Proteomic and microscopic approaches in understanding mechanisms of shell-loosening of shrimp (Pandalus borealis) induced by high pressure and protease
Research output: Contribution to journal › Journal article › Research › peer-review
Standard
Proteomic and microscopic approaches in understanding mechanisms of shell-loosening of shrimp (Pandalus borealis) induced by high pressure and protease. / Dang, Tem Thi; Jessen, Flemming; Martens, Helle Juel; Gringer, Nina; Olsen, Karsten; Bøknæs, Niels; Orlien, Vibeke.
In: Food Chemistry, Vol. 289, 2019, p. 729-738.Research output: Contribution to journal › Journal article › Research › peer-review
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - JOUR
T1 - Proteomic and microscopic approaches in understanding mechanisms of shell-loosening of shrimp (Pandalus borealis) induced by high pressure and protease
AU - Dang, Tem Thi
AU - Jessen, Flemming
AU - Martens, Helle Juel
AU - Gringer, Nina
AU - Olsen, Karsten
AU - Bøknæs, Niels
AU - Orlien, Vibeke
PY - 2019
Y1 - 2019
N2 - 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.
AB - 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.
KW - 2D gel electrophoresis
KW - Microscopy
KW - Peeling
KW - Protein
KW - Shell loosening
KW - Shrimp
U2 - 10.1016/j.foodchem.2019.03.059
DO - 10.1016/j.foodchem.2019.03.059
M3 - Journal article
C2 - 30955673
AN - SCOPUS:85063326081
VL - 289
SP - 729
EP - 738
JO - Food Chemistry
JF - Food Chemistry
SN - 0308-8146
ER -
ID: 216249418