Gelation properties of chicken myofibrillar protein induced by transglutaminase crosslinking

Sun, Xiang Dong; Arntfield, Susan D.

doi:10.1016/j.jfoodeng.2011.06.019

Cited by 42 publications

(23 citation statements)

References 28 publications

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“…Enzim ilavesi köftelerin pişirme kayıplarında azalmaya neden olmuş ve bu azalma enzim katılmayan grup ile %1 enzim ilaveli grup arasında TGaz enzimi üzerine yapılan çalışmaların sonucunda elde edilen en önemli bulgular, ürünlerin tekstür ve jel kuvvetindeki meydana gelen artışlardır. TGaz ilavesinin, moleküller arası ε (γ-glutamil)-lisil çapraz bağlarının oluşumu yoluyla daha sıkı jel ağ yapısına neden olduğu birçok araştırmada bildirilmektedir 9,[23][24][25][26] . Araştırmamızda da bu durum net bir şekilde ortaya konmuştur.…”

Section: Tartişma Ve Sonuçunclassified

Transglutaminaz Enziminin Tavuk Köftesinin Kalite Özelliklerine Etkisi

Uran

Aksu²,

Yılmaz³

et al. 2013

Kafkas Univ Vet Fak Derg

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ÖzetTransglutaminaz enzimi katılarak işlenmiş gıdaların, başta tekstür olmak üzere çeşitli kalite özelliklerinde gelişmeler olduğu farklı kaynaklarda belirtilmektedir. Bu çalışmada, tavuk göğüs etinden köfte üretimi yapılmıştır. Yapılan köfteler biri kontrol olmak üzere üç gruba ayrılmıştır. 1. grup kontrol grubu olup, enzim kullanılmamıştır. 2. grup köftelerde %0.5, 3. grup köftelerde ise %1 enzim ilavesi yapılmıştır. Bu köftelerin fiziksel, kimyasal ve duyusal özelliklerinin belirlenmesi amacıyla analizler yürütülmüştür. Bulgulara göre, enzim ilave edilen ve edilmeyen köftelerde kül, yağ, protein miktarı, renk özellikleri (L, a, b değerleri) ve duyusal açıdan farklılık olmadığı (P>0.05); %1 enzim ilavesi yapılan köftelerde, diğer köftelere göre kurumadde miktarının yükseldiği (P<0.05) ve enzim katkılı köftelerde kontrol grubuna göre pH değerinde düşme olduğu (P<0.05) saptanmıştır. Bununla birlikte enzim katkısının köftelerde pişirme kaybını azalttığı (P<0.05) tespit edilmiştir. Ayrıca, köftelerde yapılan tekstür analizi sonuçlarına göre, enzim katkısının köftelerin tekstürünü önemli ölçüde arttırdığı (P<0.01) gözlenmiştir. Anahtar sözcükler: Transglutaminaz, Tavuk köftesi, Kalite Effect of Transglutaminase on the Quality Properties of Chicken Breast Patties SummaryTransglutaminase enzyme is known to improve the textural and several other quality properties of food. In this study, patties were produced from chicken breast and dividend into three groups. The first group was not treated by transglutaminase and called as control samples. The second and third group patty samples were treated by 0.5% and 1% transglutaminase, respestively. Physical, chemical and sensory properties of the control and transglutaminase treated patty samples were studied.The transglutaminase treatment did not significantly affect the ash, lipid, protein content, colour properties (L, a, b values) and sensory properties of chicken breast patties compared to the control samples (P>0.05). However, dry matter content of the 1% enzyme treated samples was significantly (P<0.05) higher than the control and 0.5% transglutaminase treated samples. On the other hand, the pH of enzyme treated patties was found to be lower than the control samples. In addition, the transglutaminase treatments were significantly (P<0.05) effective in reducing the cooking loss and significantly improved the textural properties of the chicken breast patties (P<0.01).

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Section: Tartişma Ve Sonuçunclassified

Transglutaminaz Enziminin Tavuk Köftesinin Kalite Özelliklerine Etkisi

Uran

Aksu²,

Yılmaz³

et al. 2013

Kafkas Univ Vet Fak Derg

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“…TGase supplementation was reported to provide firmer and tighter gel net formation through intermolecular ε (γ-glutamyl)-lysyl cross bindings (Nio et al, 1986;Tseng et al, 2000;Soares et al, 2004;Yokoyama et al, 2004;Sun & Arntfield, 2011;Bourneow et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

A research on determination of quality characteristics of chicken burgers produced with transglutaminase supplementation

Uran

Yılmaz

2017

Food Sci. Technol

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Transglutaminases are enzymes that catalyze the cross-linking between peptides or proteins. They play an important role in heat stability, gel-formation capability, water-holding capacity, emulsification and nutritional properties of proteins. They are preferred in the use of a variety of meat products due to the binding properties. In this study the effect of transglutaminase on the quality characteristics of chicken burgers were investigated. The enzyme was added at 5 different concentrations (0.2%, 0.4%, 0.6%, 0.8% and 1%) and the other treatments applied in burger production were followed. After the product was formed, it was left in the cold for a while and then analyses were carried out. According to the results, the enzyme contribution did not cause changes in the nutritional items (ash, fat, protein) of the product groups. However, there was a significant decrease in the cooking loss and a significant increase in the texture values in the groups in which the enzyme amount was increased. Although the texture of the products have been increased, the transglutaminase treatment did not effect sensory parameters of burgers compared to the control samples. Scanning Electron Microscopy (SEM) images also supported to the texture values of samples with the increase of cross-linking in microstructure.Keywords: transglutaminase; chicken burger; quality; textural properties; microstructure.Practical Application: The transglutaminase enzyme is able to reduce cooking loss by improving the textural properties of chicken burgers.

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“…When heated to 65°C, the short rods of the knobby-surface myofibrillar fragments (Iwasaki, Washio, & Yamamoto, 2005a) assembled themselves in order into a dense gel matrix with smaller holes in it, most likely because of the compact and extensive cross-links (Figure 3(e)). Some studies showed that myosins or myofibrils in 0.6 mol/L NaCl or KCl could form good three dimensional network gels (Ishioroshi, Samejima, Arie, & Yasui, 1980;Morita, Choe, Yamamoto, Samejima, & Yasui, 1987;Sun & Arntfield, 2011;Xiong, 1992). Shimada, Takai, Ejima, Arakawa and Shiraki (2015) hypothesized that the dissociation of soluble filaments and thermal unfolding at high temperature, which resulted in the formation of soluble oligomers and binding interactions, provided new potential mechanics insight into the heat-induced myosin gelation in high-salt solution, while Hermansson et al (1986) and Tornberg (2005) found that coarsely aggregated myosin gel structures were formed in 0.6 mol/L.…”

Section: Microstructures Of Myofibrillar Gel From Rabbit Pm Using Semmentioning

confidence: 99%

“…And during cooling, the gradual increase suggested that slow continued hydrogen bonds occurred, which was important in stabilization of bound water and increasing gel strength by their great numbers (Lanier et al, 2013;Sun & Arntfield, 2011).…”

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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Gelation properties of chicken myofibrillar protein induced by transglutaminase crosslinking

Cited by 42 publications

References 28 publications

Transglutaminaz Enziminin Tavuk Köftesinin Kalite Özelliklerine Etkisi

Transglutaminaz Enziminin Tavuk Köftesinin Kalite Özelliklerine Etkisi

A research on determination of quality characteristics of chicken burgers produced with transglutaminase supplementation

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

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