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KMID : 1007519950040040280
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Food Science and Biotechnology
1995 Volume.4 No. 4 p.280 ~ p.284
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Production and Characterization of β-1,3- Glucanase from Microorganism
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Kim, Gi Nahm
Kil, Ji Oeun/Park, Inshik
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Abstract
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β-1,3-Glucanase from Bacillus sp. isolated from the soil has been partially purified by ethanol precipitation, Sephacryl S-200 gel filtration and DEAF-Sephacel ion-exchange chromatography. The optimum pH and temperature for the enzyme reaction with laminarin as a substrate were found to be pH 4.5 and 55℃, respectively. The enzyme was most stable at pH range between 4.0 and 7.0. It was inactivated completely within 10 min at 55℃, but thermostability of the enzyme could be increased by the addition of CaCl₂. The Michaelis-Menten constant of the enzyme with laminarin was 4.76 mg/ml. The enzyme was inhibited by metal ions such as Hg^(2+), Fe^(3-) and Cu^(2-). N-Bromosuccinimide inhibited the enzyme activity completely at 10 mM, whereas sulfhydryl reagents increased the enzyme activity.
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