Proteomic and microscopic approaches in understanding mechanisms of shell-loosening of shrimp (Pandalus borealis) induced by high pressure and protease

• Published in: Food Chemistry
• Main Authors: Dang, Tem Thi, Jessen, Flemming, Martens, Helle Juel, Gringer, Nina, Olsen, Karsten, Bøknæs, Niels, Orlien, Vibeke
• Format: Article in Journal/Newspaper
• Language: English
• Published: 2019
• Subjects: 2D gel electrophoresis; Microscopy; Peeling; Protein; Shell loosening; Shrimp; Pandalus borealis
• 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

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.