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PubMedDate not supplied

Optimization of chitin extraction from shrimp shells.

The aim of this paper is to define optimal conditions for the extraction of chitin from shrimp shells. The kinetics of both demineralization and deproteinization with, in the latter case, the role of temperature are studied. The characterization of the residual calcium and protein contents, the molecular weights, and degrees of acetylation (DA) allows us to propose the optimal conditions as follows. The demineralization is completely achieved within 15 min at ambient temperature in an excess of HCl 0.25 M (with a solid-to-liquid ratio of about 1/40 (w/v)). The deproteinization is conveniently obtained in NaOH 1 M within 24 h at a temperature close to 70 degrees C with no incidence on the molecular weight or the DA. In these conditions, the residual content of calcium in chitin is below 0.01%, and the DA is almost 95%.

Acetylation↗

PubMedDate not supplied

Characterization of shrimp shell deproteinization.

The aim of this paper was to contribute to the interpretation of the mechanism of shrimp shell deproteinization. We used amino acid analysis to quantify the amount of proteins remaining in chitin. NaOH 1 M was added to a demineralized shrimp shell powder with a solution-to-solid ratio of 15 mL/g at ambient temperature. Because of the limited precision of the technique, after 24 h the protein content measured by elemental analysis had to be considered as negligible. However, with the use of amino acid analysis, it was still possible to determine with precision this content down to 0.25%. We also showed that among the peptides remaining linked to chitin after deproteinization, acidic amino acids were always in proportion higher than alkaline ones, but the balance between the two kinds of residues increased in favor of the latter with time. The kinetic study of the deproteinization clearly revealed a three-step mechanism with very different rate constants. The variation of these constants with temperature was used to calculate the energies of activation and the frequency factors of collision, thus allowing us to propose a new interpretation of the mechanism of deproteinization.

Amino Acids↗