Gelatin was extracted from the skin of giant squid (Dosidicus gigas) with a yield of 7.5% on a wet weight basis through a novel cold maturation process and it was chemical, physicochemical and structurally characterized. Squid skin gelatin (SSG) had high protein content (89%) with an amino acid profile similar to that of interstitial collagen. Infrared spectroscopy and circular dichroism confirmed the existence of specific bands of collagen and gelatin which are modified during their thermal transition. Amino acids present in SSG were revealed by NMR signals. Fluorescence spectroscopy revealed emission due to pyridinoline cross-links. Differential scanning calorimetry confirmed that SSG is a weak thermo-reversible gel. Scanning electron microscopy showed porous components within the SSG structure which agree with the viscosity and water holding capacity values obtained. These results led to a better understanding on the molecular structure of SSG which accounts for its well known rheological and physicochemical properties.

Original languageEnglish
Pages (from-to)3243-3249
Number of pages7
JournalFood Research International
Issue number10
StatePublished - Dec 2011

Bibliographical note

Funding Information:
This research was supported by CONACYT under the grant 89879 . Author Uriarte-Montoya acknowledges doctoral fellowship from CONACYT. The authors are also grateful to Rocío Sugich for her skillful performance of CD measurements and to Benjamin Ramírez for his technical assistance.


  • Biophysical properties
  • Collagen
  • Gelatin
  • Squid


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