Konjac flour improved textural and water retention properties of transglutaminase-mediated, heat-induced porcine myofibrillar protein gel: Effect of salt level and transglutaminase incubation

Chin, Koo Bok; Go, Mi Y.; Xiong, Youling L.

doi:10.1016/j.meatsci.2008.10.012

Cited by 126 publications

(93 citation statements)

References 34 publications

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“…The lower maximum δ and the higher initial G′ and the lower final gel strength in 0.2 mol/L KCl than the ones in 0.6 mol/L KCl ( Figure 4, Table 1) showed that the incomplete dissolution and denaturation of myofibrillar proteins in 0.2 mol/L KCl resulted in insufficient ordered aggregation to form a comprehensive and good gel network. At high ionic strengths, sufficient amounts of proteins were highly solubilized and diffused throughout the protein matrix, forming a better gel network with complete structural uniformity when compared with the MP gel formed in 0.3 mol/L NaCl (Chin, Go, & Xiong, 2009). Previous studies showed that higher ionic strength produced more elastic gels, and 0.6 mol/L KCl was the most commonly used ionic strength (Hermansson et al, 1986;Stone & Stanley, 1994).…”

Section: Rheological Properties Of Myofibril Solutions During Heatingmentioning

confidence: 99%

The mechanics of formation of heat-induced myofibrillar protein gel from rabbitpsoas major

Wei

Cui

Jamali

et al. 2016

CyTA - Journal of Food

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(2017) The mechanics of formation of heat-induced myofibrillar protein gel from rabbit psoas major, CyTA -Journal of Food, 15:2, 181-190, DOI: 10.1080/19476337.2016 To link to this article: https://doi.org/10. 1080/19476337.2016 The present study was designed to analyze the formation mechanics of heat-induced myofibrillar gels from rabbit psoas major at 0.6 mol/L KCl (pH 6.5) and 0.2 mol/L KCl (pH 6.0; n = 3). Morphological structure changes were observed using phase-contrast microscopy, transmission electron microscopy, scanning electron microscopy (SEM) and gel properties were determined through water-holding capacity (WHC), gel strength and dynamic rheological test. The results revealed that myofibrillar filaments aggregated and formed larger oligomers by side-by-side interactions when heated from 25 to 65°C. In higher ionic strength at higher pH, the filaments formed a more compact homogeneous network structure and the G′ value was much lower with higher WHC and gel strength, suggesting that the myofibril gel properties could be described by ΔG′. Based on the present study, it is suggested that the desired structural and textural attributes of myofibril gel can be manipulated by temperature, ionic strength and pH.El mecanismo de la formación de gel proteínico miofibrilar inducido con calor de psoas mayor de conejo RESUMEN El presente estudio se diseñó para analizar la formación de los mecanismos de geles miofibrilares inducidos con calor de psoas mayor de conejo (PM) a 0,6 mol/L de KCl (pH 6,5) y 0,2 mol/L de KCl (pH 6,0) (n=3). Se observaron cambios en la estructura morfológica utilizando microscopio de contraste de fase, microscopio electrónico de transmisión (TEM) y microscopía electrónica de barrido (SEM), además se determinaron las propiedades del gel examinando la capacidad de retención de agua, la resistencia del gel y el ensayo reológico dinámico. Los resultados revelaron que los filamentos miofibrilares agregaron y formaron oligómeros más grandes mediante interacciones conjuntas cuando se calentaron de 25°C a 65°C. Con la mayor fuerza iónica y el mayor pH, los filamentos formaron una estructura de red homogénea más compacta y el valor G' fue más bajo con los mayores valores de WHC y resistencia del gel, sugiriendo que las propiedades miofibrilares del gel podrían describirse con ΔG'. En base al presente estudio, se sugiere que los atributos estructurales y texturales deseados del gel miofibrilar pueden ser manipulados con la temperatura, la fuerza iónica y el pH.

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Section: Rheological Properties Of Myofibril Solutions During Heatingmentioning

confidence: 99%

The mechanics of formation of heat-induced myofibrillar protein gel from rabbitpsoas major

Wei

Cui

Jamali

et al. 2016

CyTA - Journal of Food

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“…The capability of the protein gels to retain moisture was determined by measuring cooking, centrifugal, and total water loss using the methods presented by Chin, Go, and Xiong (2009) and Li, Kang, Zhao, Xu, and Zhou (2014), with slight modifications.…”

Section: Determination Of Whcmentioning

confidence: 99%

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

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(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

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“…Frozen cubed meat samples were thawed at 4 o C overnight, and MP was extracted according to a previously published method by Xiong (1993) with minor modifications (Chin et al, 2009). Minced meat was washed three times with 4 vol.…”

Section: Extraction Of Myofibrillar Protein (Mp)mentioning

confidence: 99%

“…It was generally accepted that microbial transglutaminase (TG) and calcium alginate (CA) were the useful cold-set gelling agents (Boles and Shand, 1998;Kuraish et al, 1997). The effects of TG on cold-set myofibrillar protein (MP) gelation showed some contradictions depending on several factors such as potential substrate sources, salt concentration, pH, muscle type, processing time and temperature (Anema et al, 2005;Chin et al, 2009;Kuraish et al, 1997;Kütemeyer et al, 2005). Among potential substrate sources, MPs definitely acted as a substrate for TG, while the quantity of substances contributing to TG activation in MPs, e.g., troponin, were not enough to activate TG (Bergamini et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

Optimisation of Calcium Alginate and Microbial Transglutaminase Systems to form a Porcine Myofibrillar Protein Gel

Hong¹,

Chin²

2009

Korean Journal for Food Science of Animal Resources

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The aim of this study was to model and optimize the calcium alginate (CA) and microbial transglutaminase (TG) systems to form a cold-set myofibrillar protein (MP) gel containing 0.1 M or 0.3 M NaCl using a response surface methodology. The gel strengths of cold-set and heat-induced MP gels, and cooking yields were measured. All measured parameters showed determination coefficients (R 2 ) above 0.7 without a lack-of-fit. The CA system had the best results with component ratios of 1.0:0.3:1.0 corresponding to sodium alginate, calcium carbonate and glucono-δ-lactone, respectively, and was favourable at 0.1 M NaCl. In contrast, the TG system only had an effect on cold-set MP gelation at 0.3 M salt, and the optimal ratio of TG to sodium caseinate was 0.6:0.5. By combining the two systems at 0.3 M NaCl, an acceptable cold-set MP gel with an improved texture and high cooking yield could be formed. Therefore, these results indicated that the functionality of the cold-set MP gel could be enhanced by combining these two optimized gelling system.

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Konjac flour improved textural and water retention properties of transglutaminase-mediated, heat-induced porcine myofibrillar protein gel: Effect of salt level and transglutaminase incubation

Cited by 126 publications

References 34 publications

The mechanics of formation of heat-induced myofibrillar protein gel from rabbitpsoas major

The mechanics of formation of heat-induced myofibrillar protein gel from rabbitpsoas major

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

Optimisation of Calcium Alginate and Microbial Transglutaminase Systems to form a Porcine Myofibrillar Protein Gel

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