Lipid oxidation is the primary non-microbial reason for quality deterioration of meat and meat products. Lipid oxidation can be prevented or delayed by antioxidants. In this study, 15 sage (Salvia spp. Labiatae) extracts (five genotypes, three harvest times) were tested for their ability to reduce lipid oxidation (peroxide value (PV) and thiobarbituric acid reactive substances (TBARS)) in ground, uncured, cooked porcine and bovine meat (60%/40% mixture) during 14 days of refrigerated storage. Additionally, total phenolic content was determined, and the antioxidant capacity of the extracts was measured as radical scavenging activity (2,2-diphenyl-1-picrylhydrazyl assay), reducing power, and superoxide anion scavenging activity. All 15 sage extracts were able to reduce lipid oxidation, though showing expected differences depending on genotype and harvest time. The extracts of S. officinalis accession from Foggia, Italy performed better than the other genotypes when looking at the entire storage period and considering both PV and TBARS. Of the applied methods for determining antioxidant capacity, superoxide anion scavenging activity proved to be the best determinant of the ability of sage to reduce lipid oxidation in the meat sample.

Proteins in the thioredoxin superfamily share a similar fold, contain a -CXXC- active site, and catalyze oxidoreductase reactions by dithiol-disulfide exchange mechanisms. Protein disulfide isomerase (PDI) has two -CGHC- active sites. For in vitro studies, oxidation/reduction of PDI during the catalytic cycle is accomplished with glutathione. Glutathione may act as electron donor/acceptor for PDI also in vivo, but at least for oxidation reactions, GSSG probably is not the major electron acceptor and PDI may not have evolved to react with glutathione with high affinity, but merely having adequate affinity for both glutathione and folding proteins/peptides. Glutaredoxins, on the other hand, have a high affinity for glutathione. They commonly have -CXFC- or -CXYC- active site, where the tyrosine residue forms part of the GSH binding groove. Mutating the active site of PDI to a more glutaredoxin-like motif increased its reactivity with glutathione. All such variants showed an increased rate in GSH-dependent reduction or GSSG-dependent oxidation of the active site, as well as a decreased rate of the native disulfide bond formation, with the magnitude of the effect increasing with glutathione concentration. This suggests that these variants lead to competition in binding between glutathione and folding protein substrates.

The editors of Antioxidants would like to express their sincere gratitude to the following reviewers for assessing manuscripts in 2016.

Peer review is an essential part in the publication process, ensuring that Antioxidants maintains high quality standards for its published papers.

Peer review is the driving force of journal development, and reviewers are gatekeepers who ensure that Antioxidants maintains its standards for the high quality of its published papers

The editors of Antioxidants would like to express their sincere gratitude to the following reviewers for assessing manuscripts in 2014: