The synergistic interactions of Trichoderma spp. cellulase enzyme activities in biomass conversion; Part1: comparison of cellulose Iα, Iβ and III

سال انتشار: 1392
نوع سند: مقاله کنفرانسی
زبان: انگلیسی
مشاهده: 1,019

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شناسه ملی سند علمی:

FNCAES01_397

تاریخ نمایه سازی: 25 اردیبهشت 1393

چکیده مقاله:

Three strain of Trichoderma (T. reesei, T. viride and T. harzianum) were used for cellulase enzyme production. The Avicel, CMC, BC and Whatman NO.1 filter paper, were used to cellulase activity assay. The carboxy methyl cellulose (cellulose III, CMC) and bacterial cellulose (cellulose Iα, BC) were produced by chemical modification of Avicel (cellulose Iβ) and fermentation of sucrose by G. xylinus, respectively. Their chemical structural properties were investigated by FT-IR, XRD and SEM in compare with Avicel. The molecular weight of cellulase enzymes were studied using SDS-PAGE. The lowest extracellular protein production was observed in T. reesei, T. harzianum and T. viride, respectively. The SEM image of substrates, showed more delicacy of BC fibers relative to Avicel and CMC. The diameter ratio of BC to Avicel is approximately 1/30 or less. The FTIR spectroscopy and XRD assessments designated that the produced CMC is carrying a carboxylic group and its crystallinity is 81.84. The crystallinity of the Avicel and BC were demonstrated that the crystallinity index of Avicel (89.15%) was more than that of bacterial cellulose (66.44%). The highest Endo-glucanase (CMCase), Exo-glucanase (Avicelase) and total cellulase (BCase and FPase) activity were observed in T. reesei, T.viride and T.harzianum, respectively. The high Avicelase activity in T. viride due to high produced extracellular protein concentration. The SDS-PAGE profiles have several enzyme bonds such as CBHs, EGs and BGLs. The T. harzianum and T. reesei have both enzyme bonds of Cel6A (CBHII) and Cel7A (CBHI), but T. viride has only a sharp enzyme bonds correlate to Cel7A. Cel12A (EGIII) only was observed in T. reesei. The highest synergy was observed in FPase and BCase of T. harzianum, that containing of large amount of CBH I and CBH II and minor amount of EG. Also, the Cel 3A (BGL I) and CEL 1A (BGL II) were observed for T. reesei and T. harzianum SDS-PAGE profiles, respectively. Finally, the results showed that bacterial cellulose is a good substrate for total cellulase activity assay, because it has the highest enzyme activity in compare of filter paper and avicel. The high values BCase and FPase activites in T. harzianum and T. reesei due to present of CBH and EG enzymes and synergism that occurs between the CBH and EG.

نویسندگان

s shahbazi

Radiation Application Research School, Nuclear Science and Technology Research Institute(NSTRI) Atomic Energy organization of IRAN (AEOI) Alborz, Iran

h askari

Radiation Application Research School, Nuclear Science and Technology Research Institute(NSTRI) Atomic Energy organization of IRAN (AEOI) Alborz, Iran Department of Food Science and Technology,School of Agriculture, Shiraz University, Fars, Iran

t naseripour

Plant protection Department,Gorgan University of Agricultural Sciences and Natural Resources, Golestan, Iran

m bakhtiyari

Department of Food Science and Technology,School of Agriculture, Shiraz University, Fars, Iran.