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KMID : 0364819880260030223
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Korean Journal of Microbiology
1988 Volume.26 No. 3 p.223 ~ p.29
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Purification of g-glucanase from Bacillus subtilis Using Chromogenic Substrate
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Abstract
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1
Bacillus subtilis K-43, which produces considerable amount of/3-gleeuase was selected among exit arfl-glucauase-producing bacteria isolated from soil. fl-glaaaase was purified by ammonium sulfate fractionation, Sephadex G-100 gel filtration and DEAE-sepbacel ion exchange cbromatography. The purified enzyme revealed a single band by polyacrylamide gel electrophorab and SDS-polyacrylamide gel electrophoresis. Its molecular weight was estimated to be 17000 dalton by SDSpolyacrylsmlde gel electrophoresis. The optimum pH and temperature of the purified t-glucarase were. 7.0 and 50°C, respectively. The enzyme was strongly inhibited by 1.0 mM of Fe3 ; and activated by 1.0 mm of L4+The absence of glucose after thin layer_ chromatography of reaction products revealed that the purified enzyme contains no cellobiase or laminarinbiase activity. The liberation of di, tri-and tetrasacchazlde as reaction products can be explained by endoaction of the enzyme.
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