Purification and Identification of Angiotensin I-Converting Enzyme Inhibitor from Morokheiya (Corchorus olitorius).
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概要
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In order to invesigate another function such as food in Morokheiya, the angiotensin-converting enzyme (ACE) inhibitor was extracted with 80% ethanol from the leaves of Morokheiya (<I>Corchorus olitorious</I>). The extract was dried, dissolved in water, defatted with ether and decolored with activated carbon. The ACE inhibitor was purified by successive ion-exchange chromatography, Amberlite IR-120B, Dowex 50W-X8 and Dowex 1-X4, respectively. The ACE inhibitor was further purified by silica gel column chromatography and finally purified and isolated by high performance liquid chromatography (HPLC) on Asahipak NH2P-50. The ACE inhibitor showed a positive ninhydrin reaction and no significant absorbance. The present ACE inhibitor was identified as Nicotianamine based on the comparative study using amino acid analyzer, TLC and capillary electrophoresis.
- 社団法人 日本食品科学工学会の論文
著者
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KIMOTO Koichi
Nutritional Biochemistry, Tokyo Kasei University
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KURODA Yuko
Nutritional Biochemistry, Tokyo Kasei University
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SAITO Yumiko
Nutritional Biochemistry, Tokyo Kasei University
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YAMAMOTO Junko
Nutritional Biochemistry, Tokyo Kasei University
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MURAKAMI Tetsuo
Food and Nutritional Chemistry, Kinki University
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AOYAGI Yasuo
Food Chemistry, Women's College of Nutrition
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AOYAGI Yasuo
Food Chemistry, Women's College of Nutrition