Thermal inactivation kinetics of proteases and polyphenoloxidase in brown shrimp (Crangon crangon). (15th April 2016)
- Record Type:
- Journal Article
- Title:
- Thermal inactivation kinetics of proteases and polyphenoloxidase in brown shrimp (Crangon crangon). (15th April 2016)
- Main Title:
- Thermal inactivation kinetics of proteases and polyphenoloxidase in brown shrimp (Crangon crangon)
- Authors:
- Verhaeghe, Thomas
Vlaemynck, Geertrui
De Block, Jan
Van Weyenberg, Stephanie
Hendrickx, Marc - Abstract:
- Highlights: Thermal inactivation kinetics of proteases and polyphenoloxidase were determined. Kinetic parameters were estimated using a one-step non-linear regression. Proteases showed two distinct stability fractions, polyphenoloxidase only one. Proteases should be used as a target in further process optimization. Abstract: To optimize product quality of the cooked brown shrimp ( Crangon crangon ), quantitative data on the influence of all relevant process parameters (treatment time and temperature) on several quality attributes is required. Surprisingly, kinetic data and models on heat induced inactivation of important endogenous spoilage enzymes of the brown shrimp are not available today. In this study the thermal inactivation kinetics of the most important spoilage enzymes, proteases and polyphenoloxidase (PPO), were determined from isothermal heat treatments of enzyme extracts of the cephalothorax. For both enzymes, inactivation kinetics showed first order decay(s). Proteases showed two distinct stability fractions. A labile fraction, representing 42 ± 2% of the total activity with kl, 60 °C = 0.94 ± 0.14 min −1 and Ea, l = 178 ± 8.5 kJ/mol, and a stable fraction, representing 58 ± 2%, with ks, 60 °C = 0.020 ± 0.002 min −1 and Ea, s = 155 ± 7.0 kJ/mol. PPO showed a single fraction with k 60 °C = 1.58 ± 0.02 min −1 and Ea = 161 ± 2.2 kJ/mol. Based on these results, the proteolytic activity, in particular the thermostable fraction, should be considered as a targetHighlights: Thermal inactivation kinetics of proteases and polyphenoloxidase were determined. Kinetic parameters were estimated using a one-step non-linear regression. Proteases showed two distinct stability fractions, polyphenoloxidase only one. Proteases should be used as a target in further process optimization. Abstract: To optimize product quality of the cooked brown shrimp ( Crangon crangon ), quantitative data on the influence of all relevant process parameters (treatment time and temperature) on several quality attributes is required. Surprisingly, kinetic data and models on heat induced inactivation of important endogenous spoilage enzymes of the brown shrimp are not available today. In this study the thermal inactivation kinetics of the most important spoilage enzymes, proteases and polyphenoloxidase (PPO), were determined from isothermal heat treatments of enzyme extracts of the cephalothorax. For both enzymes, inactivation kinetics showed first order decay(s). Proteases showed two distinct stability fractions. A labile fraction, representing 42 ± 2% of the total activity with kl, 60 °C = 0.94 ± 0.14 min −1 and Ea, l = 178 ± 8.5 kJ/mol, and a stable fraction, representing 58 ± 2%, with ks, 60 °C = 0.020 ± 0.002 min −1 and Ea, s = 155 ± 7.0 kJ/mol. PPO showed a single fraction with k 60 °C = 1.58 ± 0.02 min −1 and Ea = 161 ± 2.2 kJ/mol. Based on these results, the proteolytic activity, in particular the thermostable fraction, should be considered as a target in thermal processing of brown shrimp in relation to enzyme induced product quality changes during storage. … (more)
- Is Part Of:
- Food chemistry. Volume 197:Part A(2016)
- Journal:
- Food chemistry
- Issue:
- Volume 197:Part A(2016)
- Issue Display:
- Volume 197, Issue 2016 (2016)
- Year:
- 2016
- Volume:
- 197
- Issue:
- 2016
- Issue Sort Value:
- 2016-0197-2016-0000
- Page Start:
- 641
- Page End:
- 647
- Publication Date:
- 2016-04-15
- Subjects:
- Crangon crangon -- Polyphenoloxidase -- Proteases -- Thermal stability -- Kinetics
Food -- Analysis -- Periodicals
Food -- Composition -- Periodicals
664 - Journal URLs:
- http://www.sciencedirect.com/science/journal/03088146 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.foodchem.2015.11.024 ↗
- Languages:
- English
- ISSNs:
- 0308-8146
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.284000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 585.xml