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

Freezing conditions affect fish muscle protein functionality due to its denaturation/aggregation. However, jumbo squid ( ) 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...

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Bibliographic Details
Published in:Food technology and biotechnology 2019-01, Vol.57 (1), p.39-47
Main Authors: Álvarez-Armenta, Andrés, Carvajal-Millán, Elizabeth, Pacheco-Aguilar, Ramón, García-Sánchez, Guillermina, Márquez-Ríos, Enrique, Scheuren-Acevedo, Susana María, Ramírez-Suárez, Juan Carlos
Format: Article
Language:English
Subjects:
Agglomeration
Amino acids
Ammonium
Ammonium chloride
Ammonium salts
Arabinose
Arginine
Biopolymer denaturation
Calorimetry
Carbohydrates
Cryoprotectants
Cryoprotectors
cryostability
Differential scanning calorimetry
Dosidicus gigas
Fish
Food
Fourier transforms
free amino acids
Freeze thaw cycles
Freeze-thawing
Freezing
Freezing point
Fucose
Glucose
Handbooks
Infrared spectra
Infrared spectroscopy
Melting points
Monosaccharides
Muscles
myofibrillar protein
Original Scientific Papers
Phase transitions
Protein denaturation
Protein folding
Proteins
Recrystallization
Sarcosine
Spectrometry
Spectroscopy
Squid
squid muscle
Studies
Taurine
Water
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Description
Summary:Freezing conditions affect fish muscle protein functionality due to its denaturation/aggregation. However, jumbo squid ( ) 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 (
ISSN:1330-9862
1334-2606
DOI:10.17113/ftb.57.01.19.5848