Zobrazeno 1 - 10
of 40
pro vyhledávání: '"Jacques Lepetit"'
Publikováno v:
Meat Science
Meat Science, Elsevier, 2011, 88 (1), pp.28-35. ⟨10.1016/j.meatsci.2010.11.027⟩
Meat Science, Elsevier, 2011, 88 (1), pp.28-35. ⟨10.1016/j.meatsci.2010.11.027⟩
Among the techniques based on light interactions with biological tissues, fluorescence polarization offers a selective means of characterizing the organization of biological tissues. This paper presents a methodology for investigating the fluorescenc
Autor:
Sophie Allais, Jacques Lepetit, Hubert Levéziel, Christophe Denoyelle, Jean-François Hocquette, Sylvie Rousset, Peggy Raynaud, Nathalie Payet-Duprat, Laurent Journaux, Gilles Renand, Carine Bernard-Capel
Publikováno v:
Journal of Animal Science. 89:1-11
The objectives of the study were to evaluate allelic frequencies and to test the association of polymorphisms in the calpastatin (CAST) and μ-calpain (CAPN1) genes with meat tenderness in 3 French beef breeds. A total of 1,114 Charolais, 1,254 Limou
Autor:
Nathalie Payet-Duprat, Christophe Denoyelle, Gilles Renand, Carine Bernard-Capel, Hubert Levéziel, L. Journaux, Sophie Allais, Jean-François Hocquette, Jacques Lepetit, Aline Bonnot, Sylvie Rousset
Publikováno v:
Journal of Animal Science. 88:446-454
The availability of genetic tests to detect different mutations in the myostatin gene allows the identification of heterozygous animals and would warrant the superiority of these animals for slaughter performance if this superiority is confirmed. Thu
Publikováno v:
Meat Science
Meat Science, Elsevier, 2009, 83 (4), pp.672-677. ⟨10.1016/j.meatsci.2009.08.002⟩
Meat Science, Elsevier, 2009, 83 (4), pp.672-677. ⟨10.1016/j.meatsci.2009.08.002⟩
Potential of front-face fluorescence spectroscopy was evaluated to classify muscles according to their chemical and rheological characteristics. Seven bovine muscles (Semitendinosus, Semimembranosus, Tensor fasciae latae, Rectus abdominis, Longissimu
Autor:
Christophe Chambon, Jean-François Hocquette, Elisabeth Laville, Martine Morzel, Jacques Lepetit, Sylvie Blinet, Gilles Renand, Thierry Sayd
Publikováno v:
Journal of Agricultural and Food Chemistry
Journal of Agricultural and Food Chemistry, American Chemical Society, 2009, 57 (22), pp.10755-10764. ⟨10.1021/jf901949r⟩
Journal of Agricultural and Food Chemistry, American Chemical Society, 2009, 57 (22), pp.10755-10764. ⟨10.1021/jf901949r⟩
Chantier qualité GA; International audience; Within a population of Charolais young bulls, two extreme groups of longissimus thoracis muscle samples, classified according to Warner−Bratzler shear force (WBSF) of 55 °C grilled meat, were analyzed
Autor:
Jacques Lepetit
Publikováno v:
Meat Science. 80:960-967
One of the major changes in connective tissues during heating is the transformation of the quasi-crystalline structure of collagen into a random-like structure. This molecular change induces a shortening of these tissues and gives them a rubber-like
Publikováno v:
Food Control. 19:931-939
Muscle food undergoes structural modifications during postmortem ageing which affect its mechanical, electrical and dielectric properties, particularly the anisotropy of these properties. This study shows that rapid and non-invasive control methods b
Publikováno v:
Journal of Food Engineering. 85:116-122
The objective of this work was to study the electrical anisotropy behaviour of beef meat during maturation for the purpose of early assessment of meat ageing. Early assessment of beef meat fibre strength allows customised ageing of raw materials and
Publikováno v:
Meat Science. 77:512-519
The electrical properties of biological tissues have been researched for many years. Impedance measurements observed with increasing frequencies are mainly attributed to changes in membrane conductivity and ion and charged-molecule mobility (mainly N
Autor:
Jacques Lepetit
Publikováno v:
Meat Science. 76:147-159
This work concerns the relationship between meat tenderness and the rubber-like properties, i.e. pressure and elastic modulus, that endomysium and perimysium connective tissues develop when meat has been heated to a temperature above which collagen c