Inhibition of Angiotensin I-Converting Enzyme by Protease Digests from Royal Jelly

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  • 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
  • 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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Abstract

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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