TY - JOUR
T1 - Physicochemical and Structural Properties of Recovered Elastin from Jumbo Squid (Dosidicus gigas) By-Products
AU - Ramírez-Guerra, Hugo E.
AU - Márquez-Ríos, Enrique
AU - Suárez-Jiménez, Guadalupe M.
AU - Rouzaud-Sández, Ofelia
AU - Lugo-Sánchez, María E.
AU - Ramírez-Suárez, Juan C.
AU - Torres-Arreola, Wilfrido
N1 - Publisher Copyright:
© 2019, © 2019 Taylor & Francis Group, LLC.
PY - 2019/3/16
Y1 - 2019/3/16
N2 - Physicochemical and structural properties of soluble jumbo squid (Dosidicus gigas) elastin recovered from skin by-products were evaluated. The molecular weight of isolated elastin was ~40 kDa with an isoelectric point (pI) between 9 and 10. Aspartic, glutamic, arginine, proline, glycine, and lysine amino acids were the most abundant in squid elastin, whereas the hydroxyproline absence, ~0.7% cysteine content, and the calculated 0.35 isoleucine/leucine ratio were used as purity index. Total and reactive sulfhydryl contents were similar (247.0 ± 5.1 vs 242.0 ± 7.5 μmol mg−1 of protein, P ≥ 0.05) in purified squid elastin but surprisingly higher than previously reported in other elastins. On the other hand, the secondary structures of squid elastin analyzed by Fourier transform infrared spectroscopy (FTIR) were ~45% β-sheets, ~15% α-helices, ~10% β-turns, and ~30% undefined structures. In addition, squid elastin experienced glass transition at 82.01 ± 0.01ºC, denaturation temperature at 110.45 ± 0.64ºC, and aggregation at 197.5 ± 0.23ºC. In conclusion, the prevalence of charged amino acids and pI of squid elastin can facilitate its solubilization in hydrophilic systems, whereas the secondary structure profile and thermostability are desirable features in proteins used for biopolymer designs such as food biofilms or barrier systems.
AB - Physicochemical and structural properties of soluble jumbo squid (Dosidicus gigas) elastin recovered from skin by-products were evaluated. The molecular weight of isolated elastin was ~40 kDa with an isoelectric point (pI) between 9 and 10. Aspartic, glutamic, arginine, proline, glycine, and lysine amino acids were the most abundant in squid elastin, whereas the hydroxyproline absence, ~0.7% cysteine content, and the calculated 0.35 isoleucine/leucine ratio were used as purity index. Total and reactive sulfhydryl contents were similar (247.0 ± 5.1 vs 242.0 ± 7.5 μmol mg−1 of protein, P ≥ 0.05) in purified squid elastin but surprisingly higher than previously reported in other elastins. On the other hand, the secondary structures of squid elastin analyzed by Fourier transform infrared spectroscopy (FTIR) were ~45% β-sheets, ~15% α-helices, ~10% β-turns, and ~30% undefined structures. In addition, squid elastin experienced glass transition at 82.01 ± 0.01ºC, denaturation temperature at 110.45 ± 0.64ºC, and aggregation at 197.5 ± 0.23ºC. In conclusion, the prevalence of charged amino acids and pI of squid elastin can facilitate its solubilization in hydrophilic systems, whereas the secondary structure profile and thermostability are desirable features in proteins used for biopolymer designs such as food biofilms or barrier systems.
KW - Jumbo squid
KW - OFFGELelectrophoresis
KW - by-products
KW - elastin
KW - physicochemical characterization
UR - http://www.mendeley.com/research/physicochemical-structural-properties-recovered-elastin-jumbo-squid-dosidicus-gigas-byproducts
U2 - 10.1080/10498850.2019.1577932
DO - 10.1080/10498850.2019.1577932
M3 - Artículo
SN - 1049-8850
VL - 28
SP - 275
EP - 286
JO - Journal of Aquatic Food Product Technology
JF - Journal of Aquatic Food Product Technology
IS - 3
ER -