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KMID : 0613820120220070920
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Journal of Life Science
2012 Volume.22 No. 7 p.920 ~ p.927
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Inhibitory Effects of Various Mulberry Fruits (Morus alba L.) on Related Enzymes to Adult Disease
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Chae Jung-Woo
Park Hye-Jin
Kang Sun-Ae
Cha Won-Seup
Ahn Dong-Hyun
Cho Young-Je
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Abstract
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The objective of this research was to develop the functional material of water and 60% ethanol extracts from nine kinds of mulberry fruits (Morus alba L.) that influence the inhibitory activity on angiotensin-converting enzyme, xanthine oxidase, α-amylase, and α-glucosidase. The total phenolic contents in the water extracts were over 2 mg/g in two species (Cheongilppong and Kangwon III) and five species (Daeyoupchosaeng, Cheongilppong, Kangwon III, Hihak, and Cataneo) of 60% ethanol extracts. The inhibitory activity against the angiotensin-converting enzyme was determined with them. Baekwoon III was 90.9±4.5% in the water extracts, and Hihak was 81.8±4.5% in the 60% ethanol extracts. The inhibitory activity of Kuksang 20 against xanthin oxidase was about 10% in the water extracts, and Cataneo was 21.4±2.3% in the 60% ethanol extracts. Six of the species (Daeyoupchosaeng, Suwonppong, Cheongilppong, Kangwon III, Hihak, and Kuksang 20) in the water extracts showed inhibitory activities against α-amylase, as 100%, respectively. The inhibitory activity of α-glucosidase was determined for these nine species. Four species (Baekwoon III, Daeyoupchosaeng, Cheongilppong, Kangwon III, Hihak, and Kuksang 20) in the water extracts and three species (Daechoukmyeun, Kangwon III, and Kuksang 20) in the 60% ethanol extracts showed inhibition of over 20%. The results revealed strong biological activity in spite of little total phenolic contents. These water and 60% ethanol extracts with high-quality biological activity from various mulberry fruits (Morus alba L.) are expected to represent good candidates for the development of antihypertentive and antidiabetes sources.
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KEYWORD
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Mulberry fruits (Morus alba L.), angiotensin converting enzyme, xanthine oxidase, α-amylase, α-glucosidase
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