Angiotensin I-Converting Enzyme Inhibitory Proteins and Peptides from the Rhizomes of Zingiberaceae Plants |
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Authors: | Maneerat Yodjun Aphichart Karnchanatat Polkit Sangvanich |
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Institution: | (1) Program in Biotechnology, Faculty of Science, Chulalongkorn University, 254 Phayathai Road, Pathumwan, Bangkok, 10330, Thailand;(2) Institute of Biotechnology and Genetic Engineering, Chulalongkorn University, 254 Phayathai Road, Pathumwan, Bangkok, 10330, Thailand;(3) Department of Chemistry, Faculty of Science, Chulalongkorn University, 254 Phayathai Road, Pathumwan, Bangkok, 10330, Thailand; |
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Abstract: | 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 (IC50 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 (IC50 of 0.38 ± 0.012 mg/mL), was enriched to a single active hexapeptide by RP-HPLC with a strong ACEI activity (IC50 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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