Using cotton cultivar that undergoes premature senescence in the late stage of growth, we studied the effects of removing two basal fruiting branches of two cotton varieties, namely, Quanyin-2 and Jiza-999, on the leaf area index, the SPAD value of leaf subtending cotton boll, and the development of cotton fiber in the late stage of cotton growth. We focused on the differences in cotton CELLULOSE accumulation and fiber-related enzyme activities after removal of the basal fruiting branches and the development of cotton fiber during premature senescence. The results showed that removing the basal fruiting branches can maintain the green leaf area of the cotton canopy and the SPAD value of the subtending leaf during the late stage of reproductive growth. The period of rapid accumulation of fiber CELLULOSE lasted longer in plants from which the basal fruiting branches had been removed, and the beginning and end of the rapid accumulation period was later than in the control group with premature senescence. The activities of CELLULOSE synthesis-related ENZYMES (sucrose phosphate synthase, sucrose synthase, b-1, 3-glucanase, and invertase) were higher in plants in which the basal fruiting branches had been removed than in the control group after 10 days post-an thesis. Removing the basal fruiting branches can optimize the accumulation of CELLULOSE in cotton boll during the late growth stage and mitigate the effects of premature senescence on CELLULOSE synthesis. We found that the peak values for cotton fiber development-related enzyme activities in the control group occurred earlier, which tended to bring cotton fiber development forward and negatively impacted fiber yield.

Trichoderma reesei is one of the most important fungi producing CELLULOSE degrading ENZYMES in nature. In this study, 21 mutated isolate via gamma irradiation of T. reesei were screened for cellulase enzyme production on a colloidal CELLULOSE medium. The concentration of extracellular proteins of wild and mutant isolates were measured using Bradford's method. Avicel, carboxymethyl CELLULOSE and filter paper were used to measure cellulase activity. The purity and composition of enzyme-rich proteins were also evaluated using polyacrylamide gel electrophoresis (SDS-PAGE) test. The highest amount of extracellular protein production was observed in T. r M7 and T. r M17 isolates. Activity of endoglucanase, exoglucanase and total cellulase ENZYMES in mutated isolate T. r M8 showed the highest levels of enzymatic activity among mutant and wild isolates. The difference in the molecular weight of the enzyme bands showed that the EG 4, Cel 1A, Cel 12A, Cel 45A, Cel 3A, Cel 7A, Cel 6A, Cel 5A and Cel 61A ENZYMES hydrolyzed the colloidal CELLULOSE, synergictly. These results indicate that, mutation induced by gamma radiation is possible to obtain high producing Trichoderma mutants of cellulase ENZYMES.

b-glucosidase, is one of the cellulase ENZYMES system, hydrolyses cellobiose or cellooligoschrides to glucose.In this research for production of b-glucosidase enzyme, b-glucosidase activity was measured in the optimum conditions in 30 isolates of Trichoderma sp. In order to obtain the optimum conditions: an isolate of Trichoderma (T.reesei PTCC 5142) was grown in Mandels media containing CMC, Avicel and filter paper as carbon source at pH 4,5, 6 and 7. Lactose and cellubiose were added to media as inducer agents. Media were incubated at 25, 29 and 32 oC for 14 days. Samples were collected in 24h intervals, and enzyme activity was measured. Results showed that the optimum conditions for hyperproduction of b-glucosidase were pH=5, CMC as carbon source, lactose as inducer on seventh day at 29 oC. After screening the -glucosidase activity of all 30 isolates in the optimized conditions, it was shown that T.reesei PTCC 5142 had the highest level of -glucosidase specific activity (0.45 U/mg). For characterization and study of b-Glucosidase gene, CTAB method used for genomic DNA extraction.The expected PCR product with 566 bp was amplified with two specific primers (CP11 & CP12). The amplified fragment was confirmed by restriction pattern.

The stability of ENZYMES to heat and pH is one of the most important determining factors in their application. In this research, achieving thermostable and pH-stable cellulase was aimed by screening in one of the Hot springs of Garab in northeast Iran. The samples collected from one of the Hot springs of Garab, in Razavi Khorasan province in Iran, were used to isolate, screen, and identify bacteria capable of producing thermostable cellulase. The cultures were cultured at 45°C and under aerobic conditions. The bacteria were isolated on a CMC agar medium. Initial screening of the isolates was done based on specific culture medium, salt tolerance, and temperature changes. Then, their additional screening was done by evaluating endoglucanase activity at different temperatures and pH using qualitative and quantitative methods. Finally, the molecular identification of the selected isolate was done by 16S rRNA gene sequencing. The results of this study, led to the introduction of a selected strain identified primarily as Bacillus sp. G362, a moderate halophile growing in 6%(w/v) salt concentration.  It showed high endoglucanase stability at 55°C and high stability in a wide range of acidic and alkaline pH. The studied Hot spring, like some other Iranian Hot springs, has cellulase-producing bacteria, which Bacillus sp. G362 is capable of producing endoglucanase showing the thermostablity and pH stability at a wide range of alkaline and Acidic pH. In addition, the specific endoglucanase gene of G362 Bacillus sp. can be identified through molecular methods and used for further research including structural studies. It may even be used as a protein template in protein engineering.

Background and purpose: Nitrate is used as a chemical water quality indicator. The aim of this work was investigation of nitrate adsorption from aqueous solution by Nanocomposite celloluse/Fe O /ZnO as a efficient adsorption. 3 4 Materials and methods: This study was conducted in a laboratory batch reactor. The most important variables affecting adsorption process were pH (2, 4, 6, 8, 10), time (25, 50, 75, 100, 125, 150, 175, 200, 250, 300 min), nitrate concentration (0, 50, 100, 150, 200, 250 mg/L), adsorption dose (0, 2, 4, 6, 8, 10 g/ L), Mixing speed (0, 50, 100, 150, 200 r/ min) investigated and adsorption kinetic and isotherms were determinated. Spectrophotometer was used for nitrate measurement and adsorbent characteristics were determined by SEM and FTIR examinations Results: The results showed the optimum pH=6 and nitrate adsorption increased by increasing contact time and adsorbent dosage. The adsorbent specific surfact area of 10 m 2 /g was obtained and FTIR test revealed the finctional groups existing on adsorbent surface to have important role in nitrate adsorption. Experimental data was well fitted by pseudo second-order kinetic model. Langmuir isotherm model best represented the experimental data to describe adsorption. Conclusion: Results showed that the nanocomposite CELLULOSE/Fe O /ZnO can 3 4 efficiently remove nitrate from aqueous solution.

Cellobiohydrolase is one of the cellulase ENZYMES which is involved in degradation of CELLULOSE, the most abundant biopolymer in nature. Trichoderma species are known as a useful source of cellulytic ENZYMES. In this research cellulase ENZYMES activity in 30 isolates of Trichoderma sp. were studied by rapid screening on medium containing swollen CELLULOSE and isolate Trichoderma reesei (PTCC5142) was selected on the basis of clearing zone diameter (16 mm). The enzyme activity was measured in the optimum conditions for production of cellobiohydrolase enzyme in Trichoderma. In order to obtain the optimum conditions: the selected isolate was grown in Mandels media with CMC, Avicel and Filter paper as carbon source at pH 4, 5,6, and7. Lactose and cellubiose were added to media as inducer agents. Media were incubated at different temperatures (25, 28 and 320C) for 14 days. Samples were collected in 24h intervals, and enzyme activity was measured. Results showed that the optimum conditions for hyperproduction of cellobiohydrolase were pH=5, CMC as carbon source, temperature 28 0C, lactose as inducer on 7th day. After screening the cellobiohydrolase activity of all 30 isolates in the optimized conditions, results showed that isolate Trichoderma reesei (PTCC5142) with the highest enzyme activity (4.45U/ml) was the best producer of cellobiohydrolase enzyme.

Removal of antibiotics from water resources is essential for their harmful effects on living organisms. In this work, a polymeric membrane based on polyvinylidene fluoride deposited by CELLULOSE loaded with Magnesium oxide nanoparticles (PVDF /CELLULOSE/MgO) has been prepared. The prepared membrane was characterized using FESEM, XRD, AFM, and contact angle measurement. The efficiency of the prepared membranes as an adsorbent for removing amoxicillin as a model pollutant was investigated. The effect of pH, amoxicillin concentration, and the time on the removal of amoxicillin was studied. The results showed that with a decrease in pH, a reduction in the initial concentration of amoxicillin, and an increase in time, the percentage of amoxicillin removal increases, and the maximum percentage of amoxicillin removal was obtained at about 85% at 200 mg/liter of amoxicillin, pH = 3, and 100 min. The kinetic of amoxicillin removal using PVDF/CELLULOSE/MgO membrane was also investigated. These results confirmed that PVDF/CELLULOSE/MgO membrane would be a potential adsorbent for removing amoxicillin from contaminated water.

Aspergillus species are known as a usefull source of b-Glucosidases and A. niger is by far the most efficient producer of ß -Glucosidases among the microorganisms investigated.In this research ß-Glucosidases activity in 13 isolates of Aspergillus were studied by Rapid screening. Different diameter of the clearing zone surronding the clonies on the plate cellulolytic activity in these isolates. Isolate R4 and isolates 5010 and M2 showed the largest (41 mm) and lowest (15mm) cellulolytic activity, respectively.The ß -Glucosidase activity was measured in the optimum conditions for production of ß - Glucosidase ENZYMES in Aspergillus. In order to obtain the optimum condition: an isolate of Aspergillus was grown in Mandels media with CMC, Avicel and filter paper as carbon source at pH 5,6,7,8 and 9. Lactose and cellubiose were added to media as inducer agents. Media were incubated at 3˚DC with shaking for 10 days. samples were collected in 48h intervals, and enzyme activity was measured. Results showed that the optimum conditions for hyperproduction of ß -Glucosidase were pH=8, CMC as carbon source, lactose as inducer on second day. After screening the ß -Glucosidase activity of all 13 isolates in the optimized conditions, it was shown that R2, R3, R4, M3b, M2 and 5010 had the high level of enzyme activity and 5011, M3a and 5154 isolates had low level of ß -Glucosidase. For characterization and study of ß -Glucosidase gene, CT AB method used for genomic DNA extraction. The expected PCR product with 2806bp was amplified with two specific primers. The amplified fragment was confirmed by restriction pattern.

Background and Objectives: CELLULOSE is a major component of plant biomass, which can be converted into biofuels and valuable chemicals. The key step in utilization of this organic material is its hydrolysis into soluble sugars. This study evaluated cellulase production by Trichoderma harzianum under different pH values, temperatures and incubation periods with the aim to increase enzyme production and decrease its costs.Methods: The amount of protein production and the hydrolytic activity of cellulase ENZYMES including exoglucanase, endoglucanase and b-glucosidase produced by T.harzianum were evaluated using various substrates such as avicel, carboxymethyl CELLULOSE, cellobiose, Whatman grade 1 filter paper under different pH values (4, 4.8, 5.5 and 6.5), temperatures (25, 28 and 34 °C) and incubation times (48, 72, 96 and 120 h).Results: The optimum condition for cellulase production by T. harzianum is 120 hours of incubation at 25 °C and pH of 6.5.Conclusion: T. harzianum can be used for the production of all three classes of cellulase. This fungus is suitable for the efficient production of cellulolytic ENZYMES and reducing the cost of consumables.