Structural and physiological studies on the storage β-polyglucan of haptophyte Pleurochrysis haptonemofera
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- 作者：Yasutaka Hirokawa (1)
Shoko Fujiwara (1) (2)
Motoya Suzuki (1)
Tomoka Akiyama (1)
Minako Sakamoto (1)
Saori Kobayashi (1)
Mikio Tsuzuki (1) (2) - 关键词：Chrysolaminaran ; β ; Glucanase ; Haptophyta ; Laminaran ; β ; Polyglucan ; Pustulan
- 刊名：Planta
- 出版年：2008
- 出版时间：February 2008
- 年：2008
- 卷：227
- 期：3
- 页码：589-599
- 全文大小：625KB
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Shoko Fujiwara (1) (2)
Motoya Suzuki (1)
Tomoka Akiyama (1)
Minako Sakamoto (1)
Saori Kobayashi (1)
Mikio Tsuzuki (1) (2)
1. School of Life Sciences, Tokyo University of Pharmacy and Life Sciences, 1432-1, Horinouchi, Hachioji, Tokyo, 192-0392, Japan
2. Science and Technology, CREST, Kawaguchi, Saitama, 332-0012, Japan
文摘
The storage β-polyglucan and catabolic enzyme activities of the haptophyte Pleurochrysis haptonemofera were characterized. The storage β-polyglucan was prepared by the dimethylsulfoxide-extraction method. 13C- and 1H-NMR spectroscopy revealed that the polyglucan consists of β-(1?)- and β-(1?)-linked glucose polymers, with a β-(1?)- to β-(1?)-linkage ratio of 1.5. Gel permeation chromatography showed that the molecular weight of the polyglucan is 1.1-.4?×?104?Da, with a peak at 3.4?×?104?Da. The degree of polymerization, which was estimated from the amounts of total carbohydrate and reduced ends, was 203, corresponding to 3.3?×?104?Da. A method for measurement of the β-polyglucan in a small amount of liquid culture involving a mixture of β-glucanases, Westase, was established. The β-polyglucan was localized in the soluble fraction of cells. The amount of β-polyglucan per cell increased at the stationary phase under continuous illumination and decreased in the dark, like those of storage α-polyglucans, starch of green algae and glycogen of cyanobacteria. The activities of β-1,3- and β-1,6-glucanases involved in the degradation of the storage β-polyglucan were assayed in vitro, both being optimal at pH 5.0. The β-1,3-glucanase activity, which was detected on active staining after native polyacrylamide gel electrophoresis, was partially purified by ammonium sulfate precipitation and anion exchange chromatography.