Effects of l-lysine on thermal gelation properties of chicken breast actomyosin

Lei, Zhijun; Fu, Yuan; Zheng, Yangfan; Xu, Peng; Zhou, Cunliu

doi:10.1007/s10068-017-0081-7

Cited by 9 publications

(15 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…reported that the addition of basic amino acids can expose buried hydrophobic groups and reactive sulfhydryl groups and contribute to an enhanced protein gelation (Guo et al, 2015;Lei et al, 2016;Lei et al, 2017).…”

Section: Appearance and Color Of Wpi Gelsmentioning

confidence: 99%

“…The addition of basic amino acids modified the texture of the WPI gels. Several studies have demonstrated that basic amino acids strongly bind to the charged residues of proteins through electrostatic interactions, which alters the structure and thermal properties of the proteins and in turn affect their gelling properties (Guo et al, 2015;Lei et al, 2016;Lei et al, 2017;. Gel hardness and gumminess increased significantly (P < 0.05) at pH 7.59 when 0.5% arginine was added.…”

Section: Texture Profile Analysismentioning

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%

“…Since there are more effective and economic ways to adjust pH, we controlled the pH in the current investigation and examined the effectiveness of other mechanisms. Moreover, it is evident that the electrostatic interactions between the basic amino acids and the proteins play an important role in the gelling process (Cando et al, 2016;Lei et al, 2016;Lei et al, 2017). To uncover how the charge state would affect the efficacy of the basic amino acids and to test the versatility of the application at different pHs, we performed the experiments at pH 2.0 and at the isoelectric point (pI) of histidine (pH 7.59), lysine (pH 9.74), arginine (pH 10.76), and β-lactoglobulin (pH 5.2).…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

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

et al. 2020

View full text Add to dashboard Cite

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.

show abstract

Section: Appearance and Color Of Wpi Gelsmentioning

confidence: 99%

Section: Texture Profile Analysismentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

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

et al. 2020

View full text Add to dashboard Cite

show abstract

Improving the texture properties and protein thermal stability of Antarctic krill (Euphausia superba) by L‐lysinemarination

Lin

Zhang

et al. 2022

J Sci Food Agric

View full text Add to dashboard Cite

BACKGROUND: The quality deterioration of Antarctic krill (Euphausia superba) after thermal processing limits its industrial application. This study sought to improve the texture characteristics of Antarctic krill after heat treatment through pre-soaking using L-lysine (Lys) solution and sodium tripolyphosphate (STPP). Moreover, the effects of Lys on heat-treated Antarctic krill were explored.RESULTS: Lys significantly reduced the cooking loss and improved the texture characteristics of Antarctic krill during heat treatment. The low-field nuclear magnetic resonance results showed that Lys reduced the water loss of Antarctic krill during heat treatment. Additionally, the surface hydrophobicity, Fourier transform infrared spectroscopy, and endogenous fluorescence spectroscopy results showed that Lys could inhibit the structural damage of Antarctic krill protein under the thermal denaturation condition and enhance the thermal stability of the protein. The scanning electron microscopy results showed that Lys could protect the structural integrity of Antarctic krill muscle fibers during heat treatment.CONCLUSION: The cooking loss in the Lys added groups was better than the sodium tripolyphosphate added group, and 2.0% Lys solution could minimize the cooking loss of Antarctic krill. The secondary and tertiary structures of the Antarctic krill protein were actively protected by Lys during heat treatment. Overall, the study will provide insights into the application of Lys in the food industry as a natural additive and an alternative to phosphate.

show abstract

Mitigation of oxidation-induced loss of myofibrillar protein gelling potential by the combination of pyrophosphate and l-lysine

Cao

et al. 2022

LWT

View full text Add to dashboard Cite

Effects of l-lysine on thermal gelation properties of chicken breast actomyosin

Cited by 9 publications

References 25 publications

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

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

Improving the texture properties and protein thermal stability of Antarctic krill (Euphausia superba) by L‐lysinemarination

Mitigation of oxidation-induced loss of myofibrillar protein gelling potential by the combination of pyrophosphate and l-lysine

Contact Info

Product

Resources

About