Abstract
Peptides inhibitory to partially purified endopeptidase and crude proteinase from Pseudomonas fluorescens ATCC 948 were isolated from tryptic hydrolysates of zein and hordein by reversed-phase fast protein liquid chromatography and identified by sequencing. The sequences are Ser-Ala-Tyr-Pro-Gly-Gln-Ile-Thr-Ser-Asn and Gln-Val-Ser-Leu-Asn-Ser-Gly-Tyr-Tyr for peptides from zein and hordein, respectively. Inhibitions of >85% and from >50 to >85% were determined on endopeptidase and proteinase by peptides from zein and hordein. Ki values ranged from 4 to 32 μM. The same peptides also showed inhibition of the angiotensin I-converting enzyme. The concentrations of peptides providing 50% inhibition of angiotensin I-converting enzyme were 7 and 23μm for the decapeptide and nonapeptide, respectively. Other fractions containing peptides with less inhibitory activity were detected in the zein as well as in the gluten tryptic digests.
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