Partial purification and characterization of two bacteriocin-like inhibitory substances produced by bifidobacteria

Authors

  • Abdelmajid Zouhir, Ehab Kheadr, Ismail Fliss ,Jeannette Ben Hamida

Keywords:

Bifidobacterium spp., bacteriocin-like inhibitory substance, bacteriocin-like inhibitory substances activity.

Abstract

Bifidobacterium spp. RBL 68 and RBL 85 isolated from newborn faeces were found to produce two
bacteriocin-like inhibitory substances (BLIS) with inhibitory activities against a wide range of Grampositive and Gram-negative bacteria. The production of these BLIS began in late exponential phase of
growth and reached a maximum activity during and after the stationary phase. An activity level of 33
and 15 AU/ml at the end of the exponential phase that is (12 h) and maximum activity (65 and 35 AU/ml)
at the beginning of the stationary phase that is (24 and 36 h) were recorded in MRS broth at 37°C for
RBL 68 and RBL 85, respectively. The two BLIS, produced by RBL 68 and RBL 85, were partially purified
by a three-step purification protocol resulting in a specific activity of 2.66 x 103
and 7.68 x 103
AU/mg
and purification fold of 122.8 and 95, respectively. Complete inactivation of the two BLIS activities were
observed after treatment with proteolytic enzymes, including chymotrypsin, pronase E and proteinase
K. These proteinaceous compounds were active against food- borne diseases and food spoilage
pathogens such as Listeria monocytogenes, which make them potentially useful as antimicrobial
agents in foods.

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Published

2022-03-18