Skip to content
DraconiticResearch
Search Sources API
206,698 studies31 sourcesUpdated 26 min ago
Peer-reviewedCC BY-NC-NDArchivos Latinoamericanos de Nutrición

Estudio de las modificaciones en proteínas de reineta (Brama australis), sometidas a congelación y almacenamiento a -18ºC y -30ºC

  • Lilian E. Abugoch1,2
  • Vilma Quitral R1,2
  • María Angélica Larraín1,2
  • Vinagre L Julia1,2
  • Andrei Kriukov1,2
  • Gloria Chávez1,2
  1. 1Universidad de Chile Facultad de Ciencias Químicas y Farmacéuticas, Depto. Ciencia de los Alimentos y Tecnología Química
  2. 2Universidad de Chile, Santiago, Chile
Open at sourceDOICite

Abstract

The objective of the present work was to study functional and thermal properties of reineta (Brama australis) frozen meat, analysed by water retention capacity (WRC), gel forming capacity (GFC), texture, emulsifying capacity and differential scanning calorimetry (DSC). For this study, reineta fillets were obtained and extracted by the same conditions, and cutted, packaged, frozen and stored at -18 degrees C and -30 degrees C for 7 months. The results obtained, showed that there were no signifficant differences in the responses to thermal treatment for all the specimens. For samples frozen at -18 degrees C and -30 degrees C, the protein contents were 23.5 + 0.0 and 25.4 + 1.0%, respectively. The WRC values were 0.45 + 0.1 and 1.59 +/- 0.0 g water/g protein, respectively. The gel forming capacity was only present in the fresh samples, whereas the frozen stored ones only form protein aggregates. The emulsifying capacity was between 960 and 1400 g oil / g protein, and the storage time increased this value. The miosin denaturation temperature (Td) and denaturation enthalpy (?H), obtained by DSC, fluctuated between 39.2 +/- 0.5 to 44.8 +/- 0.8 degrees C and 1.12 +/- 0.3 to 0.52 +/- 0.2 J/g, respectively. The actina values were between 71.0 +/- 0.6 to 75.3 +/- 0.5 degrees C and between 0.5 +/- 0.1 to 0.7 +/- 0.1 J/g. Cooperativity decreased as the storage time increased. This is showing a certain degree of protein displacement. The values found by thermal analyses showed a direct relationship with the functional properties, both decreasing with storage time.

Related

  1. Acalypha australis as a Potential Reservoir Host of Hop Stunt Viroid in Vineyards
    Gwang-Ho Yeom, Ju-Ho Bae, Sang-Yun Cho +1
    The plant pathology journalPeer-reviewedCC BY-NCFull textPlant biologyEurope PMC
  2. Latitudinal Variation in the Phenology of the Emergent Species Phragmites australis and the Submerged Species Potamogeton crispus in Shallow Lakes of the North China Plain
    Jia Tang, Quanzhou Yu, Yong Li +6
    Plants (Basel, Switzerland)Peer-reviewedCC BYFull textPlant biologyEurope PMC
  3. Genetic canalization of nutrient resorption in the widespread grass Phragmites australis under salt stress.
    Lele Liu, Wenyi Sheng, Huijia Song +6
    ELifePeer-reviewedCC BYFull textPlant biologyEurope PMCDOAJ
  4. Molecular methods for differentiating Phragmites australis subspecies and identification of hybrid stands in the Upper Midwestern United States
    Nicholas P. Tippery, Daniel J. Larkin, Julia Bohnen +6
    Applications in Plant SciencesPeer-reviewedCC BY-NC 4.0Full textGenetics & genomicsPMC
  5. Functional Traits and Competitor-Stress-Tolerator- Ruderal Strategies of Phragmites australis in Southwestern Korean Estuaries
    Dong-Ho Son, Seok Yeoul Ko, Kyoung Hoon Yang +3
    Proceedings of the National Institute of Ecology of the Republic of KoreaPeer-reviewedCC BY-NCFull textGeneral biologyDOAJ

Cite

BibTeXRIS
BibTeX
@article{abugoch2026estudio,
  title = {{Estudio de las modificaciones en proteínas de reineta (Brama australis), sometidas a congelación y almacenamiento a -18ºC y -30ºC}},
  author = {Lilian E. Abugoch and Vilma Quitral R and María Angélica Larraín and Vinagre L Julia and Andrei Kriukov and Gloria Chávez},
  journal = {Archivos Latinoamericanos de Nutrición},
  year = {2026},
  month = jul,
  doi = {10.37527/2006.56.4.006},
  url = {https://doi.org/10.37527/2006.56.4.006},
  note = {CC BY-NC-ND},
}
RIS
TY  - JOUR
TI  - Estudio de las modificaciones en proteínas de reineta (Brama australis), sometidas a congelación y almacenamiento a -18ºC y -30ºC
AU  - Lilian E. Abugoch
AU  - Vilma Quitral R
AU  - María Angélica Larraín
AU  - Vinagre L Julia
AU  - Andrei Kriukov
AU  - Gloria Chávez
PY  - 2026
DA  - 2026/07/25
JO  - Archivos Latinoamericanos de Nutrición
DO  - 10.37527/2006.56.4.006
UR  - https://doi.org/10.37527/2006.56.4.006
AB  - The objective of the present work was to study functional and thermal properties of reineta (Brama australis) frozen meat, analysed by water retention capacity (WRC), gel forming capacity (GFC), texture, emulsifying capacity and differential scanning calorimetry (DSC). For this study, reineta fillets were obtained and extracted by the same conditions, and cutted, packaged, frozen and stored at -18 degrees C and -30 degrees C for 7 months. The results obtained, showed that there were no signifficant differences in the responses to thermal treatment for all the specimens. For samples frozen at -18 degrees C and -30 degrees C, the protein contents were 23.5 + 0.0 and 25.4 + 1.0%, respectively. The WRC values were 0.45 + 0.1 and 1.59 +/- 0.0 g water/g protein, respectively. The gel forming capacity was only present in the fresh samples, whereas the frozen stored ones only form protein aggregates. The emulsifying capacity was between 960 and 1400 g oil / g protein, and the storage time increased this value. The miosin denaturation temperature (Td) and denaturation enthalpy (?H), obtained by DSC, fluctuated between 39.2 +/- 0.5 to 44.8 +/- 0.8 degrees C and 1.12 +/- 0.3 to 0.52 +/- 0.2 J/g, respectively. The actina values were between 71.0 +/- 0.6 to 75.3 +/- 0.5 degrees C and between 0.5 +/- 0.1 to 0.7 +/- 0.1 J/g. Cooperativity decreased as the storage time increased. This is showing a certain degree of protein displacement. The values found by thermal analyses showed a direct relationship with the functional properties, both decreasing with storage time.
SN  - 0004-0622
SN  - 2309-5806
ER  -