# Sodium Benzoate and Potassium Sorbate Inhibit Proteolysis and Promote Lipid Oxidation in Atlantic Herring Marinades Produced on an Industrial Scale

**Authors:** Mariusz Szymczak, Patryk Kamiński, Barbara Szymczak, Ingrid Undeland, Izabela Dmytrów

PMC · DOI: 10.3390/molecules30204103 · Molecules · 2025-10-15

## TL;DR

This study shows that preservatives in herring marinades slow protein breakdown but increase fat oxidation, slightly reducing quality and nutrition.

## Contribution

The study reveals that sodium benzoate and potassium sorbate inhibit proteolysis and promote lipid oxidation in industrial herring marinades.

## Key findings

- Preservatives reduced proteolysis by decreasing amino acid and peptide fractions in herring muscle.
- Lipid oxidation increased significantly with higher peroxide and TOTOX levels in preserved samples.
- Microbial growth was suppressed, but sensory quality slightly declined due to chemical off-flavors.

## Abstract

Cold-ripened fish marinades, produced mainly from Atlantic herring, represent one of the major seafood products in Northern and Central Europe. Because the shelf-life of these mildly acidified, salty products rarely surpasses 4 weeks, more than half of the commercial lots contain the preservatives sodium benzoate (E211) and potassium sorbate (E202). However, the broader technological consequences of such additives remain poorly documented. This study evaluated the impact of 0.25 (w/w) benzoate + 0.10 g/100 g sorbate on the quality of industrial-scale marinades (200 kg fish; 7 d, 4 ± 1 °C). Physicochemical traits (mass loss, pH, proximate composition, salt content, colour, and texture), enzymatic indices of ripening (cathepsins, amino-peptidases, and TCA soluble nitrogen fractions), lipid oxidation, microbial growth, and sensory attributes were analyzed. Preservatives caused only marginal changes in pH and proximate composition (0.3–3.4% w/w differences) but markedly suppressed proteolysis. Free amino acid and peptide fractions in muscle decreased by 6.0% and 8.8%, in parallel to 45% and 22% reductions in leucine- and alanine-amino-peptidase activities in muscle. In the marinating brine, the levels of total nitrogen, peptides, and free amino acids were also lower in the samples with preservatives, confirming that sodium benzoate and potassium sorbate slowed down the enzymatic ripening of the marinades. Concomitantly, peroxide, p-anisidine, and TOTOXs increased by up to 9.4, 71.3, and 33.7%, respectively, indicating accelerated lipid oxidation despite the chelating capacity of benzoate/sorbate acids. Overall sensory acceptability declined slightly (−0.15 points on a five-point scale), mainly owing to chemical off-flavours and lower juiciness. Microbial counts remained <1.0 log CFU/g in the preservative batch versus 2.1 log in the control. Benzoate–sorbate combinations effectively stabilized the microbiota of marinated herring without appreciably altering basic physicochemical traits, but they retard enzymatic ripening, diminish antioxidant peptide pools, and thereby promote lipid oxidation—collectively lowering the nutritional value. The data supports a cautious, minimal-use approach to application of chemical preservatives in cold-ripened fish products.

## Linked entities

- **Chemicals:** sodium benzoate (PubChem CID 517055), potassium sorbate (PubChem CID 23673839), E211 (PubChem CID 517055), E202 (PubChem CID 23676745)

## Full-text entities

- **Genes:** cathepsins [NCBI Gene 105891892]
- **Chemicals:** acid (MESH:D000143), Potassium Sorbate (MESH:D013011), amino acids (MESH:D000596), peroxide (MESH:D010545), Benzoate (MESH:D001565), p-anisidine (MESH:C013813), Lipid (MESH:D008055), Atlantic Herring Marinades (-), salt (MESH:D012492), nitrogen (MESH:D009584), Sodium Benzoate (MESH:D020160)

## Full text

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## Figures

3 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12566114/full.md

## References

55 references — full list in the complete paper: https://tomesphere.com/paper/PMC12566114/full.md

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Source: https://tomesphere.com/paper/PMC12566114