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Confirmation of non N-glycan Linked Mannose Glycosylation in Chitinase 42 kDa Secreted by Trichoderma harzianum BIO10671

Mustafa, Muskhazli, Qamaruz Zaman, Faridah, Ramli, Salfarina, Tohfah, Nor Farizan, Ithnin, Nalisha and Wallis, G. L. F. (2008) Confirmation of non N-glycan Linked Mannose Glycosylation in Chitinase 42 kDa Secreted by Trichoderma harzianum BIO10671. Asian Journal of Biochemistry, 3 (4). pp. 235-242. ISSN 1815-9923

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Official URL: http://dx.doi.org/10.3923/ajb.2008.235.242

Abstract

Citinase 42 kDa produced by Trichoderma harzianum has been proven as a prime compund to be excreted onto the hyphae of the pathogen causing localised cell wall lysis at the point of interaction. This finally initiate the process of the host cell becomes empty of cytoplasm, disintegrates and shows a rapid collapse. This study investigates the existence of N-glyan linked mannose in chitinase 42 kDa from T.harzianum BIO10671 was initially purified using anion exchange chromatography prior to a series of experiments such as immunoblotting against the chitinase 42 kDa antibody, lectin staining for detecting any terminal linked mannose and galactofuranose detection to determine the presence of galactofuranose components in glycoproteins. The enzyme purification varvested about 12-fold of chitinase 42 kDa after overnight incubation in chitinase 42 kDa antibody suggesting taht the gene for chitinase 42 kDa was greatly expressed in this strain.There are no intervation of galactofuranose on any of the terminal mannose in chitinase 42 kDa as shown by negative results on samples treated with or without endoglycosidase-H and lectin staining. Therefore, it can be concluded that glycosylation occured in the chitinase 42 kDa from T.harianum 42 kDa was not in the form of N-glycan linked mannose as aspected.

Item Type:Article
Keyword:Trichoderma harzianum, chitinase, glycosylation, N-glycan linked, mannose
Faculty or Institute:Faculty of Science
DOI Number:10.3923/ajb.2008.235.242
Altmetrics:http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.3923/ajb.2008.235.242
ID Code:4698
Deposited By: Najwani Amir Sariffudin
Deposited On:25 Mar 2010 11:19
Last Modified:27 May 2013 07:17

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