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Asian Journal of Biochemistry
  Year: 2015 | Volume: 10 | Issue: 5 | Page No.: 190-204
DOI: 10.3923/ajb.2015.190.204
Purification, Biochemical Characterization of a Macrotermes gilvus Cellulase and Zymogram Analysis
Chamaiporn Champasri, Thongchai Champasri and Khanutsanan Woranam

Abstract:
Cellulase plays an important role in cellulose degradation. The enzyme catalyzes the cleavage of b-1,4 glycosidic bond between glucose residues. The Macrotermes gilvus cellulase was purified by using ammonium sulfate precipitation and anion exchange column with 1.38% recovery and 22-fold purification. The SDS-PAGE coupled with zymogram analysis revealed the molecular weights approximately of 54 kDa. The biochemical properties of the enzyme exhibited the optimum temperature and optimum pH of 45°C and 5.2. Interestingly, the enzyme was active over a wide range of temperatures (7-70°C) and a broad range of pH values (4.5-8). At the indicated temperatures and pH values, the enzyme exhibited more than 84 and 50% of its activity. The thermal stability and pH stability of the enzyme were also investigated. The result showed that the enzyme retained nearly 40% of its original activity after incubation in mild acidic (pH 5.2), neutral (pH 7.0) and basic (pH 10.0) conditions for 5 h. The enzyme retained its activity more than 70% of initial activity at both 37 and 45°C after incubation for 3 h. Moreover, the activity of the enzyme was strongly inhibited by Cu2+ and slightly affected by Fe2+ and EDTA, whereas the presence of Ca2+ and Mg2+ slightly increased the enzyme activity. Due to the wide temperature and pH range of enzyme activity, the Macrotermes gilvus cellulase might be potential enzyme for industrial or agricultural application.
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How to cite this article:

Chamaiporn Champasri, Thongchai Champasri and Khanutsanan Woranam, 2015. Purification, Biochemical Characterization of a Macrotermes gilvus Cellulase and Zymogram Analysis. Asian Journal of Biochemistry, 10: 190-204.

DOI: 10.3923/ajb.2015.190.204

URL: https://scialert.net/abstract/?doi=ajb.2015.190.204

 
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