Bioactivity of a pentapeptide isolated from corn gluten hydrolysate on Lolium perenne L.

Corn gluten hydrolysate (CGH) has been observed to inhibit root formation of germinating grass seeds and has the potential for use as a natural herbicide. Five dipeptides have been isolated from the aqueous solution of CGH and proved to have greater root-inhibiting activity than the crude extract of CGH. The objective of this study was to isolate and identify other biologically active compounds from CGH with herbicidal properties. A perennial ryegrass (Lolium perenne L.) Petri dish bioassay was used to test for the bioactivity. A pentapeptide, Leu-Ser-Pro-Ala-Gln, was isolated from CGH by using Sephadex G-15 gel filtration and two-step C18 reversed phase high performance liquid chromatography procedures. The compound suppressed growth of both the root and the shoot of germinating perennial ryegrass. It required 0.5 mg/mL of the pentapeptide to inhibit 50% of root length in the perennial ryegrass bioassay, and this compound is more active than any of the five dipeptides isolated previously from CGH.Abbreviations CGM corn gluten meal - CGH corn gluten hydrolysate - HPLC high performance liquid chromatography - RP reversed phase - MeOH methanol - AUFS absorbance units of full scale - Rt retention time - TFA trifluoroacetic acid - PTH phenylthiohydantoin - ANOVA analysis of variance