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KMID : 0364819870250020157
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Korean Journal of Microbiology
1987 Volume.25 No. 2 p.157 ~ p.164
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Purification and Properties of β-1. 4-glucanase from Thermophilic Clostridium thermocellum
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Kim, Uk-Han/김욱한
Ha, Ji-Hong/Chung, Ki-Taek/Lee, Yong-Hyun/하지홍/정기택/이용현
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Abstract
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1
A new endo-f4-1,4-glucanase was purified from the culture filtrate of tbermophilic anaerobic Clostridium thermoceuum. The purification procedure included two steps of ion exchange chromatography with DEAE-Sephadex A-50 and gel filtration chromatography with Sephadex G-75. Even though the 56 fold increase in CMCase specific activity was obtained, the actually recovered enzyme activity was relatively lower level of 0.7%. Judging from the two bands in SDS-polyacryhmide gel electrophoresis, the endo-fl-1,4-giucanase consists of two subunits whose M.W. are 38,000 and 58,000, respectively. The optimum pH and temperature were determined to be 5.0 and 65°C,respectively. The enzyme was stable up to 70°C, but inactivated at 80°C.The kinetic parameters of the separated fraction were also determined. The purified enzyme did not show any significant hydrolytic activity against the highly ordered crystalline cellulose as well as filter paper.
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