-"Surimi" itself is not a food; it is an intermediate phase of the production of "kamaboko"(a gel formed by the addition of salt to the surimi and direct heating to 80-90ºC) and a series of high-priced shellfish analogs. The protective effect that two cryoprotectant mixtures exerted during freezing and frozen storage of frozen surimi of surubí (Pseudoplatystoma coruscans) on the functional quality of the gels prepared was studied. The selected washing conditions selected to obtain an acceptable functional quality of gels prepared from frozen surimi (25% extracted proteins and of final moisture) using the response surface methodology were wash temperature, 18ºC; washing time for each of the three washing cycles, 4.62 min. and water-mince ratio, 3.5:1. Cryoprotectant mixtures used were sucrose/sorbitol (1:1) and maltodextrin/sorbitol (1:1) and they were added (8%) to the washed and drained minced fish before freezing. To evaluate the functionality of the frozen surimi during six months of storage, the penetration test to measure the gel strength was chosen; samples were assessed at 4, 45, 90 and 180 days of frozen storage. Results showed that even with the cryoprotectants freezing decreased gel strength, since it produced a decrease of almost 32% in the strength of the gel prepared with fresh surimi. However, the two cryoprotectant mixtures tested showed very good behaviour throughout frozen storage; specially at 45 and 90 days of storage the surimi gels with the sucrose/sorbitol mixture had a greater resistance than those with maltodextrin/sorbitol. Keywords: gel strength, frozen storage of surimi, protein functionality, surubí surimi and cryoprotectant.
A combination of molecular sieving chromatography and 2-step preparative isoelectric focusing showed that native Fh12, a fatty acid-binding protein isolated from Fasciola hepatica adult worms, is a protein complex of at least 8 isoforms with identical molecular mass but different isoelectric points. Using enzyme-linked immunosorbent assay (ELISA) and inhibition ELISA assays, immunological differences were observed between native (nFh12) and a recombinant molecule denoted rFh15 that was obtained after screening a cDNA library from F. hepatica adult worms with an anti-Fh12 monospecific polyclonal antibody. It was confirmed that in infected rabbits, antibodies to nFh12 appear by the second week postinfection, whereas antibodies to rFh15 appear much later, by 6 wk postinfection. Four acidic forms (Fh12(1-4)) showed more immunological identity with rFh15 than with nFh12, based on the observation that they inhibited ELISA activity by nearly 50% when they were added to the anti-rFh15 polyclonal antibody at 20 microg/ml of protein concentration. Moreover, the Fh12(1-4) isoforms were poorly reactive with sera from rabbits 2-4 wk postinfection. However, the 2 acidic forms, denoted Fh12(5) and Fh12(6), and the neutral/basic forms, denoted Fh12(7) and Fh12(8), showed more immunological identity with the native nFh12 molecule than with the recombinant rFh15 because they were highly reactive with sera of rabbits with early 2-wk F. hepatica infection and inhibited ELISA activity nearly 50% when they were quantitatively added to the anti-nFh12 polyclonal antibody. These results suggest that rFh15 could be one of the acidic forms of nFh12, and that it, in fact, may be one of the less immunogenic or immunoprotective members, or both, of the nFh12 protein complex.
The effect of process temperature (2 to 18 °C), time (1 to 7 min/cycle), and water-mince ratio (2:1 to 8:1) on the quality attributes of surubí (Pseudoplatystoma coruscans) surimi was studied using Response Surface Methodology (RSM). Conditions were identified that allowed to achieve 25% of extracted proteins and a moisture content of 79%, compatible with an acceptable quality of surimi gel. The verification of the prediction models was acceptable. Two cryoprotectant mixtures (sucrose-sorbitol and maltodextrin-sorbitol) were also evaluated, with regard to the freezing and frozen storage and the functional quality of the gels. Freezing proved to be an aggressive method, and the 2 mixtures tested showed to be efficient for 6 months of frozen storage.
A combination of molecular sieving chromatography and 2-step preparative isoelectric focusing showed that native Fh12, a fatty acid-binding protein isolated from Fasciola hepatica adult worms, is a protein complex of at least 8 isoforms with identical molecular mass but different isoelectric points. Using enzyme-linked immunosorbent assay (ELISA) and inhibition ELISA assays, immunological differences were observed between native (nFh12) and a recombinant molecule denoted rFh15 that was obtained after screening a cDNA library from F. hepatica adult worms with an anti-Fh12 monospecific polyclonal antibody. It was confirmed that in infected rabbits, antibodies to nFh12 appear by the second week postinfection, whereas antibodies to rFh15 appear much later, by 6 wk postinfection. Four acidic forms (Fh12(1-4)) showed more immunological identity with rFh15 than with nFh12, based on the observation that they inhibited ELISA activity by nearly 50% when they were added to the anti-rFh15 polyclonal antibody at 20 microg/ml of protein concentration. Moreover, the Fh12(1-4) isoforms were poorly reactive with sera from rabbits 2-4 wk postinfection. However, the 2 acidic forms, denoted Fh12(5) and Fh12(6), and the neutral/basic forms, denoted Fh12(7) and Fh12(8), showed more immunological identity with the native nFh12 molecule than with the recombinant rFh15 because they were highly reactive with sera of rabbits with early 2-wk F. hepatica infection and inhibited ELISA activity nearly 50% when they were quantitatively added to the anti-nFh12 polyclonal antibody. These results suggest that rFh15 could be one of the acidic forms of nFh12, and that it, in fact, may be one of the less immunogenic or immunoprotective members, or both, of the nFh12 protein complex.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
hi@scite.ai
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.