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곤충 병원성 곰팡이 Beauveria bassiana로부터 Protease의 정제와 특성
고휘진,김현규,김범기,강선철,권석태 ( Hwi Jin Ko,Hyun Kyu Kim,Beom Gi Kim,Sun Chul Kang,Suk Tae Kwon ) 한국응용생명화학회 1997 Applied Biological Chemistry (Appl Biol Chem) Vol.40 No.5
Extracellular protease (bassiasin I), from the culture filtrate of entomopathogenic fungus Beauveria bassiana ATCC7159, was successively purified by precipitation with ammonium sulfate followed by DEAE-Sephadex A-50, CM-cellulose and Hydroxyapatite column chromatography. A typical procedure provided 41-fold purification with 13.6% yield. The molecular weight of the purified protease (bassiasin I) was found to be approximately 32,000 by SDS-PAGE. Isoelectric-focusing analysis of the enzyme showed a pI of 9. 5. NH₂-terminal sequence of the protease showed homology with those of the fungal proteases. The enzyme has an optimal pH for activity at 10.5 and is stable over pH 5.0-11.0. The maximum activity of the enzyme was at 60-65℃, and approximately 20% activity remained at 60℃ after 120 min. The protease was inhibited by phenylmethylsulfonyl fluoride (PMSF) and diisopropyl fluorophosphate (DIFP).