Proteomic and microscopic approaches in understanding mechanisms of shell-loosening of shrimp (Pandalus borealis) induced by high pressure and protease
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- Proteomic and microscopic approaches in understanding mechanisms of shellloosening of shrimp (Pandalus borealis) induced by high pressure and protease
Accepted author manuscript, 1.69 MB, PDF document
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.
Original language | English |
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Journal | Food Chemistry |
Volume | 289 |
Pages (from-to) | 729-738 |
Number of pages | 10 |
ISSN | 0308-8146 |
DOIs | |
Publication status | Published - 2019 |
- 2D gel electrophoresis, Microscopy, Peeling, Protein, Shell loosening, Shrimp
Research areas
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