The temperature has a significant effect on cathepsin activity, but the effect of temperature on the ripening of marinades, and the formation of protein hydrolysis products, is less studied than other technological factors. The results of this study showed that herring marinated at 2 °C showed a higher mass yield, but lower non-protein nitrogen (NPN), peptides, and free amino acid fraction content, than after marinating at 7 and 12 °C. The higher temperature increased the free amino acid content the most, and decreased the hardness, as measured via sensory assessment, of the marinated meat. This was confirmed by the hardness measurement in the texture profile analysis. The highest activity of cathepsins D and B in the meat was found at 7 °C, while cathepsin L was found at 2 °C. Increasing the temperature by 10 °C increased the diffusion/loss of nitrogenous substances from the meat to the brine by 36%. The meat and brine showed high antioxidant activity, which depended on the marinating temperature, and originated mainly from the 5–10 or <5 kDa fraction. The meat had a higher ABTS (2,2′-azinobis-3-ethylbenzothiazoline-6-sulfonate) activity than the brine, opposite to the DPPH (2,2-diphenyl-1-picrylhydrazyl radical) activity, while the FRAP (Ferric Reducing Antioxidant Power) capacity was similar for meat and brine. The fractionation of the meat and brine extracts increased the antioxidant potential of FRAP and ABTS only for the brine. The most hydrophobic peptides were released during marinating at 7 °C. The meat and brine were dominated by 2–4 kDa peptides, followed by 4–6 and 0.5–2 kDa. The higher temperature favored a higher proportion of <4 kDa than >4 kDa peptides in the brine.