Proteomic and microscopic approaches in understanding mechanisms of shell-loosening of shrimp (Pandalus borealis) induced by high pressure and protease
Shell-loosening is of importance in facilitating shrimp peeling. In this study, enzyme and high pressure (HP) improved the shell-loosening at different degrees, which were observed as gaps by microscopy. The shell-loosening gap induced by an endoprotease with broad specificity (Endocut-03L, 53 μm) w...
| Published in: | Food Chemistry |
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| Main Authors: | , , , , , , |
| Format: | Article in Journal/Newspaper |
| Language: | English |
| Published: |
2019
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| Subjects: | |
| Online Access: | https://orbit.dtu.dk/en/publications/80fe46f8-a025-4da8-9a4f-246291208c76 https://doi.org/10.1016/j.foodchem.2019.03.059 https://backend.orbit.dtu.dk/ws/files/219905583/Pages_from_FOODCHEM_S_18_06815.pdf |
| Summary: | Shell-loosening is of importance in facilitating shrimp peeling. In this study, enzyme and high pressure (HP) improved the shell-loosening at different degrees, which were observed as gaps by microscopy. The shell-loosening gap induced by an endoprotease with broad specificity (Endocut-03L, 53 μm) was much higher than that induced by HP at 100 MPa (HP100, 12 μm), followed by an endoprotease with high specificity (Tail21, 8 μm), and HP at 600 MPa (HP600, 5 μm). The degree of shell-loosening was found to be correlated to the extent of protein changes that were obtained by 2D gel electrophoresis. Shell-loosening due to HP100 and Endocut-03L was mainly caused by physical and enzymatic degradation of high molecular-weight proteins in shell and epidermis and subsequent loss of degradation products, disrupting the structure of muscle-shell connection. However, HP100 was less effective than Endocut-03L due to its stabilizing effect on the shell collagen, lowering its shell-loosening effect. |
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