Angiotensin I-converting enzyme inhibitory proteins and peptides from the rhizomes of Zingiberaceae plants.

Applied biochemistry and biotechnology (2012-03-07)
Maneerat Yodjun, Aphichart Karnchanatat, Polkit Sangvanich
RESUMEN

Ammonium sulphate cut protein extracts, and their pepsin hydrolysates, from the rhizomes of 15 plants in the Zingiberaceae family were screened for their in vitro angiotensin I-converting enzyme inhibitory (ACEI) activity. The protein extract from Zingiber ottensii had the highest ACEI activity (IC(50) of 7.30 × 10(-7) mg protein/mL) and was enriched for by SP Sepharose chromatography with five NaCl step gradients 0, 0.25, 0.50, 0.75 and 1 M NaCl collecting the corresponding five fractions. The highest ACEI activity was found in the F75 fraction, which appeared to contain a single 20.7-kDa protein, suggesting enrichment to or near to homogeneity. The ACEI activity of the F75 fraction was moderately thermostable (-20-60 °C), showed >80% activity across a broad pH range of 4-12 (optimal at pH 4-5) and appeared as a competitive inhibitor of ACE (K(i) of 9.1 × 10(-5) mg protein/mL). For the pepsin hydrolysates, that from Zingiber cassumunar revealed the highest ACEI activity (IC(50) of 0.38 ± 0.012 mg/mL), was enriched to a single active hexapeptide by RP-HPLC with a strong ACEI activity (IC(50) of 0.011 ± 0.012 mg/mL) and acted as a competitive inhibitor of ACE (K(i) of 1.25 × 10(-6) mg protein/mL).

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SP Sepharose®, Fast Flow, aqueous ethanol suspension, 45-165 μm (wet), exclusion limit ~4,000,000 Da

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