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Zongpei Zhao,이정걸,Priyadharshini Ramachandran,최준호,김인원 한국응용생명화학회 2013 Applied Biological Chemistry (Appl Biol Chem) Vol.56 No.3
A highly efficient extracellular β-1,3/1,4-glucanase was purified from the culture broth of Sistotrema brinkmannii HQ717718. The molecular mass of β-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 β-1,3/1,4-glucanase against Avicel was observed at pH 4.0 and 65oC. Under the same conditions, Vmax,Km, and kcat values for Avicel were 136.5 U · mg−1 of protein, 3.8mM, and 211 s−1, respectively. Furthermore, the DNA sequence of gene coding the enzyme showed a significant homology with hydrolases from the glycoside hydrolase family 55. Although β-1,3/1,4-glucanases have been purified and characterized from several other sources, S. brinkmannii β-1,3/1,4-glucanase is distinct from other β-1,3/1,4-glucanases due to its high catalytic efficiency toward Avicel and broad substrate specificity.
Zhao, Zongpei,Ramachandran, Priyadharshini,Choi, Joon-Ho,Lee, Jung-Kul,Kim, In-Won 한국응용생명화학회 2013 Applied Biological Chemistry (Appl Biol Chem) Vol.56 No.3
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.