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Submitted on 12 Nov 2019
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Protein Thermal Denaturation of Beef Muscle: Neutron
Imaging and spectroscopies
Simone Scussat, Elias Bou-Maroun, Christine Fant, Philippe Cayot, Camille
Loupiac
To cite this version:
Simone Scussat, Elias Bou-Maroun, Christine Fant, Philippe Cayot, Camille Loupiac. Protein Thermal Denaturation of Beef Muscle: Neutron Imaging and spectroscopies. Neutrons and food, Jul 2014, Paris, France. �hal-02359464�
P r o t e i n T h e r m a l D e n a t u r a t i o n o f B e e f M u s c l e :
N e u t r o n I m a g i n g a n d S p e c t r o s c o p i e s
Scussat S.1,2, Bou-Maroun E.1, Fant C.3, Cayot P.1, Loupiac C.1,2
1 Équipe PAPC, UMR PAM, Université de Bourgogne – AgroSup Dijon, Dijon, France. 2 Laboratoire Léon Brillouin, CEA – CNRS, CEA Saclay, Gif-sur-Yvette, France.
3 Groupe EMN 3A, AgroSup Dijon, Dijon, France.
Context of Project
Open Food System is an academic and industrial projet with the purpose to follow meat cooking without any intrusion. It concerns two main parts 2) Biochemistry of Muscle Cooking
Our Approach:
Microscopic scale (Neutron Imaging)
Molecular scale (Spectroscopies) 1) Sensor Development
a) Spectroscopic Sensor • Visible / InfraRed
• Fluorescence b) Olfactometer Sensor Food Science Approach:Macroscopic scale
Sensory Analysis • Colour • Texture • Flavour
Neutron Imaging during Cooking
0.0 0.1 0.2 0.3 0.4 0.5 0.6 0.7 0.8 0.9 1.0 In te nsi ty (-) Temperature (°C) p1 p2 p3 p4 p5 p6 p7 p8 27.5 61.5 70 75.5 81 82.5 84.5 90 99
Main changes of attenuation coefficient
take place at the edge of the sample
Optical Image of Muscle
Raw Sample
Thickness: 2 mm Attenuation Coefficient vs Temperature
Superposition of Contour Plots on Neutron Images
Neutron Imaging was used to follow muscle morphology changes (protein contraction) and
juice migration inside the sample (through the evolution of Attenuation Coefficient)
Pixel (px) Pix el (p x) Raw Sample 1 mm Pix el (p x) Pixel (px) Cooked Sample at 100 °C 1 mm
Spectroscopies: IR and Fluorescence
InfraRed and Fluorescence were carried out on muscle samples with the purpose to detect
the spectroscopic signature of proteins at a particular cooking degree
Principal Component Analysis - InfraRed
Separation on Cooking Degree: • Beef: LT MT and HT
Principal Component Analysis - Fluorescence
Separation on Cooking Degree: • Beef: LT MT and HT 4000 3500 3000 2500 2000 1500 1000 84 86 88 90 92 94 96 98 100 Transmitta nce (%) Wavenumber (cm-1) Low Temperature Medium Temperature High Temperature 300 325 350 375 400 425 450 0 250 500 750 1000 1250 1500 1750 2000 2250 In te nsi ty ( -) Wavelength (nm) Low Temperature Medium Temperature High Temperature Calorimetry
Used to determine the cooking temperature parameters for the samples
25 3035 40 45 50 55 6065 70 75 80 8590 95100 -13.0 -12.8 -12.6 -12.4 -12.2 -12.0 -11.8 -11.6 -11.4 -11.2 -11.0
Raw Roast Beef
He at F lo w (m W ) Temperature (°C)
InfraRed Spectra Fluorescence Spectra (ex. 291 nm)
HT (High Temperature) MT (Medium Temperature) LT (Low Temperature)
Future
Acknowledgement:Open Food System is a research project supported by Vitagora, Cap Digital, Imaginove, Aquimer, Microtechnique and Agrimip, financed by the French State and the Franche-Comté Region as part of The Investments for the Future Programme managed by Bpifrance.
www.openfoodsystem.fr References:Chien et al., 322 (5907), 1494-1497 (Science)
Microscopic Scale on Neutron Imaging:
• Coupling Neutron Imaging with Surface Spectroscopies (IR and Fluorescence) during heating Process
Molecular Scale:
• Myosin Thermal Denaturation depending on ionic strength (KCl)
• Structural Studies by IR, Fluorescence and SANS spectroscopy [ ] KCl > 300 mM
[ ] KCl 100-200 mM [ ] KCl < 50 mM
Fluorescence Detector Visible /InfraRed Detector
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