Proteomes 2024, 12(4), 36; https://doi.org/10.3390/proteomes12040036 - 27 Nov 2024
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Sous vide, a cooking method that involves vacuum-sealed fish at low temperatures, yields a uniquely tender, easily flaked texture. Previous research on sous-vide tenderization has focused on thermal protein denaturation. On the other hand, the contribution of proteases, activated at low temperatures in
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Sous vide, a cooking method that involves vacuum-sealed fish at low temperatures, yields a uniquely tender, easily flaked texture. Previous research on sous-vide tenderization has focused on thermal protein denaturation. On the other hand, the contribution of proteases, activated at low temperatures in fish meat, has been suggested. However, the details of protein degradation remain unclear. This study employed SDS-PAGE/immunoblot and peptidomic analysis of rainbow trout to assess proteolysis during sous-vide cooking. The results from SDS-PAGE and immunoblot analysis indicated reduced thermal aggregation of sarcoplasmic proteins and increased depolymerization of actin under low-temperature cooking conditions. A comparison of the peptidome showed that the proteolysis of myofibrillar proteins was accelerated during sous-vide cooking, with distinct proteases potentially activated at different cooking temperatures. Terminome analysis revealed the contribution of specific proteases at higher temperatures in rainbow trout. The results of this study demonstrate the thermal denaturation of sarcoplasmic proteins and proteolysis of myofibrillar proteins in rainbow trout meat during sous-vide cooking and its temperature dependence. The methodology in the present study could provide insights into the optimization of cooking conditions for different fish species, potentially leading to improved texture and quality of sous-vide products.
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Figure 1
Figure 1
<p>Comparison of TPA parameters in raw and sous-vide-cooked rainbow trout meat: hardness (<b>a</b>); cohesiveness (<b>b</b>); springiness (<b>c</b>); and resilience (<b>d</b>) (* <span class="html-italic">p</span> < 0.05, ** <span class="html-italic">p</span> < 0.01, Dunnett test vs. raw, <span class="html-italic">n</span> = 3).</p> Full article ">Figure 2
<p>SDS-PAGE separation (<b>a</b>) and immunoreactive proteins (<b>b</b>). Separation of proteins extracted from raw and sous-vide-cooked rainbow trout meat with a low ionic strength buffer. Lane 1, raw; lane 2, SV-52; lane 3, SV-65; and lane 4, SV-80.</p> Full article ">Figure 3
<p>Quantification of the degraded muscle proteins related to meat texture in the rainbow trout meat. The data bar indicates the amount of each degraded protein.</p> Full article ">Figure 4
<p>Sequence specificity in the terminome of the rainbow trout: raw (<b>a</b>); SV-52 (<b>b</b>); SV-65 (<b>c</b>); and SV-80 (<b>d</b>). Each column corresponds to the P2−P2′ subsite.</p> Full article ">
<p>Comparison of TPA parameters in raw and sous-vide-cooked rainbow trout meat: hardness (<b>a</b>); cohesiveness (<b>b</b>); springiness (<b>c</b>); and resilience (<b>d</b>) (* <span class="html-italic">p</span> < 0.05, ** <span class="html-italic">p</span> < 0.01, Dunnett test vs. raw, <span class="html-italic">n</span> = 3).</p> Full article ">Figure 2
<p>SDS-PAGE separation (<b>a</b>) and immunoreactive proteins (<b>b</b>). Separation of proteins extracted from raw and sous-vide-cooked rainbow trout meat with a low ionic strength buffer. Lane 1, raw; lane 2, SV-52; lane 3, SV-65; and lane 4, SV-80.</p> Full article ">Figure 3
<p>Quantification of the degraded muscle proteins related to meat texture in the rainbow trout meat. The data bar indicates the amount of each degraded protein.</p> Full article ">Figure 4
<p>Sequence specificity in the terminome of the rainbow trout: raw (<b>a</b>); SV-52 (<b>b</b>); SV-65 (<b>c</b>); and SV-80 (<b>d</b>). Each column corresponds to the P2−P2′ subsite.</p> Full article ">
