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 ¥â-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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¥â-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¡É, respectively. The enzyme was most stable at pH range between 4.0 and 7.0. It was inactivated completely within 10 min at 55¡É, but thermostability of the enzyme could be increased by the addition of CaCl©ü. 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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