Volume 8, Issue 3 (2019)                   JCP 2019, 8(3): 323-337 | Back to browse issues page

XML Print

Download citation:
BibTeX | RIS | EndNote | Medlars | ProCite | Reference Manager | RefWorks
Send citation to:

Shahbazi S, Mojerlou S. The synergistic interactions of cellulase enzyme activities of Trichoderma species in colloidal cellulose bioconversion. JCP. 2019; 8 (3) :323-337
URL: http://jcp.modares.ac.ir/article-3-32712-en.html
1- Nuclear Agriculture Research School, Nuclear Science and Technology Research Institute (NSTRI), Atomic Energy Organization of Iran (AEOI), Alborz, Iran.
2- Department of Horticulture and Plant Protection, Faculty of Agriculture, Shahrood University of Technology, Shahrood, Iran. , shideh.mojerlou@shahroodut.ac.ir
Abstract:   (2942 Views)
In this study the cellulytic activity of different species of Iranian Trichoderma isolates including Trichoderma harzianum (NAS-H101), T. aureoviride (NAS-AV106), T. pleuroticola (NAS-P109), T. longibrachiatum (NAS-L110), T. ghanens (NAS-K108), T. virens (NAS- Vi114), T. atroviride (NAS-A113) and T. atroviride (NAS-A112) was studied. The extracellular protein concentration of these isolates was determined by the dye binding method of Bradford. The molecular weight of cellulase enzymes was studied using SDS-PAGE. The lowest extracellular protein production was observed in NAS-K108. The highest Endo and Exo-glucanase activity were observed in NAS-L110 and NAS-A113, respectively. The SDS-PAGE profiles had several enzyme bands such as cellobiohydrolases, endoglucanases and β-glucosidases. The NAS-K108and NAS-P109 had both enzyme bands of CBH I and CBH II, but other isolates had only a sharp enzyme band correlated to CBH I or CBH II. The highest synergy was observed in FPase of NAS-A112, that contained a large amount of Cel 6A (CBH II) and a minor amount of Cel 7B (EG I). The results indicated that NAS-A113 overproduces cellulases, ß-glycosidase, and the extracellular enzymes, which suggest that this species might be utilized as a biological agent and or a source of enzymes for cellulose degradation in colloidal cellulose.
Full-Text [PDF 630 kb]   (546 Downloads)    
Article Type: Original Research | Subject: Biocontrol of Plant Diseases
Received: 2019/05/6 | Accepted: 2019/07/7 | Published: 2019/07/23

Add your comments about this article : Your username or Email:

Send email to the article author