TY - JOUR
T1 - Effect of ionic strength on soluble protein removal from giant squid mantle (Dosidicus gigas) and functional evaluation of protein recovery
AU - Encinas-Arzate, Jose de Jesus
AU - Ezquerra-Brauer, Josafat Marina
AU - Ocaño-Higuera, Victor Manuel
AU - Ramirez-Wong, Benjamin
AU - Armenta-Villegas, Lorena
AU - Torres-Arreaola, Wilfrido
AU - Marquez-Rios, Enrique
PY - 2014/1/1
Y1 - 2014/1/1
N2 - Myofibrillar protein are the principally responsible of gelling properties in fishery resource, hence, during protein concentrate or isolated proteins preparation, sarcoplasmic protein are discarded; however, myofibrillar protein can support low levels of sarcoplasmic proteins without affecting the gelling property. Therefore, the aim of this study was to gradually remove sarcoplasmic proteins from giant squid mantle by means of different ionic strengths (I). Solutions of NaCl with different ionic strengths (I=0.0, 0.1, and 0.3) were used to obtain 3 protein concentrates. The electrophoretic profile in SDS-PAGE showed differences in protein removal with a high solubility of mantle proteins. The texture profile analysis showed that hardness increased in mantle protein washed with higher I. The total reactive sulfhydryls showed significant changes (p<0.05) detecting major formation of S-S bonds with protein removal at an I of 0.3. Differential scanning calorimetry showed a minor denaturation temperature of the actomyosin complex when protein removal was performed with an I of 0.3. The present study indicates that removal of sarcoplasmic protein as a function of I results in better quality gels. © 2014 The Korean Society of Food Science and Technology and Springer Science+Business Media Dordrecht.
AB - Myofibrillar protein are the principally responsible of gelling properties in fishery resource, hence, during protein concentrate or isolated proteins preparation, sarcoplasmic protein are discarded; however, myofibrillar protein can support low levels of sarcoplasmic proteins without affecting the gelling property. Therefore, the aim of this study was to gradually remove sarcoplasmic proteins from giant squid mantle by means of different ionic strengths (I). Solutions of NaCl with different ionic strengths (I=0.0, 0.1, and 0.3) were used to obtain 3 protein concentrates. The electrophoretic profile in SDS-PAGE showed differences in protein removal with a high solubility of mantle proteins. The texture profile analysis showed that hardness increased in mantle protein washed with higher I. The total reactive sulfhydryls showed significant changes (p<0.05) detecting major formation of S-S bonds with protein removal at an I of 0.3. Differential scanning calorimetry showed a minor denaturation temperature of the actomyosin complex when protein removal was performed with an I of 0.3. The present study indicates that removal of sarcoplasmic protein as a function of I results in better quality gels. © 2014 The Korean Society of Food Science and Technology and Springer Science+Business Media Dordrecht.
U2 - 10.1007/s10068-014-0055-y
DO - 10.1007/s10068-014-0055-y
M3 - Article
SP - 401
EP - 407
JO - Food Science and Biotechnology
JF - Food Science and Biotechnology
SN - 1226-7708
ER -