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Jose de Jesus Encinas-Arzate,Josafat Marina Ezquerra-Brauer,Victor Manuel Ocaño-Higuera,Benjamin Ramirez-Wong,Lorena Armenta-Villegas,Wilfrido Torres-Arreaola,Enrique Marquez-Rios 한국식품과학회 2014 Food Science and Biotechnology Vol.23 No.2
Myofibrillar protein are the principally responsibleof gelling properties in fishery resource, hence, during proteinconcentrate or isolated proteins preparation, sarcoplasmicprotein are discarded; however, myofibrillar protein cansupport low levels of sarcoplasmic proteins without affectingthe gelling property. Therefore, the aim of this study was togradually remove sarcoplasmic proteins from giant squidmantle by means of different ionic strengths (I). Solutionsof NaCl with different ionic strengths (I=0.0, 0.1, and 0.3)were used to obtain 3 protein concentrates. The electrophoreticprofile in SDS-PAGE showed differences in protein removalwith a high solubility of mantle proteins. The texture profileanalysis showed that hardness increased in mantle proteinwashed with higher I. The total reactive sulfhydryls showedsignificant changes (p<0.05) detecting major formation ofS-S bonds with protein removal at an I of 0.3. Differentialscanning calorimetry showed a minor denaturation temperatureof the actomyosin complex when protein removal wasperformed with an I of 0.3. The present study indicates thatremoval of sarcoplasmic protein as a function of I results inbetter quality gels.