Characterization of fish myosin aggregates using static and dynamic light scattering

Brenner, Tom; Jóhannsson, Ragnar; Nicolai, Taco

doi:10.1016/j.foodhyd.2008.01.003

Cited by 35 publications

(22 citation statements)

References 41 publications

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“…The shifts between the spectra at different temperatures probably reflect the changes in relative scattering intensities caused by protein denaturation. Protein denaturation as a result of heat treatment lead to aggregation of denatured fish proteins, which is accompanied by changes in light scattering intensity (Brenner, Johannsson, & Nicolai, 2009;Chanthai, Nieda, Ogawa, Tamiya, & Tsuchiya, 1998). In the lowest region of the spectrum an apparent correlation between temperature treatment and absorbance intensities is observed (Fig.…”

Section: Reflectance Spectroscopymentioning

confidence: 91%

Endpoint temperature of heat-treated surimi can be measured by visible spectroscopy

Stormo¹,

Sivertsen²,

Heia³

et al. 2012

Food Control

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Section: Reflectance Spectroscopymentioning

confidence: 91%

Endpoint temperature of heat-treated surimi can be measured by visible spectroscopy

Stormo¹,

Sivertsen²,

Heia³

et al. 2012

Food Control

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“…In meat, muscle cells contain both globular and fibrous proteins that exhibit different behaviors upon heating. Myosin and BSA have been extensively studied as a protein model (Brenner, Johannsson, & Nicolai, 2009;Su, Qi, He, Zhang, & Jin, 2008;Ye, 2006). Slight heat-induced aggregation starts in BSA at above 60°C, whereas 50°C is enough to induce the aggregation process in myosin.…”

Section: Introductionmentioning

confidence: 99%

Characterization of protein aggregates following a heating and freezing process

Kajak-Siemaszko,

Aubry,

Peyrin

et al. 2011

Food Research International

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“…Similar methods have been used to study thermal denaturation behavior of myosin [20][21][22] and actin 23,24 . Nevertheless, most of these methods require extraction and solubilization of the protein of interest and are neither applicable for the investigation of complex tissues nor do they allow for simultaneous observation of ongoing structural changes at the required optical resolution.…”

Section: Introductionmentioning

confidence: 99%

Second Harmonic Generation Microscopy: A Tool for Spatially and Temporally Resolved Studies of Heat Induced Structural Changes in Meat

et al. 2009

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Myofibers and collagen show non-linear optical properties enabling imaging using second harmonic generation (SHG) microscopy. The technique is evaluated for use as a tool for real-time studies of thermally induced changes in thin samples of unfixed and unstained pork. The forward and the backward scattered SHG light reveal complementary features of the structures of myofibers and collagen fibers. Upon heating the myofibers show no structural changes before reaching a temperature of 53°C. At this temperature the SHG signal becomes extinct. The extinction of the SHG at 53°C coincides with a low-temperature endotherm peak observable in the differential scanning calorimetry (DSC) thermograms. DSC analysis of epimysium, the connective tissue layer that enfold skeletal muscles, produces one large endotherm starting at 57°C and peaking at 59.5°C. SHG microscopy of collagen fibers reveals a variability of thermal stability. Some fibers show severe shrinkage at 57°C, before the signal for most of them vanishes between 59°C and 61°C and thus coinciding with the endotherm of the thermograms. However, in some areas, strong SHG signals from collagen can be visualized even after prolonged heating to 67°C and thus indicating regions of much higher thermal stability. It is seen that the benefits of the structural and temporal information available from SHG microscopy reveals complementary information to a traditional DSC measurement and enables a more complete understanding of the thermal denaturation process.

show abstract

Characterization of fish myosin aggregates using static and dynamic light scattering

Cited by 35 publications

References 41 publications

Endpoint temperature of heat-treated surimi can be measured by visible spectroscopy

Endpoint temperature of heat-treated surimi can be measured by visible spectroscopy

Characterization of protein aggregates following a heating and freezing process

Second Harmonic Generation Microscopy: A Tool for Spatially and Temporally Resolved Studies of Heat Induced Structural Changes in Meat

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