC) analyses indicated that PGaseLg is an exopolygalacturonase.
%K Polygalacturonase
%K &lt
%K i&gt
%K L. gongylophorus
%K A. sexdens&lt
%K /i&gt
%K Plague Control
%U http://www.scirp.org/journal/PaperInformation.aspx?PaperID=64432