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[Separation, purification and identification of angiotensin converting enzyme inhibitory silk fibroin peptide].

Silk fibroin peptides could be obtained from soluble silk fibroin by enzymatic hydrolysis. Its hydrolyzates produced with Alcalase showed significant inhibitory activity against the angiotensin I-converting enzyme (ACE). One inhibitory peptide from the hydrolyzate at a degree of hydrolysis of 20% (sample A20) was purified and identified. Sample A20 was first isolated by size exclusion chromatography(SEC), eluted with 0.01 mol/L hydrochloric acid solution on a Sephadex G-15 column (1.6 cm i.d. x 100 cm). The peak of No. 5 on the SEC chromatography was further purified by reversed-phase HPLC (mu Bondapak C18 P/N 84176 column, 7.8 mm i.d. x 300 mm), eluted with a linear gradient elution with acetonitrile from 0% to 15% at temperature (30 +/- 2) degrees C. Then the pure peptide with ACE inhibitory activity was obtained, the amino acid sequence of which was identified as Gly-Tyr by mass spectrometry.