Heat-Induced Changes in Myofibrillar Protein Structures and Myowater of Two Pork Qualities. A Combined FT-IR Spectroscopy and Low-Field NMR Relaxometry Study

Bertram, Hanne Christine; Köhler, Achim; Böcker, Ulrike; Ofstad, Ragni; Andersen, Henrik J.

doi:10.1021/jf0514726

Cited by 140 publications

(110 citation statements)

References 28 publications

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“…For HOLA-MP, heat treatment caused a decrease in a-helical structure and an increase in total β-Sheet structure. These results might be attributed to the formation of aggregates or enhanced protein-protein interaction under oxidative stress, which were similar to those reported previously [32].…”

Section: Ftirsupporting

confidence: 92%

Influence of Linoleic Acid-Induced Oxidative Modification on Gel Properties of Myofibrillar Protein from Silver Carp (Hypophthalmichthys molitrix) Muscle

et al. 2016

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Oxidation extent of myofibrillar protein (MP) from silver carp (Hypophthalmichthys molitrix) was affected by the content and type of lipid peroxidation (LPO) products. Oxidized linoleic acid (OLA) was selected as a main representative of lipid peroxidation to investigate the effects of oxidative modification of LPO products on MP structure. Structural changes of the oxidized myofibrillar protein were evaluated by the contents of carbonyl and total sulfhydryls, surface hydrophobicity, SDS-PAGE and Fourier transform infrared spectroscopy. Heating procedure was also applied for further evaluation of gelling properties. The results from SDS-PAGE indicated that aggregation and denaturation of myosin occurred in the oxidized system. The presence of OLA intensified oxidation-initiated loss of a-helix conformation as well as tertiary structure of MP. With the addition of OLA concentration less than 3 mM, a remarkably enhanced gelling capacity of MP was observed. While the excessive covalent bond (OLA > 5 mM) could lead to the breakage of protein-protein bonds, causing the collapse of the gel structure. The gelation procedure induced by OLA involved simultaneous protein oxidation and internal cross-linking.

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Section: Ftirsupporting

confidence: 92%

Influence of Linoleic Acid-Induced Oxidative Modification on Gel Properties of Myofibrillar Protein from Silver Carp (Hypophthalmichthys molitrix) Muscle

et al. 2016

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“…Otros trabajos coinciden en afirmar que los cambios microestructurales, como la formación de huecos entre miofibrillas, ocurre mas frecuente durante el cocinado de productos cárnicos cocidos que de carnes frescas. Esto refleja que la desintegración de la fina estructura es más sensible al calor y afecta principalmente proteínas del colágeno y miofibrilar, alterando la integridad de la estructura nativa (17).…”

Section: Discussionunclassified

Análisis estructural de la carne de jamón durante el proceso de cocción y temperatura de almacenamiento

H¹,

M²,

A³

2009

Rev MVZ Córdoba

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RESUMENObjetivo. Determinar los cambios estructurales de jamón de cerdo por efecto del proceso de cocción y temperatura de almacenamiento. Materiales y métodos. Fueron realizados seis tratamientos, utilizando tres temperaturas internas de cocción (72, 75 y 78°C) a una temperatura de almacenamiento de 4°C. Un tratamiento definido como patrón absoluto, cocido hasta alcanzar una temperatura interna de 72°C, sin tiempo de retención en cocción y un patrón relativo, elaborado bajo las mismas condiciones del patrón absoluto pero almacenado a 0°C. En cada ensayo, fueron realizadas observaciones con microscopio óptico de luz sobre la estructura del tejido muscular y análisis instrumental de textura los días 0, 26 y 42. Los datos obtenidos en este estudio fueron examinados mediante un análisis de varianza de una vía. Resultados. Los resultados reportaron que el jamón cocido a una temperatura de 75°C y tiempo de retención en cocción de 5 minutos, es más efectivo para disminuir el efecto negativo de la separación por pérdida de integridad estructural de las microfibrillas y de la estructura de la red de colágeno. El incremento en la dureza fue reportado para todos los tratamientos al final del periodo de almacenamiento. Conclusiones. El tratamiento que mejor comportamiento presentó a nivel microscópico fue el elaborado a 75°C como temperatura de cocción y 5 min de retención, donde las fibras de colágeno del tejido conectivo mantienen una arquitectura mas ordenada junto con la fibra muscular a lo largo del tiempo.

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“…Cooking loss is significantly related to water loss and fat drip. As the meat temperature increases, the water capacity decreases due to the thermal denaturation of meat proteins (Straadt et al, 2007;Shaarani et al, 2006;Bertram et al, 2006). The gelatinization of collagen significantly influences water capacity.…”

Section: Texture Measurementmentioning

confidence: 99%

Effect of Long Low Temperature-Short High Temperature Cooking Cycle on Physicochemical Properties of Beef

Ko¹,

Yoo，Sang-ho²,

Lee³

et al. 2010

FSTR

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A two-step heating process, long low temperature-short high temperature cooking cycle, is used to maximize fat reduction in roast beef. First, the beef was cooked at a low temperature for a long time; then, it was cooked at a higher temperature for a short time. The study examines cooking loss, fat content, texture, and inosine 5'-monophosphate (IMP) production of cooked meat under different heating conditions. In an oven, the internal temperature of the meat increased to a transition point of 48 or 54℃ at oven temperatures of 80 or 100℃ and reached 60℃ at 220℃. The fat was reduced by up to 44.2% compared to 27.8% under conventional roasting conditions. In addition, the two-step heating process kept the meat tender and juicy but improved IMP content.

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Heat-Induced Changes in Myofibrillar Protein Structures and Myowater of Two Pork Qualities. A Combined FT-IR Spectroscopy and Low-Field NMR Relaxometry Study

Cited by 140 publications

References 28 publications

Influence of Linoleic Acid-Induced Oxidative Modification on Gel Properties of Myofibrillar Protein from Silver Carp (Hypophthalmichthys molitrix) Muscle

Influence of Linoleic Acid-Induced Oxidative Modification on Gel Properties of Myofibrillar Protein from Silver Carp (Hypophthalmichthys molitrix) Muscle

Análisis estructural de la carne de jamón durante el proceso de cocción y temperatura de almacenamiento

Effect of Long Low Temperature-Short High Temperature Cooking Cycle on Physicochemical Properties of Beef

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