Heat-induced gel properties of porcine myosin in a sodium chloride solution containing L-lysine and L-histidine

Zhang, Yawei; Wu, Junjun; Jamali, Muneer Ahmed; Guo, Xiuyun; Peng, Zengqi

doi:10.1016/j.lwt.2017.06.059

Cited by 40 publications

(29 citation statements)

References 34 publications

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“…At a 100% level of substitution, the WHC was not significantly different from the 0%, 25% and 75% replacement (P> 0.05). This positive result was considered to be due to the introduction of L-his and L-lys into the salt substitute, as it has been reported L-his and/or L-lys enhanced the WHC of porcine myosin gels (Zhang, Wu, Jamali, Guo, & Peng, 2017) and chicken breast myofibril gel (Chen et al, 2016). L-His could dissociate myosin filament and increase the solubility of myosin at low ionic strength solution (Hayakawa et al, 2009;Hayakawa, Ito, Wakamatsu, Nishimura, & Hattori, 2010), which affected intermolecular interactions (Chen et al, 2014) and increased water entrapment of myofibrils.…”

Section: Water Holding Capacity (Whc)mentioning

confidence: 94%

Effects of substitution of NaCl with KCl, L-histidine, and L-lysine on instrumental quality attributes of cured and cooked pork loin

Zhang

Guo

Liu

et al. 2018

CyTA - Journal of Food

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This study evaluated the effect of substituting of NaCl with varying amounts of a combination of KCl, L-histidine (L-his), and L-lysine (L-lys) on the instrumental characteristics of cooked loin. Fifteen cooked loins were produced by replacing 0%, 25%, 50%, 75% and 100% of NaCl with the salt substitute. Experiments were conducted in triplicate to determine the water-holding capacity (WHC), and T 2 relaxation time, and a texture profile analysis (TPA) and color determination test were also performed. T 2 relaxation time analysis indicated that substitution affected the distribution of water by increasing the proportion of immobilized water and improving the WHC. results of TPA and color tests showed no adverse effect from using the experimental treatments. Results showed that 50% was the most suitable substitution ratio (actual 30.15% subsitution level of NaCl), for which the Na content was approximately 27% lower than that of the control for cooked loin. Efectos de sustituir NaCl con KCl, L-histidina y L-lisina en los atributos de calidad instrumental del lomo de cerdo curado y cocido RESUMEN El presente estudio evaluó el efecto que provoca la sustitución del NaCl con cantidades variables de una combinación de KCl, L-histidina (L-his) y L-lisina (L-lys) en las características instrumentales del lomo cocido. Para ello se prepararon 15 lomos cocidos, remplazando 0%, 25%, 50%, 75% y 100% del NaCl con sustituto de sal. Los experimentos fueron realizados en triplicado para determinar la capacidad de retención de agua (WHC) y el tiempo de relajación T 2 ; además, se practicó un análisis de perfil de textura (TPA) y una prueba de determinación de color. El análisis del tiempo de relajación T 2 indicó que la sustitución afecta la distribución de agua al elevar la proporción de agua inmovilizada y mejorar la WHC. Los resultados del TPA y las pruebas de color no mostraron efectos adversos con el uso de tratamientos experimentales. Asimismo, los resultados dieron cuenta de que la ratio de sustitución de 50% es la más apropiada (nivel de sustitución real de 30.15 de NaCl), en la que el contenido de Na fue aproximadamente 27% más bajo que en el lomo cocido de control.

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Section: Water Holding Capacity (Whc)mentioning

confidence: 94%

Effects of substitution of NaCl with KCl, L-histidine, and L-lysine on instrumental quality attributes of cured and cooked pork loin

Zhang

Guo

Liu

et al. 2018

CyTA - Journal of Food

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“…The storage modulus (G') is a measure of gel's ability to be non-permanently deformed, and it is often employed to characterize a transition from viscous protein paste to a solid (Tahergorabi & Jaczynski, 2012a). The G' change rate was calculated by ΔG' = (G 1ʹ -G 0ʹ )/G 0ʹ , where G 1ʹ is the G' at 85°C and G 0ʹ is the G' at 25°C (Zhang, Wu, Jamali, Guo, & Peng, 2017). It was observed that the ΔG'of SS treatments was 135.53%, 144.54% and 248.73% more than that of NaCl treatments at 0.4 mol/L, 0.6 mol/L and 0.8 mol/L, respectively.…”

Section: Dynamic Rheological Property Of Myosinmentioning

confidence: 99%

Influence of salt substitute containing KCl, L-histidine and L-lysine on the secondary structure and gel properties of myosin

Zhang

Jamali

Peng

2019

CyTA - Journal of Food

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The effect of a salt substitute (SS) containing L-lysine (Lys) and L-histidine (His) on secondary structure and gel properties of myosin from grass carp was examined. The results indicated that the α-helix content of myosin treated with SS was 29.00%, 29.03% and 35.93% more than that with NaCl at 0.4, 0.6 and 0.8 mol/L (P < 0.05), respectively, suggesting that some fractions of the β-sheet, β-turn and random coil were transformed into α-helix. A similar pattern of storage modulus (G') was found between NaCl and SS treatments, and the G' of SS treatments at the end of gelation completion was higher than that of NaCl treatments. The salt substitute improved the gel strength and hardness of myosin at 0.4, 0.6 and 0.8 mol/L. The results indicated that the changes in secondary structure and gel properties of myosin may be mainly due to the L-lys and/or L-his in salt substitute.Influencia de un sustituto de sal que contiene KCl, L-histina y L-lisina en la estructura secundaria y las propiedades gelatinosas de la miosina RESUMEN El presente estudio examinó el efecto que tiene un sustituto de la sal (SS) que contiene L-lisina (Lys) y L-histidina (His) en la estructura secundaria y las propiedades gelatinosas de la miosina extraída de carpas herbívoras (Ctenopharyngodon idella). Los resultados dan cuenta de que el contenido de hélice-α de la miosina tratada con SS es 29.00%, 29.03% y 35.93% superior al del que contiene NaCl en concentraciones de 0.4, 0.6 y 0.8 mol/L (P < 0.05), respectivamente. Ello sugiere que algunas fracciones de la lámina-β, el giro-β y la espiral aleatoria se transformaron en una hélice-α. Además, entre los tratamientos con NaCl y SS se detectó un patrón similar en el módulo de almacenamiento (G'); el G' correspondiente a los tratamientos con SS al final de la gelificación fue más elevado que el de los tratamientos con NaCl. El sustituto de la sal mejoró la fuerza gelatinosa y la dureza de la miosina a 0.4, 0.6 y 0.8 mol/L. Estos resultados indican que los cambios en la estructura secundaria y en las propiedades gelatinosas de la miosina pueden responder principalmente a la L-lys y/o la L-his en el sustituto de la sal. ARTICLE HISTORY PALABRAS CLAVE bajo contenido de sodio; aminoácido; miosina KEYWORDS Low sodium; amino acid; myosin CONTACT Yawei Zhang

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“…Recently, the application of amino acids as gelation enhancers has attracted considerable attention. Amino acids such as arginine, cysteine, histidine, lysine, proline, and γ-aminobutyric acid (Cando, Herranz, Borderías, & Moreno, 2016;Liu et al, 2015;Primacella, Fei, Acevedo, & Wang, 2018;Wang, Liu, Ma, & Zhao, 2019;Wang, Zhao, Liu, & Li, 2019;Zhang, Wu, Jamali, Guo, & Peng, 2017) have been reported to improve gelling properties of a myriad of food protein gels. Among these novel additives, basic amino acids, particularly lysine and arginine, have been studied extensively.…”

Section: Introductionmentioning

confidence: 99%

“…Adding basic amino acids resulted in gels with improved water holding capacity, viscoelasticity and texture profile, and sensory attributes (Cando et al, 2016;Hayakawa et al, 2012;Lei, Fu, Xu, Zheng, & Zhou, 2016;Qin, Xu, Zhou, & Wang, 2015;Zhang et al, 2017;Zhou, Li, Tan, & Sun, 2014;Zhu et al, 2018). The underlying mechanisms include pH modulation, reduced water mobility, increased protein solubility, suppressed protein aggregation, altered protein thermal stability, facilitated protein unfolding and exposure of buried hydrophobic groups and sulfhydryls, and formation of a fine gel network (Cando et al, 2016;Chen et al, 2016;Fu et al, 2017;Gao, Wang, Mu, Shi, & Yuan, 2018;Guo, Peng, Zhang, Liu, & Cui, 2015;Hayakawa et al, 2012;Lei et al, 2016;Lei et al, 2017;Li et al, 2019;Qin et al, 2015;Zhang et al, 2017;Zhou, Li, Tan, & Sun, 2014). In addition, basic amino acids can improve emulsion stability Zhu et al, 2018), inhibit lipid and protein oxidation , and stabilize heme color Zhou, Li, Tan, & Sun, 2014;Zhou, Ye, Nishiumi, Qin, & Chen, 2014;Zhou, Ye, Wang, Qin, & Li, 2015), and are particularly useful in emulsified gel systems such as sausages.…”

Section: Introductionmentioning

confidence: 99%

“…Although extensive evidence has demonstrated that basic amino acids are effective in improving quality of muscle protein gels (Fu et al, 2017;Hayakawa et al, 2012;Lei et al, 2016;Lei et al, 2017;Qin et al, 2015;Zhang et al, 2017), egg yolk gel (Primacella et al, 2018), and complex gel systems such as sausages Zhou, Li, Tan, & Sun, 2014;Zhu et al, 2018), surimi (Cando et al, 2016), and cheese (Felicio et al, 2016), to the best of our knowledge, no study has investigated the effect of basic amino acids on gelling properties of whey protein isolate (WPI) gels. WPI is a widely used gelling and thickening agent in a variety of foods such as processed meat, bakery products, and dairy products (Havea, Watkinson, & Kuhn-Sherlock, 2009).…”

Section: Introductionmentioning

confidence: 99%

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Modification of heat-induced whey protein gels by basic amino acids

et al. 2020

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Various amino acids have been studied as gelation enhancers. This study investigated the effect of histidine, lysine, and arginine on gelling properties of heat-induced whey protein isolate (WPI) gels at different pHs. Basic amino acids modified WPI gels in a pH-and amino aciddependent manner. Hardness and gumminess of the WPI gel was improved by arginine at pH 7.59 while springiness was enhanced by histidine at pHs 7.59 and 9.74 and by lysine at pH 7.59 (P < 0.05). At pH 2.0, WPI formed a weak gel. Lysine and arginine facilitated β-lactoglobulin cross-linking at pH 2.0 and reduced protein leach out from the gel (P < 0.05). At pH 5.2, WPI formed a particulate gel with poor water holding capacity (WHC). Lysine improved WHC of the WPI gel at pH 5.2 by changing the structure of the gel network. At pHs away from 5.2, basic amino acid treatments resulted in a more uniform and porous gel matrix and a greater WHC (P < 0.05). In conclusion, different basic amino acids may be applied as WPI gel enhancers depending on the pH and desired attributes of the product.

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Heat-induced gel properties of porcine myosin in a sodium chloride solution containing L-lysine and L-histidine

Cited by 40 publications

References 34 publications

Effects of substitution of NaCl with KCl, L-histidine, and L-lysine on instrumental quality attributes of cured and cooked pork loin

Effects of substitution of NaCl with KCl, L-histidine, and L-lysine on instrumental quality attributes of cured and cooked pork loin

Influence of salt substitute containing KCl, L-histidine and L-lysine on the secondary structure and gel properties of myosin

Modification of heat-induced whey protein gels by basic amino acids

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