Physicochemical characterisation and substrate specificity of purified ß-1,6-glucanase from Trichoderma longibrachiatum
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...
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| Format: | Article |
| Language: | English |
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Universiti Putra Malaysia Press
2009
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| Online Access: | http://psasir.upm.edu.my/id/eprint/40549/ http://psasir.upm.edu.my/id/eprint/40549/1/Physicochemical%20Characterisation%20and%20Substrate%20Specificity%20of%20Purified%20%C3%9F-1%2C6-glucanase%20from%20Trichoderma%20longibrachiatum.pdf |
| _version_ | 1848849459135381504 |
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| author | Mustafa, Muskhazli Abd. Aziz, Nor Azwady Kaimi, Anida Noor, Nurul Shafiza Ahmad Bedawi, Salifah Hasanah Ithnin, Nalisha |
| author_facet | Mustafa, Muskhazli Abd. Aziz, Nor Azwady Kaimi, Anida Noor, Nurul Shafiza Ahmad Bedawi, Salifah Hasanah Ithnin, Nalisha |
| author_sort | Mustafa, Muskhazli |
| building | UPM Institutional Repository |
| collection | Online Access |
| description | 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. |
| first_indexed | 2025-11-15T09:50:44Z |
| format | Article |
| id | upm-40549 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T09:50:44Z |
| publishDate | 2009 |
| publisher | Universiti Putra Malaysia Press |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-405492015-11-20T03:42:00Z http://psasir.upm.edu.my/id/eprint/40549/ Physicochemical characterisation and substrate specificity of purified ß-1,6-glucanase from Trichoderma longibrachiatum Mustafa, Muskhazli Abd. Aziz, Nor Azwady Kaimi, Anida Noor, Nurul Shafiza Ahmad Bedawi, Salifah Hasanah Ithnin, Nalisha 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. Universiti Putra Malaysia Press 2009-01 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/40549/1/Physicochemical%20Characterisation%20and%20Substrate%20Specificity%20of%20Purified%20%C3%9F-1%2C6-glucanase%20from%20Trichoderma%20longibrachiatum.pdf 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 http://www.pertanika.upm.edu.my/Pertanika%20PAPERS/JST%20Vol.%2017%20%281%29%20Jan.%202009/17%2077-2008-Muskhazli.pdf |
| spellingShingle | Mustafa, Muskhazli Abd. Aziz, Nor Azwady Kaimi, Anida Noor, Nurul Shafiza Ahmad Bedawi, Salifah Hasanah Ithnin, Nalisha Physicochemical characterisation and substrate specificity of purified ß-1,6-glucanase from Trichoderma longibrachiatum |
| title | Physicochemical characterisation and substrate specificity of purified ß-1,6-glucanase from Trichoderma longibrachiatum |
| title_full | Physicochemical characterisation and substrate specificity of purified ß-1,6-glucanase from Trichoderma longibrachiatum |
| title_fullStr | Physicochemical characterisation and substrate specificity of purified ß-1,6-glucanase from Trichoderma longibrachiatum |
| title_full_unstemmed | Physicochemical characterisation and substrate specificity of purified ß-1,6-glucanase from Trichoderma longibrachiatum |
| title_short | Physicochemical characterisation and substrate specificity of purified ß-1,6-glucanase from Trichoderma longibrachiatum |
| title_sort | physicochemical characterisation and substrate specificity of purified ß-1,6-glucanase from trichoderma longibrachiatum |
| url | http://psasir.upm.edu.my/id/eprint/40549/ http://psasir.upm.edu.my/id/eprint/40549/ http://psasir.upm.edu.my/id/eprint/40549/1/Physicochemical%20Characterisation%20and%20Substrate%20Specificity%20of%20Purified%20%C3%9F-1%2C6-glucanase%20from%20Trichoderma%20longibrachiatum.pdf |