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Partial Characterization of a Low-Molecular-Mass Fraction with Cryoprotectant Activity from Jumbo Squid (Dosidicus gigas) Mantle Muscle

Andrés Álvarez-Armenta1orcid tiny, Elizabeth Carvajal-Millán2orcid tiny, Ramón Pacheco-Aguilar1orcid tiny, Guillermina García-Sánchez1orcid tiny, Enrique Márquez-Ríos3orcid tiny, Susana María Scheuren-Acevedo1orcid tiny and Juan Carlos Ramírez-Suárezorcid tiny


Fishery Products Quality Laboratory, Food and Development Research Center, A.C. Carretera a La Victoria Km. 0.6, 83304 Hermosillo, Sonora, Mexico
2Biopolymers Laboratory, Food and Development Research Center, A.C. Carretera a La Victoria Km. 0.6, 83304 Hermosillo, Sonora, Mexico
3Department of Research and Postgraduate in Foods, University of Sonora, Blvd. Luis Encinas y Rosales S/N, Col. Centro, 83000 Hermosillo, Sonora, Mexico

Article history:
Received: 14 May 2018
Accepted: 11 December 2018

Key words:
squid muscle, myofibrillar protein, monosaccharides, free amino acids, cryostability

Freezing conditions affect fish muscle protein functionality due to its denaturation/aggregation. However, jumbo squid (Dosidicus gigas) muscle protein functionality remains stable even after freezing, probably due to the presence of low-molecular-mass compounds (LMMC) as cryoprotectants. Thus, water-soluble LMMC (<1 kDa) fraction obtained from jumbo squid muscle was evaluated by Fourier transform infrared spectrometry. From its spectra, total carbohydrates, free monosaccharides, free amino acids and ammonium chloride were determined. Cryoprotectant capacity and protein cryostability conferred by LMMC were investigated by differential scanning calorimetry. Fraction partial characterization showed that the main components are free amino acids (18.84 mg/g), carbohydrates (67.1 μg/mg) such as monosaccharides (51.1 μg/mg of glucose, fucose and arabinose in total) and ammonium chloride (220.4 μg/mg). Arginine, sarcosine and taurine were the main amino acids in the fraction. LMMC, at the mass fraction present in jumbo squid muscle, lowered the water freezing point to –1.2 °C, inhibiting recrystallization at 0.66 °C. Significant myofibrillar protein stabilization by LMMC was observed after a freeze-thaw cycle compared to control (muscle after extraction of LMMC), proving the effectiveness on jumbo squid protein muscle cryostability. Osmolytes in LMMC fraction inhibited protein denaturation/aggregation and ice recrystallization, maintaining the muscle structure stable under freezing conditions. LMMC conferred protein cryostability even at the very low mass fraction in the muscle.

*Corresponding author: tel3 +526622892400 ext: 654
                                          fax2 +526622800421

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