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KMID : 0545119960060020086
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Journal of Microbiology and Biotechnology
1996 Volume.6 No. 2 p.86 ~ p.91
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Purification and Characterization of Thermostable β-Mannanase from a Bacillus sp. YA-14
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Min, Do Sik
Chung, Yong Joon/Hahm, Byoung Kwon/Yu, Ju Hyun
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Abstract
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Thermostable β-mannanase from Bacillus sp. YA-14 was purified by acetone precipitation, CM-cellulose, Sephadex G-100 and hydroxyapatite column chromatography from culture supernatant. The final enzyme preparation appeared to be homogeneous on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). β-Mannanase appeared to be a monomeric protein with a molecular weight of 67,000 daltons. The optimal pH and temperature of the enzyme reaction were pH 6.0 and 75℃, respectively. The enzyme was stable at a pH range of 6.0 to 9.0 and at temperatures between 45 and 85℃. The kinetic constants of β-mannanase as determined with a galactomannan (locust bean) as substrate were a Vmax of 25 unit/㎖ and a Km of 1.1 ㎎/㎖. The enzyme had only limited activity on galactomannan substrate. It was suggested that β-mannanase activity is limited by the number of branched α-galactose residues.
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