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KMID : 0545120090190101184
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Journal of Microbiology and Biotechnology
2009 Volume.19 No. 10 p.1184 ~ p.1190
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Purification and Characterization of Endo-β-1,4 Mannanase from Aspergillus niger gr for Application in Food Processing Industry
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Naganagouda K.
Salimath P. V.
Mulimani Veerappa H.
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Abstract
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A thermostable extracellular β-mannanase from the culture supernatant of a fungus Aspergillus niger gr was purified to homogeneity. SDS-PAGE of the purified enzyme showed a single protein band of molecular mass 66 kDa. The β- mannanase exhibited optimum catalytic activity at pH 5.5 and 55oC. It was thermostable at 55oC, and retained 50% activity after 6 h at 55oC. The enzyme was stable at a pH range of 3.0 to 7.0. The metal ions Hg2+, Cu2+, and Ag2+ inhibited complete enzyme activity. The inhibitors tested, EDTA, PMSF, and 1,10-phenanthroline, did not inhibit the enzyme activity. N-Bromosuccinimide completely inhibited enzyme activity. The relative substrate specificity of enzyme towards the various mannans is in the order of locust bean gum>guar gum>copra mannan, with Km of 0.11, 0.28, and 0.33 mg/ml, respectively. Since the enzyme is active over a wide range of pH and temperature, it could find potential use in the food-processing industry.
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KEYWORD
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Aspergillus niger gr, food processing, β-mannanase, purification
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