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In vitro ability of nonviable cells of lactic acid bacteria strains in combination with sorbitan monostearate to bind to aflatoxin M1 in skimmed milk.

Authors :
Muaz, Khurram
Riaz, Muhammad
Rosim, Roice Eliana
Akhtar, Saeed
Corassin, Carlos Humberto
Gonçalves, Bruna Leonel
Oliveira, Carlos Augusto Fernandes
Source :
LWT - Food Science & Technology. Jul2021, Vol. 147, pN.PAG-N.PAG. 1p.
Publication Year :
2021

Abstract

This study aimed to evaluate the in vitro ability of heat-killed (HK) and acid-killed (AK) cells from three commercial strains of lactic acid bacteria, alone or in combination with sorbitan monostearate (SM), to bind to aflatoxin M 1 (AFM 1) in skimmed milk at concentrations of 0.05, 0.2 and 0.5 ng mL−1. The stability of the AFM 1 -bacterial cell bonds and the cell wall and exopolysaccharides (EPS) contribution to AFM 1 decontamination were also investigated. Compared with HK cells, AK cells exhibited higher binding capacities in milk containing the highest AFM 1 level, with maximum removal of 81.4, 56.8, and 50.8% by Lactococcus lactis ssp. cremoris , Lacticaseibacillus rhamnosus (formerly Lactobacillus rhamnosus), and L. lactis ssp. lactis at 1010 cells mL−1, respectively. The combination of HK cells with SM increased the AFM 1 binding capacity, although no effect was found regarding AK cells. SM treatment also enhanced the stability of the AFM 1 bond formed with both HK and AK cells. Cell wall isolates and EPS were the major components involved in the AFM 1 binding process. Combining SM with HK cells is an interesting approach to reduce AFM 1 levels in milk, although further studies are needed to optimize the adsorbing process. [Display omitted] • Heat-killed (HK) and acid-killed (AK) LAB capacities to adsorb AFM 1 in skimmed milk. • Higher AFM 1 adsorption percentages (50.8–81.4%) by AK cells. • HK cells combined with sorbitan monoesterase (SM) had increased AFM 1 bind capacity. • SM increased the stability of the AFM 1 – bacterial cell complex. • Exopolysaccharides were the major components involved in the AFM 1 binding process. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00236438
Volume :
147
Database :
Academic Search Index
Journal :
LWT - Food Science & Technology
Publication Type :
Academic Journal
Accession number :
151022668
Full Text :
https://doi.org/10.1016/j.lwt.2021.111666