Review: Quality and authentication of organic animal products in Europe.

The 'organic' label guarantees a production process that avoids the use of synthetic fertilisers, pesticides and hormones and minimises the use of veterinary drugs; however, consumers are demanding guarantees regarding food quality. This article reviews the current state of knowledge on the quality of organic animal products, including the authentication of their organic origin. Quality has been considered as an integrative combination of six core attributes: commercial value, and nutritional, sensory, technological, convenience and safety attributes. The comparison of these attributes between organic and conventional animal products shows high heterogeneity due to variability in farming pratices in both organic and conventional systems. To overcome this, we pinpoint the farming practices underlying the differences observed. This enables light to be shed on the consequences of possible trajectories of organic farming, if specifications are relaxed or tightened up on commitments concerning farming practices that impact product quality. Two recent meta-analyses showed better nutritional attributes in organic milk and meat linked to their higher poly-unsaturated fatty acid (PUFA) content, particularly n-3 PUFAs. Regarding safety, we point to a lack of integrated studies quantifying the balance between positive and negative effects. Organic farming reduces the risk of drug residues and antibiotic resistance, but both outdoor rearing and a frequently longer rearing period increase the animals' exposition to environmental contaminants and the risk of their bioaccumulation in milk, eggs, meat and fish flesh. We highlight antagonisms between quality attributes for certain animal products (lamb, pork). In general, attributes are more variable for organic products, which can be explained by lower genetic selection (poultry), lower inputs and/or greater variability in farming conditions. However, the literature does not address the implications of this greater variability for the consumers' acceptability and the necessary adaptation of manufacturing processes. Further research is needed to document the impacts on human nutritional biomarkers and health. Methods used to authenticate organic origin are based on differences in animal diet composition between organic and conventional systems, but their reliability is hampered by the variability in farming practices.

Monitoring of four DNA extraction methods upstream of high-throughput sequencing of Anisakidae nematodes.

Different methods were evaluated to extract DNA from pooled nematodes belonging to Anisakis, Contracaecum, Pseudoterranova and Hysterothylacium genera isolated from edible fish. Pooled DNA extraction is the first and compulsory step to allow the identification of a large number of samples through high-throughput DNA sequencing with drastic time and cost reductions.

Effect of high pressure on the calpain-calpastatin system in fish muscle.

Calpains (calcium-activated neutral proteases) of sea bass (Dicentrarchus labrax L.) muscle may participate in the degradation of muscle tissue during postmortem storage. These enzymes are regulated by calpastatin, their endogenous specific inhibitor. The objective of this study was to evaluate the changes encountered by the calpain system during the postmortem storage of fish muscle after high-pressure treatment. From 100 MPa, high-pressure treatment of purified calpains results in a loss of their activity as well as in the dissociation of the heterodimeric form. In muscle, the high-pressure processing decreases the initial activity of calpain. This loss in activity may be due to an inactivation by a change of structure. Initial calpastatin activity is not modified by the high-pressure treatment, but it decreases during the storage from the beginning for a treatment at 300 MPa after which calpastatin is stable during 2 d. Therefore, this study also suggests that high-pressure treatment could be a useful way to improve fish flesh quality.

Protein changes in post mortem sea bass (Dicentrarchus labrax) muscle monitored by one- and two-dimensional gel electrophoresis.

This study was devoted to the identification of specific peptides and proteins which can be used as indicators of freshness in fish. The post mortem evolution of protein patterns in farmed sea bass muscle was monitored by Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and two-dimensional electrophoresis (2-DE) after 0, 2, 4, and 6 days cold storage. SDS-electrophoresis, of total proteins and proteins soluble in low-ionic-strength solutions, revealed the gradual disappearance of a protein band of 16 kDa immediately after fish death. 2-DE allowed the classification of fish samples according to post mortem time. Three spots of interest, which disappeared progressively, were identified on the 2-DE patterns. Further research is required to establish the identity of these polypeptides and to evaluate their expression and post mortem evolution in another fish species.

Neutral calcium-activated proteases from European sea bass (Dicentrarchus labrax L.) muscle: polymorphism and biochemical studies.

Calcium-dependent proteinases or calpains were studied in fish muscle. Hydrophobic chromatography, followed by anion-exchange chromatography of the soluble fraction of sea bass white muscle proteins, resulted in three peaks of calcium-dependent protease activity at neutral pH (A, B and C). They are all neutral cysteine calcium-activated proteinases and can, therefore, be classified as calpain-like enzymes. From the Ca2+ concentration required for activity, A is a mu-calpain, and B and C are m-calpains. They share many properties with calpains from other vertebrate cells but differ in native mass, subunit composition, and the unusual numbers in which they are present. Their specific pattern of expression throughout the year could be of great importance to the resulting rate and extent of degradation of fish flesh after death.

Use of two-dimensional electrophoresis to evaluate proteolysis in salmon (Salmo salar) muscle as affected by a lactic fermentation.

Two-dimensional electrophoresis was used to study proteolysis in salmon fillets inoculated or not with the starter culture Lactobacillus sake LAD. Protein fragments appeared increasingly with time in both samples, indicating that the main quantitative changes were due to endogenous enzymes. In the most acidic zone (pI = 4-6. 20) particularly, proteolysis was overall independent from processing. In contrast, fermentation had a significant effect in the pH range 6.20-8.35, suggesting a specificity of the bacterial proteases of L. sake toward alkaline to slightly acidic proteins. Furthermore, fragments surrounding tropomyosin (apparent pI = 4.70) appeared in fermented samples, indicating that the protein may be a suitable substrate for the metabolism of L. sake LAD.

Isolation and properties of white skeletal muscle alpha-actinin from sea-trout (Salmo trutta) and bass (Dicentrarchus labrax).

Fish alpha-actinin purified from sea-trout and bass white muscle by means of two different extraction procedures was used to investigate the eventual presence of different muscle isoforms in Z-disks. These fish alpha-actinins have the same apparent molecular weight (100 kDa) and the same isoelectric point (pI = 5.6), and also have a total antigenic identity towards anti-bass and anti-chicken alpha-actinin antibodies, suggesting a single molecular species. The role of fish alpha-actinin as an anchorage site for thin actin filaments and elastic titin filaments in Z-bands was studied. Despite conservation of the actin-binding site, fish alpha-actinin has a better actin-binding ability (kD = 0.3 microM) than chicken smooth muscle alpha-actinin (kD = 1.6 microM). Several other structural and functional characteristics of fish alpha-actinin were also studied: conservation of sequence and domain structure, the role of divalent ions (Ca2+, Mg2+) and the dielectric constant of the medium in alpha-actinin-actin interaction. Although the reason for fish white muscle alpha-actinin's close affinity to actin was not clearly established, our results suggested that the physicochemical environment of the Z-filaments in Z-disks might be crucial.

Physico-chemical properties and rheological behaviour of Patella caerula paramyosin.

Paramyosin is a muscle protein which is characteristic of all invertebrates but which is not present in vertebrate muscles. Given the functional importance of paramyosin, the purpose of this paper was to study the physico-chemical properties, including the amino acid composition and rheological behaviour, of purified paramyosin and to investigate its mode of interaction with myosin. Paramyosin was purified from the limpet (Patella caerula) by an ethanol precipitation step. It was soluble at ionic strengths below 0.05 M NaCl and its maximum solubility at neutral pH occurred at approximately 0.4 M NaCl. At this high ionic strength, the pH dependence of solubility was such that paramyosin passed quickly into solution when pH exceeded pH 5, the transitional pH value. By using an immunological method, it was shown that interactions between paramyosin and myosin occurred, even in the presence of actin. The molecular assembly of both proteins was probably specified by hydrophobic interactions, as well as by interactions enhanced by divalent cations. The changes in the dynamic shear storage modulus (G') started between 40 degrees C and 50 degrees C, and reached a maximum at about 75 degrees C.