Abstract

Pulsed electric field (PEF) technology was used to enrich Lactobacillus rhamnosus B 442 cells in zinc ions to obtain source of this element with high bioavailability. The highest bioaccumulation of zinc was achieved when electroporation was performed at optimal parameters: field strength of 3.0 kV/cm, pulse width of 20 µs, electroporation time of 15 min after 20 h of culturing and at zinc concentration of 500 µg/mL medium. The maximum bioaccumulation of ions in cells (2.85 mg Zn/g d.m.) was 164% higher than in the control sample which was supplemented with zinc but not treated with PEF. The action of PEF did not reduce the total number of microorganisms in the medium or the biomass of bacteria.

Highlights

  • Zinc is one of the most important micronutrients in people’s diet, as it is a component of over 200 metalloproteins and takes part in a number of biochemical reactions involving enzymes, structural proteins, and hormones [1]

  • When cultures were treated with Pulsed electric field (PEF) at 750 μg Zn/mL medium and 1000 μg Zn/mL medium, a statistically significant reduction in Z­ n2+ bioaccumulation was noted when compared to the sample electroporated at 500 μg Zn/mL medium

  • In the case of the samples not treated with PEF, the highest total number of microorganisms was found for the cultures supplemented with 1000 μg Zn/mL medium

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Summary

Introduction

Zinc is one of the most important micronutrients in people’s diet, as it is a component of over 200 metalloproteins and takes part in a number of biochemical reactions involving enzymes, structural proteins, and hormones [1]. The appropriate zinc concentration in cells is essential for the proper functioning of the system which protects the body from oxidative damage [2, 3]. This element participates in the metabolic processes of the cell and in gene expression and it is considered to be safe for health (has no oxidizing capacity) [4, 5]. In zinc-supplemented microorganisms it is bound in protein complexes that are absorbed in the small intestine analogously to proteins and peptides [14]

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