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Fang Gong,Tong Zhang,Jun Sheng,Jing Li,Xianghong Wang,Zhenming Chi 한국생물공학회 2008 Biotechnology and Bioprocess Engineering Vol.13 No.5
The extracellular inulinase of the marine yeast Pichia guilliermondii strain 1 was purified to homogeneity resulting in a 7.2-fold increase in specific inulinase activity. The molecular mass of the purified enzyme was estimated to be 50.0 kDa. The op-timal pH and temperature for the purified enzyme were 6.0 and 60C, respectively. The enzyme was activated by Mn²+, Ca²+, K+, Li+, Na+, Fe³+, Fe²+, Cu²+, and Co²+, but Mg²+, Hg²+, and Ag+ inhibited activity. The enzyme was strongly inhibited by phenylmethanesulphonyl fluoride (PMSF), iodoacetic acid, EDTA, and 1, 10-phenanthroline. The Km and Vmax values of the purified inulinase for inulin were 21.1 mg/mL and 0.08 mg/min, respectively. A large number of monosaccharides were de-tected after the hydrolysis of inulin. The deduced protein sequence from the cloned P. guilliermondii strain 1 inulinase gene contained the consensus motifs R-D-P-K-V-F-W-H and W-M-N-D-P-N-G, which are conserved among the inulinases from other microorganisms.