Low-field NMR study of heat-induced gelation of pork myofibrillar proteins and its relationship with microstructural characteristics

Han, Minyi; Wang, Peng; Xu, Xinglian

doi:10.1016/j.foodres.2014.05.062

Cited by 336 publications

(168 citation statements)

References 41 publications

Supporting

Mentioning

154

Contrasting

Unclassified

Order By: Relevance

“…[21] One to three grams of each gel sample was placed in a glass tube (inner diameter: 60 mm). Data were collected using a Niumag Benchtop Pulsed NMR Analyzer MesoMR23-060H-I (Niumag Electric Corporation, Shanghai, China).…”

Section: Hardnessmentioning

confidence: 99%

See 1 more Smart Citation

Gelling properties of myosin as affected by L-lysine and L-arginine by changing the main molecular forces and microstructure

Zheng

Lei

et al. 2017

International Journal of Food Properties

View full text Add to dashboard Cite

This paper investigated the effects of L-lysine (Lys) and L-arginine (Arg) on the water-holding capacity (WHC) and hardness of myosin gel as well as the mechanism of these effects. The results showed that Lys, Arg, and KOH increased the WHC but decreased the hardness in all cases. At pH 6.32, the WHC increased in the order control < KOH < Lys ≈ Arg, while the hardness decreased in the order control > KOH > Lys > Arg. Lys shortened low field nuclear magnetic resonance spin-spin relaxation times (T 2 ), while Arg and KOH slightly affected T 2 . Lys, Arg, and KOH had different influences on the molecular forces in myosin gels and the distribution of myosin size. Lys formed a gel with porous clusters, while Arg generated a gel with fine caves. Therefore, both Lys and Arg changed the microstructure of myosin gel by changing the distribution of the myosin size as well as the molecular forces that form and/or maintain myosin gel, ultimately contributing to the differences in the WHC, hardness, and T 2 .ARTICLE HISTORY

show abstract

Section: Hardnessmentioning

confidence: 99%

“…[21] As illustrated in Fig. 2 23 ), were assigned to the bound, partially immobilized, immobilized, and free water, respectively.…”

Section: Lf-nmr Spin-spin Relaxation Timesmentioning

confidence: 99%

Gelling properties of myosin as affected by L-lysine and L-arginine by changing the main molecular forces and microstructure

Zheng

Lei

et al. 2017

International Journal of Food Properties

View full text Add to dashboard Cite

show abstract

“…Low-field NMR relaxation measurements were taken according to the method developed by Han et al (2014), with slight modifications. Approximately 1.5 g of paste was placed inside the NMR tubes (15 mm in diameter) and cooked at 72°C for 30 min.…”

Section: Low-field Nmrmentioning

confidence: 99%

“…WHC is an important property of meat products (Han, Wang, Xu, & Zhou, 2014). Low-field nuclear magnetic resonance (NMR) relaxation is a rapid, nondestructive, and noninvasive method that is used to determine the mobility and distribution of water pools with different relaxation time rates in meat products (Bertram, Kohler, Böcker, Ofstad, & Andersen, 2006;Han et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

“…Low-field nuclear magnetic resonance (NMR) relaxation is a rapid, nondestructive, and noninvasive method that is used to determine the mobility and distribution of water pools with different relaxation time rates in meat products (Bertram, Kohler, Böcker, Ofstad, & Andersen, 2006;Han et al, 2014). It has also been used to study changes in WHC and water mobility as a result of various treatments such as heating and high pressure (Hinrichs et al, 2004;Møller et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Effects of NaCl on water characteristics of heat-induced gels made from chicken breast proteins treated by isoelectric solubilization/precipitation

Shao

Zou

et al. 2015

CyTA - Journal of Food

View full text Add to dashboard Cite

(2016) Effects of NaCl on water characteristics of heat-induced gels made from chicken breast proteins treated by isoelectric solubilization/precipitation, CyTA -Journal of Food, 14:1, 145-153, DOI: 10.1080/19476337.2015 To link to this article: https://doi.org/10. 1080/19476337.2015 Effects of NaCl contents (0%, 0.5%, 1%, 1.5%, and 2%) on texture, water-holding capacities and microstructures of heat-induced gels made from chicken breast meat proteins isolated by isoelectric solubilization/precipitation (ISPC-gels) were investigated. The water characteristics during heating were also elucidated by low-field nuclear magnetic resonance T 2 relaxometry. The ISPC-gels with increased NaCl content exhibited good texture and low cooking loss but high centrifugal loss. The amount of free water (T 22 component) that was converted into immobilized water (T 21 component) increased with NaCl addition in accordance with the decline in cooking loss. However, increased T 21 values at 1.5% and 2% NaCl content indicated that water was weakly bound to the macromolecules and was highly mobile. These results were strongly corroborated by microstructure images that illustrated ISPC-gels containing 1% NaCl showed a continuous and dense structure with small pores and thin cross-linked strands, which had the lowest total water loss.Keywords: chicken breast proteins; isoelectric solubilization/precipitation; texture; water-holding capacities; low-field nuclear magnetic resonance; microstructural characteristics Se investigaron los efectos de los contenidos de NaCl (0%, 0,5%, 1%, 1,5% y 2%) en la textura, capacidad de retención del agua y microestructuras de los geles inducidos por calor elaborados a partir de proteínas de pechuga de pollo mediante solubilización/precipitación isoeléctrica (geles ISPC). Las características del agua durante el calentamiento fueron también dilucidas mediante relaxometría T 2 por resonancia magnética nuclear de baja intensidad. Los geles ISPC con mayor contenido de NaCl exhibieron una buena textura y una menor pérdida de volumen en el cocinado, aunque una mayor pérdida centrífuga. La cantidad de agua libre (componente T 22 ) que se convirtió en agua inmovilizada (componente T 21 ) aumentó cuando se le añadió NaCl de acuerdo con la reducción de la pérdida de volumen en el cocinado. Sin embargo, los valores T 21 con aumento de 1,5% y 2% en el contenido de NaCl indicaron que el agua estaba ligeramente vinculada a las macromoléculas y era altamente móvil. Estos resultados fueron corroborados ampliamente por las imágenes de la microstructura que ilustraron que los geles ISPC que contenían un 1% de NaCl mostraban una estructura continua y densa con pequeños poros y hilos ligeramente entrecruzadas entre sí, los cuales obtuvieron el menor volumen total de pérdida de agua.Palabras clave: proteínas de pechuga de pollo; solubilización/precipitación isoeléctrica; textura; capacidad de retención de agua; resonancia magnética nuclear de baja intensidad; características microestructurales

show abstract

Manipulating the Self‐Assembly of Multicomponent Low Molecular Weight Gelators (LMWGs) through Molecular Design

et al. 2022

View full text Add to dashboard Cite

Multicomponent low molecular weight gelators (LMWGs) may self‐assemble by co‐assembly (CA), social self‐sorting (SSS), or narcissistic self‐sorting (NSS). Understanding the nuances of the self‐assembly processes is important to predict the behavior of multicomponent organogels. Here, we investigate the effect of molecular structure on self‐assembly in a series of amino‐acid based bicomponent LMWGs that differ in headgroup and alkyl chain length. Packing preference of the organogels was determined using differential scanning calorimetry, nuclear magnetic resonance spectroscopy and small angle X‐ray scattering. From 66 bicomponent samples we found 50 CA, 14 SSS and 2 NSS. Furthermore, we performed statistical analysis to investigate the role of hydrophobicity and chain length on the overall pathway of self‐assembly for these systems. We found the hydrophobicity of the headgroup strongly affected the assembly preference of the organogel, but alkyl chain length only played a small role.

show abstract

Low-field NMR study of heat-induced gelation of pork myofibrillar proteins and its relationship with microstructural characteristics

Cited by 336 publications

References 41 publications

Gelling properties of myosin as affected by L-lysine and L-arginine by changing the main molecular forces and microstructure

Gelling properties of myosin as affected by L-lysine and L-arginine by changing the main molecular forces and microstructure

Effects of NaCl on water characteristics of heat-induced gels made from chicken breast proteins treated by isoelectric solubilization/precipitation

Manipulating the Self‐Assembly of Multicomponent Low Molecular Weight Gelators (LMWGs) through Molecular Design

Contact Info

Product

Resources

About