Rheological behavior, conformational changes and interactions of water-soluble myofibrillar protein during heating

Chen, Xing; Xu, Xinglian; Li, Dongmei; Han, Minyi; Wang, Peng

doi:10.1016/j.foodhyd.2017.10.030

Cited by 105 publications

(58 citation statements)

References 42 publications

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“…Chumngoen, Chen, Chen, and Tan () reported that protein solubility in chicken meat was reduced with increases in the cooking temperature. Chen et al () also demonstrated a proportional decrease in the protein solubility of chicken meat with the increase in cooking temperature (Chen et al, ; Comfort & Howell, ), which results in protein denaturation and formation of intermolecular cross‐links (Luo et al, ), and due to the production of large aggregates thereafter and cooking driven protein oxidation, protein digestibility decreases (Luo et al, ). The results obtained from the current study indicated that greater protein denaturation occurred in BM which is more sensitive to protein denaturation than TM.…”

Section: Resultsmentioning

confidence: 99%

Changes in chicken meat proteins during microwave and electric oven cooking

Taşkıran

Olum²,

Candoğan

2019

J Food Process Preserv

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Alterations in proteins and some functional properties of chicken thigh (TM) and breast meats (BM) cooked with microwave oven (MWO) were evaluated in comparison to traditional electric oven (EO). Cooking loss in both TM and BM did not differ between the cooking methods (p > .05). In TM, MWO cooking resulted in higher water‐holding capacity (WHC) than EO (p < .05). Sarcoplasmic protein solubility of TM decreased with MWO cooking while both cooking methods resulted in reduction in both sarcoplasmic and myofibrillar protein solubility in BM (p < .05). TM and BM cooked with MWO were harder in texture (p < .05) than EO cooked samples as determined in texture profile analysis. The intensity of myofibrillar protein bands in the Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis (SDS‐PAGE) decreased after cooking by both MWO and EO, whereas EO cooked samples demonstrated more fragmentation in both sarcoplasmic and myofibrillar proteins in comparison with MWO cooked chicken meats. Practical applications Microwave cooking is an alternative, efficient method to reduce time, energy, and cost as compared to conventional oven cooking. In oven cooking, thermal energy is transmitted quite slow from the surface of the food to the center, whereas microwave energy is converted into heat inside the food itself which provides homogeneous heat distribution. In the present study, the effects of microwave and EO cooking methods on some quality characteristics, mainly proteins of TM and BM were evaluated. It was found that microwave cooking resulted in harder texture, but better WHC to its counterpart which also caused more degradation in myofibrillar and sarcoplasmic proteins. Because microwaves shorten cooking time, lowers the energy consumption, and makes the production process sustainable and more efficient than with conventional ovens, while better preserving the nutritional quality of the product becomes a sound alternative. Therefore, it is worth to keep exploring this novel cooking approach that might render significant advantages in industrial applications.

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Section: Resultsmentioning

confidence: 99%

Changes in chicken meat proteins during microwave and electric oven cooking

Taşkıran

Olum²,

Candoğan

2019

J Food Process Preserv

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“…From 20 to 66°C, the solubility of meat batters declined gradually. This suggests that nondisulfide covalent bonds and proteins underwent a denaturation process that favored interactions, leading to a decrease of solubility during heating (Chen et al, ; Gómez‐Guillén et al, ). A significant negative correlation ( p < .05) between cooking loss and solubility ( r = −.722) was observed, which indicated that the formation of the nondisulfide covalent bonds might be conducive to cooking loss.…”

Section: Resultsmentioning

confidence: 99%

“…This was consistent with previous disulfide bonds. Because the existing disulfide bonds can be cleaved by heating, heating also caused unfolded protein to activate buried sulfhydryl groups and oxidation of sulfhydryl groups led to the formation of new intermolecular disulfide bonds during continuous or intense heating (Chen et al, ).…”

Section: Raman Spectroscopic Analysismentioning

confidence: 99%

“…Error column indicates the mean values ± standard deviations of three replicates. Different letters indicate significant differences (p < .05) F I G U R E 5 Percentages of protein secondary structure: α-helix, β-sheet, turns, out of order of the meat batter analyzed bonds can be cleaved by heating, heating also caused unfolded protein to activate buried sulfhydryl groups and oxidation of sulfhydryl groups led to the formation of new intermolecular disulfide bonds during continuous or intense heating (Chen et al, 2017).…”

Section: Changes Of Disulfide Bondsmentioning

confidence: 99%

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Raman spectroscopy and low‐field nuclear magnetic resonance used to monitor the relationship between protein conformation and water retention in the formation for process of gel

Zheng

Zhao

et al. 2019

J Food Process Preserv

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The objective of this study was to assess the relationship between protein conformations and water retention during gelation, investigated by Raman spectroscopy and low‐field nuclear magnetic resonance. There were significant positive correlations (p < .05) between hydrophobic bonds (r = .690), disulfide bonds (r = .672), and cooking loss and a significant negative correlations (p < .05), between cooking loss and ionic bonds (r = −.668) and hydrogen bonds (r = −.600). There was significant negative correlation between β‐sheets and peak area ratio of P22 (r = −.754). With the decrease of immobilized water and the increase of β‐sheets, the cooking loss was increased. The changes in chemical interactions will lead to conformational changes that will influence state of water and water retention. Results indicated that water retention was affected by conformational changes during gelation. Practical applications Water retention is important for obtaining high‐quality meat products (tenderness, mouth feel, and production). The paper provided some data for the preservation and processing of gel products from the relationship between water retention and conformation.There are several ways of preserving water in meat products, including adding phosphates and additives, and some physical processes. However, the most common method is to add a certain amount of phosphate. Phosphates were found as a novel risk factor and that physical processes lose some nutrients. Therefore, studying the relationship between protein conformation and cooking loss will provide a new method for preserving water. Besides providing technical support for the development of food industry technology, it also provides a certain way for the development of green food. Using the characteristics of food raw materials to change the characteristics of products will be themainstream of market production.

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“…According to Chen et al, (2018) denaturation decreases the water solubility of proteins, since these have their conformational state and their intramolecular interactions altered. Since the application of the fibers made with SPI and PVA is intended for the production of coatings for active food packaging applications, the decrease in water solubility is shown as a positive factor, which will allow for a more gradual release of the bioactive into the food product.…”

Section: Morphological Thermal Characterization and Stability Of Thementioning

confidence: 99%

Electrospun β-carotene–loaded SPI:PVA fiber mats produced by emulsion-electrospinning as bioactive coatings for food packaging

Bruni

Oliveira

Gómez‐Mascaraque

et al. 2020

Food Packaging and Shelf Life

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In this work, emulsion electrospinning was used to develop an active internal coating for food packaging applications. Specifically, the antioxidant molecule β-carotene, was encapsulated in a mixture of soy protein isolate (SPI) and polyvinyl alcohol (PVA) which was directly electrospun onto a polyhydroxybutyrate-co-valerate (PHB92/PHV8) film. An annealing treatment was applied to improve the adhesion of the electrospun mat onto the packaging film, which contributed to modulate the release of the active compound. Stable SPI:PVA emulsions (with a 50:50 ratio) were developed using soybean oil (SBO) as carrier of the hydrophobic -carotene. The encapsulation efficiency of β-carotene in the electrospun SPI:PVA fibers was 65.0% ± 2.6 %, being 51.4 % ± 0.9 % effectively incorporated into their cores. Finally, the in-vitro release assay of the antioxidant in soybean oil, which simulates fatty foods, demonstrated that the heat treatment (anneling) contributed to a slower and more sustained released of the bioactive compound.

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Rheological behavior, conformational changes and interactions of water-soluble myofibrillar protein during heating

Cited by 105 publications

References 42 publications

Changes in chicken meat proteins during microwave and electric oven cooking

Changes in chicken meat proteins during microwave and electric oven cooking

Raman spectroscopy and low‐field nuclear magnetic resonance used to monitor the relationship between protein conformation and water retention in the formation for process of gel

Electrospun β-carotene–loaded SPI:PVA fiber mats produced by emulsion-electrospinning as bioactive coatings for food packaging

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