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Freezing processes
Two freezing processeswere applied: air-blast freezing (conventional method) was performed in a pilot freezer (Servathin, Poissy, France) at −30 ¡ãC using an air speed 4 m/s, during 2 h (AF samples); pressure shift freezing (PSF samples) was carried out in a 3.5 L reactor unit (ACB Pressure Systems, Nantes, France) equipped with temperature and pressure regulator device. The temperature of the transmittingmedium (ethanol/water 50/50 %v/v) was maintained at −18 ¡ãC. Samples were placed in the vessel and the pressurewas increased to 200 MPa at a rate of 3 MPa/s.When the temperature of samples reached−18 ¡ãC, pressure
was rapidly released (2 s) to initiate the nucleation process. After depressurization, samples were left in the vessel for completion of the freezing under atmospheric conditions.

Microstructure analysis
Small pieces (approximately 5¡Á5¡Á10mm) were cut transversally to the fibers of frozen muscle inside a chamber at −20 ¡ãC. The isothermal freeze substitution technique (Martino & Zaritzky, 1986) was carried out with some modifications in these samples to visualize the size and location of the ice crystals. Pieces (3 pieces/sample, 2 samples/system) were placed in a fixative solution at −20 ¡ãC (Carnoy solution: 60% ethanol absolute, 30% chloroform, and 30% glacial acetic
acid). In the case of unfrozen samples (F), cuts and fixation were performed in a chamber at 5 ¡ãC. After fixation (24¨C48 h), samples were brought to room temperature, dehydrated with ethanol absolute (2 h), ethanol:toluene (50:50 %v/v) overnight and treated with toluene (4¨C 5 h). Dehydrated samples were consecutively immersed in toluene/ paraffin solutions of increasing paraffin concentration at 60 ¡ãC (1 h each) and in paraffin pure (2 h). Finally, samples were embedded in paraffin in small molds. Ten ¦Ìm thick sections (4 sections/piece) were
obtainedwith amicrotome (SM-2000-R, LeicaMicrosystems, Bensheim, Germany) and fixed to glass plates with glycerin albumin inwater (1/ 25 v/v), heating at 57 ¡ãC to melting the paraffin. After paraffin removing (toluene, twice, 10 min), solvent elimination (ethanol absolute) and rehydration (ethanol:water and pure water), sections were stained. First, samples were treated for 2 min with Orange G (0.5 g Orange G, 1 ml acetic acid, 99 ml distilled water, filtered at 0.45 ¦Ìm), which stained muscle proteins orange. After washing with distilled water, a second staining with Aniline blue for 2 min (0.01 g Aniline blue, 1 ml acetic acid, 99 ml distilled water, filtered at 0.45 ¦Ìm) was performed (for collagen staining) (Ch¨¦ret, Chapleau, Delbarre-Ladrat, Verrez-Bagnis & Lamballerie, 2006). Stained sections were mounted with Eukitt (Labonord, France). Observations were carried out in a microscope (Leica DML, Germany) equipped with a CCD RGB camera (MACC-C71, Sony, Japan).

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