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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

pH optima and pH stability curve of xylanase ofS. obclavatumfrom SSF and SF. Panel (A) pH optima curve of xylanase from SSF. Panel (B) pH optima curve of xylanase from SF. Panel (C) pH stability curve of xylanase from SSF. Panel (D) pH stability curve of xylanase from SF. Relative enzyme activities (% of maximum) were plotted against pH. All the results were expressed in mean ± SD from n = 3.
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Fig4: pH optima and pH stability curve of xylanase ofS. obclavatumfrom SSF and SF. Panel (A) pH optima curve of xylanase from SSF. Panel (B) pH optima curve of xylanase from SF. Panel (C) pH stability curve of xylanase from SSF. Panel (D) pH stability curve of xylanase from SF. Relative enzyme activities (% of maximum) were plotted against pH. All the results were expressed in mean ± SD from n = 3.

Mentions: Partially purified xylanase exhibited the highest xylanase activity at pH 5 and retained 80% activity at the pH 9 (Figure 4A). This data corroborated well with 2D zymogram where a distinct isoform was present at around pH 9. Four isoforms were found to be present at pH 5. One isoform was present at around ~ pH 4 in 2D zymogram. On the other hand the Xylanase produced from SF condition showed the optimum activity (1.55 IU/min) at pH 5 and then the activity gradually decreased down at alkaline condition (Figure 4B). The partially purified xylanases from S. obclavatum MTCC 9604 grown in SSF were highly stable within a broad pH range, ranging from pH 4.0 to 9.0 (Figure 4C). Thus, the pH stability of xylanase obtained from S. obclavatum MTCC 9604 showed to be a promising fungus for potential biotechnological applications. The xylanase produced in SF also showed a wide range of pH stability starting from pH 5.0 to 9.0 (Figure 4D).Figure 4


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)

pH optima and pH stability curve of xylanase ofS. obclavatumfrom SSF and SF. Panel (A) pH optima curve of xylanase from SSF. Panel (B) pH optima curve of xylanase from SF. Panel (C) pH stability curve of xylanase from SSF. Panel (D) pH stability curve of xylanase from SF. Relative enzyme activities (% of maximum) were plotted against pH. 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

Fig4: pH optima and pH stability curve of xylanase ofS. obclavatumfrom SSF and SF. Panel (A) pH optima curve of xylanase from SSF. Panel (B) pH optima curve of xylanase from SF. Panel (C) pH stability curve of xylanase from SSF. Panel (D) pH stability curve of xylanase from SF. Relative enzyme activities (% of maximum) were plotted against pH. All the results were expressed in mean ± SD from n = 3.
Mentions: Partially purified xylanase exhibited the highest xylanase activity at pH 5 and retained 80% activity at the pH 9 (Figure 4A). This data corroborated well with 2D zymogram where a distinct isoform was present at around pH 9. Four isoforms were found to be present at pH 5. One isoform was present at around ~ pH 4 in 2D zymogram. On the other hand the Xylanase produced from SF condition showed the optimum activity (1.55 IU/min) at pH 5 and then the activity gradually decreased down at alkaline condition (Figure 4B). The partially purified xylanases from S. obclavatum MTCC 9604 grown in SSF were highly stable within a broad pH range, ranging from pH 4.0 to 9.0 (Figure 4C). Thus, the pH stability of xylanase obtained from S. obclavatum MTCC 9604 showed to be a promising fungus for potential biotechnological applications. The xylanase produced in SF also showed a wide range of pH stability starting from pH 5.0 to 9.0 (Figure 4D).Figure 4

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