지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2013.1
- 수록면
- 263 - 270 (8page)
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초록· 키워드
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A highly efficient extracellular ${\beta}$-1,3/1,4-glucanase was purified from the culture broth of Sistotrema brinkmannii HQ717718. The molecular mass of ${\beta}$-1,3/1,4-glucanase was respectively determined to be 83 and 166 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration chromatography, indicating that the enzyme is a dimer. The optimum activity of ${\beta}$-1,3/1,4-glucanase against Avicel was observed at pH 4.0 and $65^{\circ}C$. Under the same conditions, $V_{max}$, $K_m$, and $k_{cat}$ values for Avicel were $136.5U{\cdot}mg^{-1}$ of protein, 3.8 mM, and $211s^{-1}$, respectively. Furthermore, the DNA sequence of gene coding the enzyme showed a significant homology with hydrolases from the glycoside hydrolase family 55. Although ${\beta}$-1,3/1,4-glucanases have been purified and characterized from several other sources, S. brinkmannii ${\beta}$-1,3/1,4-glucanase is distinct from other ${\beta}$-1,3/1,4-glucanases due to its high catalytic efficiency toward Avicel and broad substrate specificity.
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