期刊
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
卷 65, 期 1-4, 页码 63-67出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molcatb.2010.01.009
关键词
Hydroperoxide lyase; Yarrowia lipolytica; Secondary structure; Prediction; Circular dichroism spectroscopy
Fatty acid hydroperoxide lyase (HPL) is a member of the cytochrome P450 family acting on fatty acid hydroperoxides in many organisms. The active green bell pepper HPL, cloned and expressed in the yeast Yarrowia lipolytica, was purified by immobilized metal-ion affinity chromatography (IMAC) in the presence of 2% of Triton X-100R. The secondary structure prediction by bioinformatics servers of HPL was realized by ANTHEPROT software, using the GOR, DPM and Predator methods. The theoretical results which are average values obtained from three different calculation methods showed 33% alpha-helix, 18% beta-sheet, 7% turn and 42% coil. On the other hand, the secondary structure approach of the purified active HPL (specific activity of 2.94 U/mg protein) was realized by differential scanning calorimetry (DSC) and circular dichroism (CD) spectroscopy, and showed 13% alpha-helix, 29% beta-sheet, 5% turn and 53% random coil. (C) 2010 Elsevier B.V. All rights reserved.
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