単離したダイズオイルボデイの構造解析と酵素による分解

島根大学農学部研究報告 Volume 28 Page 93-98 published_at 1994-12-20
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Title
単離したダイズオイルボデイの構造解析と酵素による分解
Title
Isolation and Structural Analysis of Soybean Oil Bodies and in vitro Enzymatic Degradation of the Bodies
Title Transcription
タンリ シタ ダイズ オイル ボディ ノ コウゾウ カイセキ ト コウソ ニヨル ブンカイ
Creator
Tsuru Takami
Mori Megumu
Takinami Koichi
Source Title
島根大学農学部研究報告
Bulletin of the Faculty of Agriculture, Shimane University
Volume 28
Start Page 93
End Page 98
Journal Identifire
ISSN 0370940X
Descriptions
Plant seed oils which are stored in cotyledons and embryos from small discrete intracellular particles called oil bodies. An oil body has a matrix of TAG, which is surrounded by a layer composed of phospholipids and proteins termed oleosins. In order to investigate the phycicochemcal and biochemical properties of oil bodies, the isolated and purified oil bodies were prepared from native soybean by the methods of flotation centrifugation, and then they were provided for the following experiments. Oil bodies were considerably stable at neutral pH and at less than 100℃. The surface active agents used here except sodium dodecyl sulfate did not decompose d the oil bodies. Thus, an oil body structure was indicated that the surface of the membrane was occupied by oleosins behind which there existed phospholipids. On the other hand, lipase broke the oil bodies and hydrolyzed triacylglycerol in them. Trypsin hydrolyzed partially the surface protein of the oil body, but the particle from of the oil body was maintained further. Lipase has been reported to hydrolyze the triacylglycerol in oil bodies during seed germination. The in vivo lipase reaction was reappeared in vitro in this investigation. It seems that oleosins, oil body membrane proteins, would be necessary to maitain the oil body structure and would play an important role in the lipase reaction.
Key words: Oilbody; oleosin; lipase.
Language
jpn
Resource Type departmental bulletin paper
Publisher
島根大学農学部
Shimane University, Faculty of Agriculture
Date of Issued 1994-12-20
Access Rights open access
Relation
[NCID] AN00108015