Abstract

In this study, broad bean protein hydrolysates (BPH) produced by alcalase with strong-stimulating activity for lactic acid bacteria (LAB) was first time reported. In order to obtain the key peptide that have growth-stimulating activity for lactic acid bacteria (LAB), gel filtration chromatography and Reverse Phase High Performance Liquid Chromatography (RP-HPLC) were applied to isolate and purify the peptides from BPH. Finally, F4-2 elicited the highest activity for LAB, corresponding to amino acid sequence Ser-Ala-Gln (304.10Da) was identified by Matrix-Assisted Laser Desorption/Ionization Time of Flight Mass Spectrometry (MALDI-TOF/TOF MS/MS). Thus, this study shows that broad bean peptide is a good source to promote the LAB growth and this function is reported for the first time.

Keywords:

Broad bean peptide, growth-stimulating, identification, lactic acid bacteria (LAB), purification,

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