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Application of ZnO Nanoparticles for Improving the Thermal and pH Stability of Crude Cellulase Obtained from Aspergillus fumigatus AA001.

Srivastava N, Srivastava M, Mishra PK, Ramteke PW - Front Microbiol (2016)

Bottom Line: Cellulases are the enzymes which are responsible for the hydrolysis of cellulosic biomass.The crude thermostable cellulase has been obtained from the Aspergillus fumigatus AA001 and treated with ZnO nanoparticle which shows thermal stability at 65°C up to 10 h whereas it showed pH stability in the alkaline pH range and retained its 53% of relative activity at pH 10.5.These findings may be promising in the area of biofuels production.

View Article: PubMed Central - PubMed

Affiliation: Department of Molecular and Cellular Engineering, Sam Higginbottom Institute of Agriculture Technology & SciencesAllahabad, India; Department of Chemical Engineering and Technology, Indian Institute of Technology (Banaras Hindu University)Varanasi, India.

ABSTRACT
Cellulases are the enzymes which are responsible for the hydrolysis of cellulosic biomass. In this study thermal and pH stability of crude cellulase has been investigated in the presence of zinc oxide (ZnO) nanoparticles. We synthesized ZnO nanoparticle by sol-gel method and characterized through various techniques including, X-ray Diffraction, ultraviolet-visible spectroscope, field emission scanning electron microscope and high resolution scanning electron microscope. The crude thermostable cellulase has been obtained from the Aspergillus fumigatus AA001 and treated with ZnO nanoparticle which shows thermal stability at 65°C up to 10 h whereas it showed pH stability in the alkaline pH range and retained its 53% of relative activity at pH 10.5. These findings may be promising in the area of biofuels production.

No MeSH data available.


Thermal stability of crude cellulase in presence of different concentration of ZnO nanoparticles at 60°C.
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Figure 3: Thermal stability of crude cellulase in presence of different concentration of ZnO nanoparticles at 60°C.

Mentions: Thermal stability of crude cellulase was performed at different concentrations of ZnO nanoparticles for 4 h. It is clear from the (Figure 3), at 60°C, enzyme showed its 100% stability at three different concentrations. It was recorded that at the same temperature, the enzyme reflected its maximum stability at concentration 7.5 μg/mL for 4 h whereas it retains its 89 and 70% relative activity at the concentrations of 10 μg/mL and 12.5 μg/mL, respectively (with a significance level of 1.0%). However, the enzyme retained its 58% of relative activity for 4 h at the concentration of 15 μg/mL, which shows fall in the enzyme activity beyond the concentration of 7.5 μg/mL for the same period. It was striking to mention here that the untreated cellulase which was designated as the control retained its half-life for 4 h while ZnO nanoparticles treated cellulase retained its 100% stability for the same period between the concentration of 2.5 μg/mL to 7.5 μg/mL. Moreover, it is well documented that the immobilization property of nanoparticles improves the stability of enzyme, and the biocompatibility of ZnO nanoparticles might be a reason to retain the complete stability of ZnO nanoparticles treated cellulase as compared to the control at the same temperature and time. However, decreasing the stability of ZnO nanoparticles treated cellulase on increasing the concentration over 7.5 μg/mL might be due to the non-supportive interaction of nanoparticles with the enzyme at higher concentrations.


Application of ZnO Nanoparticles for Improving the Thermal and pH Stability of Crude Cellulase Obtained from Aspergillus fumigatus AA001.

Srivastava N, Srivastava M, Mishra PK, Ramteke PW - Front Microbiol (2016)

Thermal stability of crude cellulase in presence of different concentration of ZnO nanoparticles at 60°C.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4834293&req=5

Figure 3: Thermal stability of crude cellulase in presence of different concentration of ZnO nanoparticles at 60°C.
Mentions: Thermal stability of crude cellulase was performed at different concentrations of ZnO nanoparticles for 4 h. It is clear from the (Figure 3), at 60°C, enzyme showed its 100% stability at three different concentrations. It was recorded that at the same temperature, the enzyme reflected its maximum stability at concentration 7.5 μg/mL for 4 h whereas it retains its 89 and 70% relative activity at the concentrations of 10 μg/mL and 12.5 μg/mL, respectively (with a significance level of 1.0%). However, the enzyme retained its 58% of relative activity for 4 h at the concentration of 15 μg/mL, which shows fall in the enzyme activity beyond the concentration of 7.5 μg/mL for the same period. It was striking to mention here that the untreated cellulase which was designated as the control retained its half-life for 4 h while ZnO nanoparticles treated cellulase retained its 100% stability for the same period between the concentration of 2.5 μg/mL to 7.5 μg/mL. Moreover, it is well documented that the immobilization property of nanoparticles improves the stability of enzyme, and the biocompatibility of ZnO nanoparticles might be a reason to retain the complete stability of ZnO nanoparticles treated cellulase as compared to the control at the same temperature and time. However, decreasing the stability of ZnO nanoparticles treated cellulase on increasing the concentration over 7.5 μg/mL might be due to the non-supportive interaction of nanoparticles with the enzyme at higher concentrations.

Bottom Line: Cellulases are the enzymes which are responsible for the hydrolysis of cellulosic biomass.The crude thermostable cellulase has been obtained from the Aspergillus fumigatus AA001 and treated with ZnO nanoparticle which shows thermal stability at 65°C up to 10 h whereas it showed pH stability in the alkaline pH range and retained its 53% of relative activity at pH 10.5.These findings may be promising in the area of biofuels production.

View Article: PubMed Central - PubMed

Affiliation: Department of Molecular and Cellular Engineering, Sam Higginbottom Institute of Agriculture Technology & SciencesAllahabad, India; Department of Chemical Engineering and Technology, Indian Institute of Technology (Banaras Hindu University)Varanasi, India.

ABSTRACT
Cellulases are the enzymes which are responsible for the hydrolysis of cellulosic biomass. In this study thermal and pH stability of crude cellulase has been investigated in the presence of zinc oxide (ZnO) nanoparticles. We synthesized ZnO nanoparticle by sol-gel method and characterized through various techniques including, X-ray Diffraction, ultraviolet-visible spectroscope, field emission scanning electron microscope and high resolution scanning electron microscope. The crude thermostable cellulase has been obtained from the Aspergillus fumigatus AA001 and treated with ZnO nanoparticle which shows thermal stability at 65°C up to 10 h whereas it showed pH stability in the alkaline pH range and retained its 53% of relative activity at pH 10.5. These findings may be promising in the area of biofuels production.

No MeSH data available.