Original scientific paper

https://doi.org/10.17113/ftb.57.01.19.5848

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

Andrés Álvarez-Armenta ; Fishery Products Quality Laboratory, Food and Development Research Center, A.C. Carretera a La Victoria Km. 0.6, 83304 Hermosillo, Sonora, Mexico
Elizabeth Carvajal-Millán ; Biopolymers Laboratory, Food and Development Research Center, A.C. Carretera a La Victoria Km. 0.6, 83304 Hermosillo, Sonora, Mexico
Ramón Pacheco-Aguilar ; Fishery Products Quality Laboratory, Food and Development Research Center, A.C. Carretera a La Victoria Km. 0.6, 83304 Hermosillo, Sonora, Mexico
Guillermina García-Sánchez ; Fishery Products Quality Laboratory, Food and Development Research Center, A.C. Carretera a La Victoria Km. 0.6, 83304 Hermosillo, Sonora, Mexico
Enrique Márquez-Ríos ; Department of Research and Postgraduate in Foods, University of Sonora, Blvd. Luis Encinas y Rosales S/N, Col. Centro, 83000 Hermosillo, Sonora, Mexico
Susana María Scheuren-Acevedo ; Fishery Products Quality Laboratory, Food and Development Research Center, A.C. Carretera a La Victoria Km. 0.6, 83304 Hermosillo, Sonora, Mexico
Juan Carlos Ramírez-Suárez ; Fishery Products Quality Laboratory, Food and Development Research Center, A.C. Carretera a La Victoria Km. 0.6, 83304 Hermosillo, Sonora, Mexico

Abstract

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.

Keywords

squid muscle; myofibrillar protein; monosaccharides; free amino acids; cryostability

Hrčak ID:

218876

URI

https://hrcak.srce.hr/218876

Publication date:

29.3.2019.

Article data in other languages: croatian

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