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Novel xylanases from Simplicillium obclavatum MTCC 9604: comparative analysis of production, purification and characterization of enzyme from submerged and solid state fermentation.

Roy S, Dutta T, Sarkar TS, Ghosh S - Springerplus (2013)

Bottom Line: The production of extracellular xylanase by a newly isolated fungus Simplicillium obclavatum MTCC 9604 was studied in solid-state and submerged fermentation.Multiple xylanases and endoglucanases were produced by the strain during growth on wheat bran in solid state fermentation (SSF).A single xylanase isoform was found to be produced by the same fungus under submerged fermentation (SF) using wheat bran as sole carbon source.

View Article: PubMed Central - PubMed

Affiliation: Department of Biochemistry, University of Calcutta, 35, Ballygunge Circular Road, Kolkata, 700 019 West Bengal India.

ABSTRACT
The production of extracellular xylanase by a newly isolated fungus Simplicillium obclavatum MTCC 9604 was studied in solid-state and submerged fermentation. Multiple xylanases and endoglucanases were produced by the strain during growth on wheat bran in solid state fermentation (SSF). A single xylanase isoform was found to be produced by the same fungus under submerged fermentation (SF) using wheat bran as sole carbon source. Enzyme activity, stability and the protein yield were much higher in SSF than SF. The two dimensional zymogram of the crude enzyme indicated the presence of six isoforms with different pI values starting from pH 3-10. The optimum temperature and pH for the partially purified xylanase activity were 50°C and pH 5.0 respectively; xylanase enzymes exhibited remarkable stability over a broad pH range and the temperature range of 30-60°C which has great potential to be used in biofuels, animal feed and food industry applications.

No MeSH data available.


Related in: MedlinePlus

Temperature optima and thermal stability curve of xylanase ofS. obclavatumfrom SSF and SF. Panel (A) Temperature optima of xylanase from SSF. Panel (B) Temperature optima of xylanase from SF. Panel (C) Thermal stability of the xylanase from SSF. Panel (D) Thermal stability of the xylanase from SF. Relative enzyme activities (% of maximum) were plotted against temperature. All the results were expressed in mean ± SD from n = 3.
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Fig5: Temperature optima and thermal stability curve of xylanase ofS. obclavatumfrom SSF and SF. Panel (A) Temperature optima of xylanase from SSF. Panel (B) Temperature optima of xylanase from SF. Panel (C) Thermal stability of the xylanase from SSF. Panel (D) Thermal stability of the xylanase from SF. Relative enzyme activities (% of maximum) were plotted against temperature. All the results were expressed in mean ± SD from n = 3.

Mentions: The optimum temperature of the purified xylanase from both SSF and SF was found to be 50°C at pH 7.0 (Figure 5A). Partially purified xylanases produced from SSF were more thermo stable with compare to the xylanases produced from SF condition. The partially purified xylanases from SSF exhibited stability over the temperature range of 30-60°C and retained about 80% residual activity on that range (Figure 5B). Whereas the xylanase produced in SF gradually lost its activity and retained only 50% residual activity after 1 h incubation at 60°C (Figure 5B).Figure 5


Novel xylanases from Simplicillium obclavatum MTCC 9604: comparative analysis of production, purification and characterization of enzyme from submerged and solid state fermentation.

Roy S, Dutta T, Sarkar TS, Ghosh S - Springerplus (2013)

Temperature optima and thermal stability curve of xylanase ofS. obclavatumfrom SSF and SF. Panel (A) Temperature optima of xylanase from SSF. Panel (B) Temperature optima of xylanase from SF. Panel (C) Thermal stability of the xylanase from SSF. Panel (D) Thermal stability of the xylanase from SF. Relative enzyme activities (% of maximum) were plotted against temperature. All the results were expressed in mean ± SD from n = 3.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3755804&req=5

Fig5: Temperature optima and thermal stability curve of xylanase ofS. obclavatumfrom SSF and SF. Panel (A) Temperature optima of xylanase from SSF. Panel (B) Temperature optima of xylanase from SF. Panel (C) Thermal stability of the xylanase from SSF. Panel (D) Thermal stability of the xylanase from SF. Relative enzyme activities (% of maximum) were plotted against temperature. All the results were expressed in mean ± SD from n = 3.
Mentions: The optimum temperature of the purified xylanase from both SSF and SF was found to be 50°C at pH 7.0 (Figure 5A). Partially purified xylanases produced from SSF were more thermo stable with compare to the xylanases produced from SF condition. The partially purified xylanases from SSF exhibited stability over the temperature range of 30-60°C and retained about 80% residual activity on that range (Figure 5B). Whereas the xylanase produced in SF gradually lost its activity and retained only 50% residual activity after 1 h incubation at 60°C (Figure 5B).Figure 5

Bottom Line: The production of extracellular xylanase by a newly isolated fungus Simplicillium obclavatum MTCC 9604 was studied in solid-state and submerged fermentation.Multiple xylanases and endoglucanases were produced by the strain during growth on wheat bran in solid state fermentation (SSF).A single xylanase isoform was found to be produced by the same fungus under submerged fermentation (SF) using wheat bran as sole carbon source.

View Article: PubMed Central - PubMed

Affiliation: Department of Biochemistry, University of Calcutta, 35, Ballygunge Circular Road, Kolkata, 700 019 West Bengal India.

ABSTRACT
The production of extracellular xylanase by a newly isolated fungus Simplicillium obclavatum MTCC 9604 was studied in solid-state and submerged fermentation. Multiple xylanases and endoglucanases were produced by the strain during growth on wheat bran in solid state fermentation (SSF). A single xylanase isoform was found to be produced by the same fungus under submerged fermentation (SF) using wheat bran as sole carbon source. Enzyme activity, stability and the protein yield were much higher in SSF than SF. The two dimensional zymogram of the crude enzyme indicated the presence of six isoforms with different pI values starting from pH 3-10. The optimum temperature and pH for the partially purified xylanase activity were 50°C and pH 5.0 respectively; xylanase enzymes exhibited remarkable stability over a broad pH range and the temperature range of 30-60°C which has great potential to be used in biofuels, animal feed and food industry applications.

No MeSH data available.


Related in: MedlinePlus