Angiotensin I-converting enzyme inhibitory activities of Chinese fermented soypaste and estimation of the inhibitory substances

Abstract

Angiotensin I-converting enzyme (ACE) inhibitory activities of aqueous extracts of Chinese commercial soypaste were investigated in this work. Six samples from northern China showed potent ACE inhibitory activities with IC50 values less than 40.0 μg/mL. ACE inhibitors in the sample with the strongest activity were purified by ultrafiltration, solid-phase extraction and gradient RP-HPLC. According to spectroscopic methods, a compound (M328.1) was separated as C15H21NO7. It was supposed to be a conjugate of phenylalanine and glucose generated by Maillard reaction during soypaste production, providing support on the contribution of Maillard reaction products to the ACE inhibitory activity of the sample. Results further indicated that the total ACE inhibition by the sample occurred from the combined function of various bioactive substances, suggesting that Chinese soypaste could be a good source of ACE inhibitors for exploring functional foods or ingredients with antihypertensive effect.

Keywords

• Angiotensin I-converting enzyme (ACE)
• Chinese soypaste
• ACE inhibitor
• Maillard reaction product
• Separation