プロテアーゼによるローヤルゼリー分解物のアンジオテンシンＩ変換酵素阻害活性

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  • Inhibition of Angiotensin I-Converting Enzyme by Protease Digests from Royal Jelly
  • プロテアーゼ ニ ヨル ローヤルゼリー ブンカイブツ ノ アンジオテンシン 1 ヘンカン コウソ ソガイ カッセイ

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Royal jelly from the honeybee, Apis mellifera, is traditionally known to have some diverse nutritional and pharmacological functions. In order to clarify the potential physiological function of royal jelly, angiotensin-I converting enzyme (ACE)-inhibitory activities of its several protease digests were investigated. Not intact royal jelly but some protease digests showed ACE-inhibitory activities. The digests produced by Bacillus subtilis protease, protease N, had ACE-inhibitory activities with the 50% inhibition against ACE at 0.25mg/ml, which is the most potent among the various protease digests. The ACE-inhibitory activities of the protease-N digest did not change after further digestion by pepsin, trypsin and chymotrypsin. These results suggest that ACE-inhibitory activities in the protease-N digests were stable without being digested by gastrointestinal enzymes.

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