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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.
Enrique Marquez-Rios,Octavio Cota-Arriola,Ana Gloria Villalba-Villalba,Josafat Marina Ezquerra-Brauer,Victor Manuel Ocaño-Higuera,Betzabe Ebenhezer Lopez-Corona,Wilfrido Torres-Arreola 한국식품과학회 2016 Food Science and Biotechnology Vol.25 No.4
Chymotrypsin was purified from jumbo squid hepatopancreas (HP) with 2.4-fold and yield1.9%, and characterized with a molecular weight of 31 kDa, as estimated by sodium dodecyl sulfatepolyacrylamidegel electrophoresis (SDS-PAGE). Chymotrypsin effect over collagen extracted from themantle, fins and arms of the jumbo squid was evaluated. The enzyme exhibited the maximum activityat pH 7 and 65oC using Suc-Ala-Ala-Pro-Phe-p-nitroanilide (SAAPNA) as a substrate and it was identifiedusing the specific inhibitors N-tosyl-L-phenylalaninechloromethyl ketone (TPCK) and phenyl methylsulfonyl fluoride (PMSF), showing residual activities of 6% and 0%, respectively. Furthermore, highactivity was observed in the pH range of 4.0 to 8.0. Purified enzyme showed a moderate in vitro activityusing muscle collagen as a substrate. Although further research is needed, the results suggest that theenzyme has a potential application where acidic or slightly alkaline conditions are needed.