Mostrar el registro sencillo del ítem
dc.contributor.author
Velazquez, Diego Ezequiel
dc.contributor.author
Latorre, Maria Emilia
dc.date.available
2021-02-26T13:47:35Z
dc.date.issued
2019-09
dc.identifier.citation
Velazquez, Diego Ezequiel; Latorre, Maria Emilia; Physicochemical, thermal and mechanical characterization study of perimysial collagen of two bovine muscles; Elsevier Science; International Journal of Biological Macromolecules; 136; 9-2019; 404-409
dc.identifier.issn
0141-8130
dc.identifier.uri
http://hdl.handle.net/11336/126760
dc.description.abstract
Chemical, thermal and mechanical collagen characteristics of intramuscular perimysial connective tissue (IMCT) from bovine Semitendinosus (ST) and Pectoralis profundus (PP) muscles were studied. Furthermore, these collagen characteristics in presence/absence of other extracellular matrix components were analyzed for both muscles. Differences between muscles were observed for collagen content; all IMCT-PP perimysial samples were higher than ST samples. In addition, for both muscles, IMCT-alkali resistant samples allowed the highest trypsin soluble collagen. The main differences between muscles were recorder for thermal and mechanical properties. The denaturation of collagen in the perimysium evidenced differences in total denaturation energy (ΔH) and peak temperatures (Tp). The ΔH resulted higher for IMCT-PP than for IMCT-ST tissues in all samples. By the tensile test it was observed that the maximum loads were constant and higher in all PP samples. In the FTIR assay, the peaks for the main amides were registered in both tissues. However, slight differences between ST and PP-IMCT were detected on hydrogen bond interactions and in secondary structure of the protein. The results reinforce the hypothesis of the presence of different IMCT-perimysial-collagen pools. In this study, chemical, thermal and mechanical characteristics were considered and quantified. However, the mechanical function and development of muscle in-vivo could be the main influence on the extracellular collagen characteristics as well as its interactions with non-collagen compounds. Its formation is essential for muscle function.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Science
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
COLLAGEN
dc.subject
DSC
dc.subject
FTIR
dc.subject
INTRAMUSCULAR CONNECTIVE TISSUE
dc.subject
MEAT
dc.subject
TENSION LOAD
dc.subject.classification
Otras Ingeniería de los Materiales
dc.subject.classification
Ingeniería de los Materiales
dc.subject.classification
INGENIERÍAS Y TECNOLOGÍAS
dc.title
Physicochemical, thermal and mechanical characterization study of perimysial collagen of two bovine muscles
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2021-02-18T15:47:43Z
dc.journal.volume
136
dc.journal.pagination
404-409
dc.journal.pais
Países Bajos
dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Velazquez, Diego Ezequiel. Universidad Nacional del Centro de la Provincia de Buenos Aires. Facultad de Ciencias Exactas. Instituto de Física de Materiales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Latorre, Maria Emilia. Universidad Nacional del Centro de la Provincia de Buenos Aires. Facultad de Ciencias Veterinarias. Departamento de Tecnologia y Calidad de los Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.journal.title
International Journal of Biological Macromolecules
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0141813019303307
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.ijbiomac.2019.06.092
Archivos asociados