期刊
BIOTECHNOLOGY AND BIOPROCESS ENGINEERING
卷 13, 期 5, 页码 533-539出版社
KOREAN SOC BIOTECHNOLOGY & BIOENGINEERING
DOI: 10.1007/s12257-007-0177-7
关键词
inulinase; inulinase gene; marine yeasts; purification; Pichia guilliermondii
资金
- Hi-Tech Research and Development Program of China [2006AA09Z403]
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 optimal pH and temperature for the purified enzyme were 6.0 and 60 degrees C, 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 K-m and V-max values of the purified inulinase for inulin were 21.1 mg/mL and 0.08 mg/min, respectively. A large number of monosaccharides were detected 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. (C) KSBB
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据