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The control of micro-organisms responsible for pre- and postharvest diseases of agricultural products, mainly viruses and fungi, is a problem that remains unresolved, together with the environmental impact of the excessive use of chemicals to tackle this problem. Current efforts are focused on the search for efficient alternatives for microbial control that will not result in damage to the environment or an imbalance in the existing biota. One alternative is the use of natural antimicrobial compounds such as chitosan, a linear cationic biopolymer, which is biodegradable, biocompatible and non-toxic, has filmogenic properties and is capable of forming matrices for the transport of active substances. The study of chitosan has attracted great interest owing to its ability to form complexes or matrices for the controlled release of active compounds such as micro- and nanoparticles, which, together with the biological properties of chitosan, has allowed a major breakthrough in the pharmaceutical and biomedical industries. Another important field of study is the development of chitosan-based matrices for the controlled release of active compounds in areas such as agriculture and food for the control of viruses, bacteria and fungi, which is one of the least exploited areas and holds much promise for future research. © 2013 Society of Chemical Industry [ABSTRACT FROM AUTHOR]

Muscle texture, which plays an important role in the acceptability and commercialization of seafood products, can be affected by collagen, the principal component of connective tissue in animals. In recent years, research in food science and technology has focused on how the physicochemical properties of collagen and cross-linking indicators affect the muscular texture of cephalopods; nonetheless, to date there are no reviews addressing these issues together. Information has been gathered on the physicochemical characterization and the collagen cross-linking level from the main cephalopods, founding a close interdependence with the structural characteristic of their muscle. As a conclusion, it is suggested that the texture of cephalopods is tougher than that of other marine organisms because their muscle fibers are covered by more extensively crosslinked connective tissue; therefore, the muscle is more stable during post-catch handling, such as during heating, freezing, and other processes that affect the quality of their meat. [ABSTRACT FROM AUTHOR]

Collagen is the major connective tissue (CT) protein and one of the main constituents of the jumbo squid (Dosidicus gigas). Therefore, physicochemical changes of pepsin-solubilized collagen (PSC) and insoluble collagen (IC) were studied after cooking (100°C/30 min) of muscle (mantle, fins, and arms). Different pyridinoline (Pyr) contents (the major cross-linking molecule in collagen fibers) were found in the fresh muscle of the three anatomical regions. After the cooking process, a decrease from 10 to 30% in the thermal resistance of collagen was observed, depending on the anatomical region and fraction evaluated. Furthermore, the electrophoretic profile, Fourier transform infrared (FTIR) spectroscopy, and the amino-acid profile revealed that structural changes occurred in the two different collagen fractions caused by the thermal process, and the changes were greater in the mantle. Under the conditions applied in this study, collagen fractions from the squid arms showed more stability during the cooking process due to the high cross-linking degree of their fibers. [ABSTRACT FROM AUTHOR]

Connective tissue (CT) proteins in jumbo squid ( Dosidicus gigas) play an important role because they are the responsible for the union between various cells; hence, there is a close relationship between their functions and muscle firmness during ice storage. In this study, the thermal resistance and solubility of the CT extracted from the fins, mantle and arms of jumbo squid during ice storage (20 days) was evaluated. The CT was fractionated based on solubility [NaCl-soluble (SSCT) and insoluble (ICT)]. The solubility of the CT was affected during ice storage. An increase in the thermal resistance of the SSCT after 10 days with a subsequent decrease was found in the mantle. Furthermore, the ICT was thermally more resistant than the SSCT in all the anatomical regions. Finally, the electrophoretic profile revealed that structural changes occurred, causing changes in its solubility, due to an increase in the thermal resistance. Practical Applications Jumbo squid ( Dosidicus gigas) is an important seafood resource in Mexico, which is commercialized primarily iced and fresh-frozen. Its muscle connective tissue (CT) has different physicochemical characteristics that differ from other seafood products; it is thermally more resistant and might be responsible for the textural changes during ice storage. Moreover, specific studies about the behavior of CT proteins in such organism may result in improved post-catch management of jumbo squid muscle, focused on the processing of the species in the food industry or anywhere that CT proteins are used as raw material. The main objective of this research is to investigate solubility changes and thermal resistance of CT proteins of iced jumbo squid mantle. [ABSTRACT FROM AUTHOR]