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

Tem Thi Dang, Flemming Jessen, Helle Juel Martens, Nina Gringer, Karsten Olsen, Niels Bøknæs, Vibeke Orlien*

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

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 languageEnglish
JournalFood Chemistry
Volume289
Pages (from-to)729-738
ISSN0308-8146
DOIs
Publication statusPublished - 2019

Keywords

  • 2D gel electrophoresis
  • Microscopy
  • Peeling
  • Protein
  • Shell loosening
  • Shrimp

Cite this

@article{80fe46f8a0254da89a4f246291208c76,
title = "Proteomic and microscopic approaches in understanding mechanisms of shell-loosening of shrimp (Pandalus borealis) induced by high pressure and protease",
abstract = "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.",
keywords = "2D gel electrophoresis, Microscopy, Peeling, Protein, Shell loosening, Shrimp",
author = "Dang, {Tem Thi} and Flemming Jessen and Martens, {Helle Juel} and Nina Gringer and Karsten Olsen and Niels B{\o}kn{\ae}s and Vibeke Orlien",
year = "2019",
doi = "10.1016/j.foodchem.2019.03.059",
language = "English",
volume = "289",
pages = "729--738",
journal = "Food Chemistry",
issn = "0308-8146",
publisher = "Elsevier",

}

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 journalJournal articleResearchpeer-review

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

VL - 289

SP - 729

EP - 738

JO - Food Chemistry

JF - Food Chemistry

SN - 0308-8146

ER -