Details

Autor(en) / Beteiligte

• Ramírez-Guerra, Hugo E.
• Mazorra-Manzano, Miguel A.
• Ezquerra-Brauer, Josafat M.
• Carvajal-Millán, Elizabeth
• Pacheco-Aguilar, Ramón
• Lugo-Sánchez, María E.
• Ramírez-Suárez, Juan C.

Titel

Hydroxylysyl-pyridinoline occurrence and chemical characteristics of collagen present in jumbo squid (Dosidicus gigas) tissues

Ist Teil von

• Journal of food composition and analysis, 2015-12, Vol.44, p.10-17

Ort / Verlag

Elsevier Inc

Erscheinungsjahr

2015

Link zum Volltext

Quelle

Alma/SFX Local Collection

Beschreibungen/Notizen

• •Chemical differences between muscle and skin squid collagens were reported.•Lysine was highly hydroxylated in muscle collagen.•Hydroxylysyl-pyridinoline was distributed only in muscle collagen.•A high amount of carbohydrates was found in analyzed collagens.•Muscle collagen cross-linking can be related with squid physiological requirements. Hydroxylysyl-pyridinoline (HP) occurrence and chemical characteristics of collagen from jumbo squid tissues were investigated. Muscle collagen (MC) was higher in Glu, Arg and Gly, but lower in hydrophobic amino acids compared with skin collagen (SC). Lys hydroxylation (%) was higher (P<0.05) in MC (46.9±4.01) than SC (23.4±1.70). Carbohydrate content (% dry wt.) was similar (P≥0.05) among MC (16.6±0.53) and SC (15.2±1.12), showing arabinose (MC, 11.1±0.21 vs. SC, 11.7±0.91), glucose (MC, 3.3±0.10 vs. SC, 2.8±0.10, P<0.05) and xylose (MC, 0.9±0.10 vs. SC, 0.7±0.11, P<0.05); mannose (1.1±0.11) and galactose (0.2±0.01) were found only in MC. FT-IR analysis suggests major supra-organizational rearrangement in MC than SC, through presence of more stable triple-helix structures associated to Gly, Hyl, polar amino acids and carbohydrate contents. HP chemical nature and its tissue-specific distribution (MC, 4.6mmol/mol collagen) indicate that specific Lys hydroxylation can be a critical regulatory step on cross-link formation. Chemical composition variations and HP distribution suggest squid collagens have quite different biomechanical requirements, i.e., muscle or skin collagen rigidity or elasticity.