1. Academic Validation
  2. Eritadenine from Edible Mushrooms Inhibits Activity of Angiotensin Converting Enzyme in Vitro

Eritadenine from Edible Mushrooms Inhibits Activity of Angiotensin Converting Enzyme in Vitro

  • J Agric Food Chem. 2016 Mar 23;64(11):2263-8. doi: 10.1021/acs.jafc.5b05869.
Sadia Afrin 1 Md Abdur Rakib 1 Boh Hyun Kim 1 Jeong Ok Kim 2 Yeong Lae Ha 1
Affiliations

Affiliations

  • 1 Division of Applied Life Sciences, Graduate School, and Institute of Agriculture & Life Science, Gyeongsang National University , Jinju 660-701, Republic of Korea.
  • 2 HK Biotech. Co., Ltd. , Jinju 660-884, Republic of Korea.
Abstract

The inhibition of angiotensin converting Enzyme (ACE) activity was determined in vitro by mushroom-derived eritadenine (EA), which was analyzed in 11 principal Korean edible mushrooms. EA inhibited ACE activity with 0.091 μM IC50, whereas the IC50 of captopril (CP), which is a reference compound, was 0.025 μM. Kinetic measurements of ACE reaction in the substrate of hippuryl-l-histidyl-l-leucine (HHL) with or without EA revealed that the Vmax (0.0465 O.D/30 min) was unchanged, but the the Km increased from 2.063 to 3.887 mM, indicating that EA competes with HHL for the active site. When EA was analyzed by HPLC, Lentinus edodes with a soft cap contained the highest amount EA (642.8 mg%); however, Phellinus linteus with a hard cap contained the least amount of EA (9.4 mg%). These results indicate that EA was a strong competitive inhibitor for ACE, and edible mushrooms with soft caps contained a significant amount of EA.

Keywords

IC50 value; angiotensin converting enzyme (ACE); competitive inhibition; edible mushrooms; eritadenine.

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