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  1. Artikel: Transformation of highly marbled meats under various cooking processes

    Anne, Duconseille / Thierry, Astruc / Keisuke, Sasaki / Michiyo, Motoyama

    Meat science. 2022 Mar. 21,

    2022  

    Abstract: Cooking induces modifications in meat structure and composition, affecting its sensory and nutritional properties. These changes depend on the cooking method and meat characteristics. In the present study, beef were cooked in three different ways— ... ...

    Abstract Cooking induces modifications in meat structure and composition, affecting its sensory and nutritional properties. These changes depend on the cooking method and meat characteristics. In the present study, beef were cooked in three different ways—grilling, boiling, and sous-vide cooking—with two endpoint temperatures, 55 °C and 77 °C, to better understand the general impact of cooking on the structure of fatty meat. Light microscopy was used to visualize muscle, connective, and adipose tissues. After cooking, muscle fibers were more compact, which can be attributed to perimysium shrinkage and water transfer, for all cooking processes except grilling at 55 °C. The cross-sectional area of muscle fibers was not impacted by cooking, regardless of the temperature or cooking method. Connective tissue between adipocytes was affected by cooking at 77 °C, but not at 55 °C. Despite the cooking method used, cooking to well-done (77 °C) clearly affected the structure of the perimysium of beef, possibly because of collagen denaturation.
    Schlagwörter adipocytes ; beef ; collagen ; denaturation ; light microscopy ; meat science ; muscles ; shrinkage ; sous vide ; temperature
    Sprache Englisch
    Erscheinungsverlauf 2022-0321
    Erscheinungsort Elsevier Ltd
    Dokumenttyp Artikel
    Anmerkung Pre-press version
    ZDB-ID 753319-6
    ISSN 1873-4138 ; 0309-1740
    ISSN (online) 1873-4138
    ISSN 0309-1740
    DOI 10.1016/j.meatsci.2022.108810
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  2. Artikel ; Online: Transformation of highly marbled meats under various cooking processes.

    Anne, Duconseille / Thierry, Astruc / Keisuke, Sasaki / Michiyo, Motoyama

    Meat science

    2022  Band 189, Seite(n) 108810

    Abstract: Cooking induces modifications in meat structure and composition, affecting its sensory and nutritional properties. These changes depend on the cooking method and meat characteristics. In the present study, beef were cooked in three different ways- ... ...

    Abstract Cooking induces modifications in meat structure and composition, affecting its sensory and nutritional properties. These changes depend on the cooking method and meat characteristics. In the present study, beef were cooked in three different ways-grilling, boiling, and sous-vide cooking-with two endpoint temperatures, 55 °C and 77 °C, to better understand the general impact of cooking on the structure of fatty meat. Light microscopy was used to visualize muscle, connective, and adipose tissues. After cooking, muscle fibers were more compact, which can be attributed to perimysium shrinkage and water transfer, for all cooking processes except grilling at 55 °C. The cross-sectional area of muscle fibers was not impacted by cooking, regardless of the temperature or cooking method. Connective tissue between adipocytes was affected by cooking at 77 °C, but not at 55 °C. Despite the cooking method used, cooking to well-done (77 °C) clearly affected the structure of the perimysium of beef, possibly because of collagen denaturation.
    Mesh-Begriff(e) Animals ; Cattle ; Meat/analysis ; Cooking/methods ; Muscle, Skeletal ; Temperature ; Connective Tissue
    Sprache Englisch
    Erscheinungsdatum 2022-03-24
    Erscheinungsland England
    Dokumenttyp Journal Article
    ZDB-ID 753319-6
    ISSN 1873-4138 ; 0309-1740
    ISSN (online) 1873-4138
    ISSN 0309-1740
    DOI 10.1016/j.meatsci.2022.108810
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel ; Online: Preferred metabolic pathway of bovine muscle fibre revealed by synchrotron–deep ultraviolet fluorescence imaging

    Thierry Astruc / Olivier Loison / Frédéric Jamme / Matthieu Réfrégiers / Annie Vénien

    Journal of Spectral Imaging, Vol 8, Iss 1, p a

    2019  Band 14

    Abstract: The different bovine muscle fibre types I, IIA and IIX are characterised by their preferred metabolic pathway, either oxidative (I, IIA) or glycolytic (IIX), and their contraction speed, either slow-twitch (I) or fast-twitch (IIA, IIX). These ... ...

    Abstract The different bovine muscle fibre types I, IIA and IIX are characterised by their preferred metabolic pathway, either oxidative (I, IIA) or glycolytic (IIX), and their contraction speed, either slow-twitch (I) or fast-twitch (IIA, IIX). These physiological specificities are associated with variations in intracellular composition and their fluorescence spectra signatures. We hypothesised that these slight differences in autofluorescence responses could be used to discriminate the muscle fibre types by fluorescence imaging. Serial histological cross-sections of beef longissimus dorsi were performed: the start set was used to identify the metabolic and contractile type of muscle fibres by both immunohistoenzymology and immunohistofluorescence, and the following set was used to acquire synchrotron–deep ultraviolet (UV) autofluorescence images after excitation in the UV range (275 nm and 315 nm). This strategy made it possible to explore the label-free autofluorescence of muscle cells previously subtyped by histochemistry. Glycolytic cells (IIX) showed more intense fluorescence than oxidative cells (I and IIA) with near-90 % accuracy. This discrimination is more specifically assigned to the fluorescence of nicotinamide adenine dinucleotide. UV autofluorescence was unable to discriminate contractile type.
    Schlagwörter skeletal muscle ; fibre type ; myosin isoform ; UV microspectroscopy ; histology ; synchrotron radiation ; Analytical chemistry ; QD71-142
    Sprache Englisch
    Erscheinungsdatum 2019-07-01T00:00:00Z
    Verlag IM Publications Open
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  4. Artikel ; Online: Effect of dry salt versus brine injection plus dry salt on the physicochemical characteristics of smoked salmon after filleting

    Thierry Astruc / Annie Vénien / Sylvie Clerjon / Raphael Favier / Olivier Loison / Pierre-Sylvain Mirade / Stéphane Portanguen / Jacques Rouel / Mailys Lethiec / Arno Germond

    Heliyon, Vol 8, Iss 11, Pp e11245- (2022)

    2022  

    Abstract: Smoked fish fillets are pre-salted as a food conservation and quality preservation measure. Here we investigated biochemical and sensory aspects of smoked salmon fillets. Left-side salmon fillets were dry-salted while the right-side fillets underwent a ... ...

    Abstract Smoked fish fillets are pre-salted as a food conservation and quality preservation measure. Here we investigated biochemical and sensory aspects of smoked salmon fillets. Left-side salmon fillets were dry-salted while the right-side fillets underwent a mixed salting method consisting of an injection of saturated brine followed by surface application of dry salt. After 6 h of salting, all the fillets were smoked. At each step of the process, quality was evaluated using instrumental measurements (pH, color, texture, water content, salt content, aw), and lipid distribution was visualized by MRI. Mixed-salted fillets had a higher salt content than dry-salted fillets and variability in salt distribution was dependent on the salting process. However, these variations had no effect on pH, color or texture, which showed similar values regardless of salting method. Fatty areas had a lower salt content due to slower diffusion of aqueous salt solutions through them. Mixed salting speeds up the salting of the muscle without significantly affecting the quality traits of the salmon fillet.
    Schlagwörter Salmo salar ; Dry salting ; Brine injection ; NaCl distribution ; Lipid distribution ; Science (General) ; Q1-390 ; Social sciences (General) ; H1-99
    Sprache Englisch
    Erscheinungsdatum 2022-11-01T00:00:00Z
    Verlag Elsevier
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  5. Artikel: Toward the design of functional foods and biobased products by 3D printing: A review

    Portanguen, Stéphane / Pascal Tournayre / Jason Sicard / Thierry Astruc / Pierre-Sylvain Mirade

    Trends in food science & technology. 2019 Apr., v. 86

    2019  

    Abstract: 3D printing or additive manufacturing (AM) now provides enormous freedom to design, manufacture and innovate in various domains, even in foodstuffs development. Given the immense potential applications related to AM, many authors are even talking about a ...

    Abstract 3D printing or additive manufacturing (AM) now provides enormous freedom to design, manufacture and innovate in various domains, even in foodstuffs development. Given the immense potential applications related to AM, many authors are even talking about a new industrial revolution.In this article, we review the state of the science in applied AM methods for developing biobased products in the medical and food sectors, with these two sectors having similar points. We were therefore interested in the technological locks encountered in the various studies carried out on the subject. Consideration has also been given to the possibility of using alternative sources of protein, such as animal by-products, to address resource management and sustainable development issues. One of the strengths of 3D printing is personalization, so we chose to evaluate the impact of this technology on target populations and evaluate the possible evolutions.In order to design food in optimal conditions, the development of new 3D printers is fundamental 1) to ensure the sanitary quality (both microbiological and chemical) of these products, and 2) to control the structure and texture of these 3D-printed foods. From there, it will be possible to propose personalized foods, adapted to different categories of population (e.g. seniors or young people …). The major challenge in the next years will be to develop, using 3D printing, meat products or products blending alternative protein sources that remain perfectly structured without having to use additives. The final step will be to garner consumer acceptance for these 3D-printed foods.
    Schlagwörter additives ; animal byproducts ; biobased products ; consumer acceptance ; functional foods ; manufacturing ; meat products ; mixing ; printers ; protein sources ; resource management ; sustainable development ; texture
    Sprache Englisch
    Erscheinungsverlauf 2019-04
    Umfang p. 188-198.
    Erscheinungsort Elsevier Ltd
    Dokumenttyp Artikel
    ZDB-ID 1049246-x
    ISSN 1879-3053 ; 0924-2244
    ISSN (online) 1879-3053
    ISSN 0924-2244
    DOI 10.1016/j.tifs.2019.02.023
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  6. Artikel: Molecular and structural changes in gelatin evidenced by Raman microspectroscopy

    Duconseille, Anne / Cédric Gaillard / Thierry Astruc / Véronique Santé-Lhoutellier

    Food hydrocolloids. 2018 Apr., v. 77

    2018  

    Abstract: The gelatin used for the hard capsules manufacturing must meet strict dissolution specification to ensure the delivery of drugs at right time in the digestive tract. However, the environment of production and storage time affect the quality of gelatin ... ...

    Abstract The gelatin used for the hard capsules manufacturing must meet strict dissolution specification to ensure the delivery of drugs at right time in the digestive tract. However, the environment of production and storage time affect the quality of gelatin dissolution. This study aimed to identify the mechanisms underlying the geographical environment of production and aging impact on the gelatin dissolution rate. Gelatins from 3 different origins of production (A, B & C), whose dissolution rate had been previously characterized, were analyzed by Raman microspectroscopy before and after aging. The principal component analysis (PCA) clearly separated the aged gelatins from non-aged ones. The spectra interpretation suggested the denaturation of gelatin triple-helices. In addition, the formation of cross-links such as dityrosine, glucosyl-galactosylhydroxylysinonorleucine and proteoglycan-like sugar adducts was strongly suspected. Whatever the gelatin aging state, PCA systematically separated the B-gelatins from A and C-gelatins. Pentosidine cross-link was likely to vary depending on the production origin. Finally, the quality of dissolution was discriminated for aged gelatins of A-origin: the non-compliant gelatins exhibited higher lipid content than the compliant ones.
    Schlagwörter crosslinking ; denaturation ; digestive tract ; drugs ; gelatin ; hydrocolloids ; lipid content ; manufacturing ; pentosidine ; principal component analysis ; Raman spectroscopy ; storage time ; sugars
    Sprache Englisch
    Erscheinungsverlauf 2018-04
    Umfang p. 777-786.
    Erscheinungsort Elsevier Ltd
    Dokumenttyp Artikel
    ZDB-ID 742742-6
    ISSN 1873-7137 ; 0268-005X
    ISSN (online) 1873-7137
    ISSN 0268-005X
    DOI 10.1016/j.foodhyd.2017.11.020
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  7. Artikel: Variability in pig skin gelatin properties related to production site: A near infrared and fluorescence spectroscopy study

    Duconseille, Anne / Donato Andueza / Fabienne Picard / Thierry Astruc / Véronique Santé-Lhoutellier

    Food hydrocolloids. 2017 Feb., v. 63

    2017  

    Abstract: The pharmaceutical industry requires narrow variability in the dissolution rate of hard gelatin capsules. To test this property, gelatin is aged in high temperature and humidity conditions to mimic gelatin shelf-life. These conditions induce cross-link ... ...

    Abstract The pharmaceutical industry requires narrow variability in the dissolution rate of hard gelatin capsules. To test this property, gelatin is aged in high temperature and humidity conditions to mimic gelatin shelf-life. These conditions induce cross-link formation in gelatin chains and change the properties of the capsule. Gelatin is produced worldwide in various environmental conditions. This study set out to evaluate the impact of geographic production origin on gelatin composition, before and after aging treatment, and on its dissolution properties. Non-aged and aged pig skin gelatins from three different production plants (A, B and C) were analyzed in raw granules and in powder by near infrared and fluorescence spectroscopy to identify the mechanisms of cross-link formation during aging. Gelatin composition (lipids, dityrosine, 3,4 dihydroxyphenylalanine (DOPA)) and oxidation level, before and after aging, varied according to production origin. The gelatin from C showed no variability in dissolution rate, while gelatins from A and B dissolved more slowly after aging. Near infrared spectroscopy results suggest that water was more strongly bound to the gelatin chains in the gelatins that yielded non-compliant dissolution test results. Non-compliant gelatin exhibited more CH2, usually assigned to lipids, and more aldehydes. Even before aging we found that non-compliant gelatins tended to fluoresce more at 344 nm under 280 nm excitation. These results open new perspectives for designing tools to predict the dissolution quality of freshly produced gelatins.
    Schlagwörter aldehydes ; dihydroxyphenylalanine ; environmental factors ; fluorescence emission spectroscopy ; gelatin ; granules ; humidity ; hydrocolloids ; lipids ; near-infrared spectroscopy ; oxidation ; pharmaceutical industry ; shelf life ; swine ; temperature
    Sprache Englisch
    Erscheinungsverlauf 2017-02
    Umfang p. 108-119.
    Erscheinungsort Elsevier Ltd
    Dokumenttyp Artikel
    ZDB-ID 742742-6
    ISSN 1873-7137 ; 0268-005X
    ISSN (online) 1873-7137
    ISSN 0268-005X
    DOI 10.1016/j.foodhyd.2016.08.001
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  8. Artikel: Molecular changes in gelatin aging observed by NIR and fluorescence spectroscopy

    Duconseille, Anne / Donato Andueza / Fabienne Picard / Thierry Astruc / Véronique Santé-Lhoutellier

    Food hydrocolloids. 2016 Dec., v. 61

    2016  

    Abstract: The pharmaceutical industry requires a narrow variability in gelatin properties during storage to meet strict quality standards for hard capsules. To test the properties of gelatin during shelf life, gelatin is aged in high temperature and high humidity ... ...

    Abstract The pharmaceutical industry requires a narrow variability in gelatin properties during storage to meet strict quality standards for hard capsules. To test the properties of gelatin during shelf life, gelatin is aged in high temperature and high humidity conditions. These conditions induce the formation of cross-links in gelatin chains that impact its chemical composition and thereby the properties of the capsules. Non-aged and aged pig skin gelatins were analyzed in raw granule or powder forms by near-infrared and fluorescence spectroscopy to elucidate the mechanisms of cross-link formation during aging. Both near-infrared and fluorescence spectroscopy clearly separated non-aged from aged samples. Aging induced the formation of dityrosine and other cross-links involving amine and aldehyde functions. The presence of 3,4-dihydroxyphenylalanine (DOPA), a fluorescent product of tyrosine oxidation involved in cross-link formation, was evidenced in gelatin.
    Schlagwörter aldehydes ; chemical composition ; crosslinking ; dihydroxyphenylalanine ; fluorescence emission spectroscopy ; gelatin ; humidity ; hydrocolloids ; oxidation ; pharmaceutical industry ; shelf life ; swine ; temperature ; tyrosine
    Sprache Englisch
    Erscheinungsverlauf 2016-12
    Umfang p. 496-503.
    Erscheinungsort Elsevier Ltd
    Dokumenttyp Artikel
    ZDB-ID 742742-6
    ISSN 1873-7137 ; 0268-005X
    ISSN (online) 1873-7137
    ISSN 0268-005X
    DOI 10.1016/j.foodhyd.2016.06.007
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  9. Artikel: Sodium Chloride Diffusion during Muscle Salting Evidenced by Energy-Dispersive X-ray Spectroscopy Imaging

    Filgueras, Renata / Frederic Peyrin / Annie Venien / Jean Marc Henot / Thierry Astruc

    Journal of agricultural and food chemistry. 2016 Jan. 27, v. 64, no. 3

    2016  

    Abstract: To better understand the relationship between the muscle structure and NaCl transfers in meat, we used energy-dispersive X-ray spectroscopy (EDS) coupled with scanning electron microscopy (SEM) to analyze brined and dry-salted rat muscles. The muscles ... ...

    Abstract To better understand the relationship between the muscle structure and NaCl transfers in meat, we used energy-dispersive X-ray spectroscopy (EDS) coupled with scanning electron microscopy (SEM) to analyze brined and dry-salted rat muscles. The muscles were freeze-dried to avoid the delocalization of soluble ions that happens in regular dehydration through a graded series of ethanol. Na and Cl maps were superimposed on SEM images to combine the muscle structure and NaCl diffusion. Brining causes rapid diffusion of NaCl through the tissue. Most brine diffuses in a linear front from the muscle surface, but a small proportion enters through the perimysium network. The muscle area penetrated by brine shows heterogeneous patterns of NaCl retention, with some connective tissue islets containing more NaCl than other parts of perimysium. NaCl penetration is considerably slower after dry salting than after brining.
    Schlagwörter brining ; energy-dispersive X-ray analysis ; ethanol ; freeze drying ; image analysis ; ions ; meat ; muscles ; rats ; salting ; scanning electron microscopy ; sodium ; sodium chloride
    Sprache Englisch
    Erscheinungsverlauf 2016-0127
    Umfang p. 699-705.
    Erscheinungsort American Chemical Society, Books and Journals Division
    Dokumenttyp Artikel
    ZDB-ID 241619-0
    ISSN 1520-5118 ; 0021-8561
    ISSN (online) 1520-5118
    ISSN 0021-8561
    DOI 10.1021/acs.jafc.5b04058
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  10. Artikel: The effect of origin of the gelatine and ageing on the secondary structure and water dissolution

    Duconseille, Anne / Amidou Traore / Fabrice Audonnet / Frank Wien / Matthieu Refregiers / Thierry Astruc / Veronique Santé-Lhoutellier

    Food hydrocolloids. 2017 May, v. 66

    2017  

    Abstract: Gelatin is used to make hard capsules and has to meet strict dissolution specifications to guarantee homogeneous drug delivery. The aging of gelatin induces a decrease of its dissolution rate due to the formation of intra- and intermolecular cross-links. ...

    Abstract Gelatin is used to make hard capsules and has to meet strict dissolution specifications to guarantee homogeneous drug delivery. The aging of gelatin induces a decrease of its dissolution rate due to the formation of intra- and intermolecular cross-links. Cross-link formation has shown to be dependent on the environmental conditions of production, such as temperature and humidity, and therefore on the geographic origin of production. Gelatin structure consists of an amorphous phase (coil structure) and a crystal phase (triple-helixes) and is very sensitive to environmental changes. The present work aims at understanding the role and effects of structural changes during aging on gelatin dissolution, taking into account the origin of production. The molecular structure of pig skin gelatins from three different production sites of the same company were studied by differential scanning calorimetry, synchrotron circular dichroism and 1H nuclear magnetic resonance. It turned out that aging induced the melting of triple-helixes, an increase of random coils and, probably, β-turn conformations. The gelatin structure varied with the origin of production and thus affected the dissolution rate. Gelatins with non-compliant dissolution rates exhibited a higher amount of amorphous phase after aging than compliant gelatins. Although it was not possible to formulate any certain interpretation of the synchrotron circular dichroism results regarding gelatin dissolution, this technique is able to differentiate compliant dissolutions from non-compliant ones, even before gelatin aging.
    Schlagwörter circular dichroism spectroscopy ; crosslinking ; differential scanning calorimetry ; drugs ; environmental factors ; gelatin ; humidity ; hydrocolloids ; melting ; nuclear magnetic resonance spectroscopy ; provenance ; swine ; temperature
    Sprache Englisch
    Erscheinungsverlauf 2017-05
    Umfang p. 378-388.
    Erscheinungsort Elsevier Ltd
    Dokumenttyp Artikel
    ZDB-ID 742742-6
    ISSN 1873-7137 ; 0268-005X
    ISSN (online) 1873-7137
    ISSN 0268-005X
    DOI 10.1016/j.foodhyd.2016.12.005
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