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Physicochemical characterisation and substrate specificity of purified ß-1,6-glucanase from Trichoderma longibrachiatum


Citation

Mustafa, Muskhazli and Abd. Aziz, Nor Azwady and Kaimi, Anida and Noor, Nurul Shafiza and Ahmad Bedawi, Salifah Hasanah and Ithnin, Nalisha (2009) Physicochemical characterisation and substrate specificity of purified ß-1,6-glucanase from Trichoderma longibrachiatum. Pertanika Journal of Science & Technology, 17 (1). pp. 137-147. ISSN 0128-7680; ESSN: 2231-8526

Abstract / Synopsis

The ß-1,6-glucanases are ubiquitous enzymes which appear to be implicated in the morphogenesis and have the ability to become virulence factor in plant-fungal symbiotic interaction. To our knowledge, no report on ß-1,6-glucanases purification from Trichoderma longibrachiatum has been made, although it has been proven to have a significant effect as a biocontrol agent for several diseases. Therefore, the aim of this study was to purify ß-1,6- glucanase from T. longibrachiatum T28, with an assessment on the physicochemical properties and substrate specificity. ß-1,3-glucanase enzyme, from the culture filtrate of T. longibrachiatum T28, was successively purified through precipitation with 80% acetone, followed by anionexchange chromatography on Neobar AQ and chromatofocusing on a Mono P HR 5/20 column. (One ß-1,6-glucanase) band at 42kDa in size was purified, as shown by the SDS-PAGE. The physicochemical evaluation showed an optimum pH of 5 and optimum temperature of 50°C for enzyme activity with an ability to maintain 100% enzyme stability. Enzyme activity was slightly reduced by 10-20% in the presence of 20 mM of Zn2+, Ca2+, Co2+, Mg2+, Cu2+, Mn2+ and Fe2+. The highest ß-1,6-glucanase hydrolysis activity was obtained on pustulan due to the similarity of ß-glucosidic bonds followed by laminarin, glucan and cellulose. Therefore, it can be concluded that the characterization of ß-1,6- lucanase secreted by T. longibrachiatum in term of molecular weight, responsed to selected physicochemical factors and the substrate specificity are approximately identical to other Trichoderma sp.


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Additional Metadata

Item Type: Article
Divisions: Faculty of Science
Publisher: Universiti Putra Malaysia Press
Keywords: ß-1,6-glucanase; Characterisation; Metal ion; PH; Purification; Substrate specificity; Trichoderma longibrachiatum
Depositing User: Noor Syafini Zamani
Date Deposited: 20 Nov 2015 11:42
Last Modified: 20 Nov 2015 11:42
URI: http://psasir.upm.edu.my/id/eprint/40549
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