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Partial Characterization of a Low-Molecular-Mass Fraction with Cryoprotectant Activity from Jumbo Squid (Dosidicus gigas) Mantle Muscle.
Álvarez-Armenta, Andrés; Carvajal-Millán, Elizabeth; Pacheco-Aguilar, Ramón; García-Sánchez, Guillermina; Márquez-Ríos, Enrique; Scheuren-Acevedo, Susana María; Ramírez-Suárez, Juan Carlos.
Afiliação
  • Álvarez-Armenta A; Fishery Products Quality Laboratory, Food and Development Research Center, A.C. Carretera a La Victoria Km. 0.6, 83304 Hermosillo, Sonora, Mexico.
  • Carvajal-Millán E; Biopolymers Laboratory, Food and Development Research Center, A.C. Carretera a La Victoria Km. 0.6, 83304 Hermosillo, Sonora, Mexico.
  • Pacheco-Aguilar R; Fishery Products Quality Laboratory, Food and Development Research Center, A.C. Carretera a La Victoria Km. 0.6, 83304 Hermosillo, Sonora, Mexico.
  • García-Sánchez G; Fishery Products Quality Laboratory, Food and Development Research Center, A.C. Carretera a La Victoria Km. 0.6, 83304 Hermosillo, Sonora, Mexico.
  • Márquez-Ríos E; Department of Research and Postgraduate in Foods, University of Sonora, Blvd. Luis Encinas y Rosales S/N, Col. Centro, 83000 Hermosillo, Sonora, Mexico.
  • Scheuren-Acevedo SM; Fishery Products Quality Laboratory, Food and Development Research Center, A.C. Carretera a La Victoria Km. 0.6, 83304 Hermosillo, Sonora, Mexico.
  • Ramírez-Suárez JC; Fishery Products Quality Laboratory, Food and Development Research Center, A.C. Carretera a La Victoria Km. 0.6, 83304 Hermosillo, Sonora, Mexico.
Food Technol Biotechnol ; 57(1): 39-47, 2019 Mar.
Article em En | MEDLINE | ID: mdl-31316275
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 cryo- stability. 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.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Revista: Food Technol Biotechnol Ano de publicação: 2019 Tipo de documento: Article País de afiliação: México País de publicação: Croácia

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Revista: Food Technol Biotechnol Ano de publicação: 2019 Tipo de documento: Article País de afiliação: México País de publicação: Croácia