| As people pay more attention to healthy diet,low sodium and low phosphorus meat products have become an important trend in the development of meat products.Amino acids have attracted more scholars’ attention because of their advantages of safety,health,low cost and the ability of improving the quality characteristics of meat products.The paper aimed at the effects of L-Arginine(L-Arg)/L-Lysine(L-Lys)on the extraction of salt-soluble meat proteins from chicken breast and the gelling properties of the corresponding protein extracts.On the basis of this,myosin with higher purity was taken as the research object to further investigate whether structural and micro environment changes were induced by L-Arg/L-Lys,and subsequently lead to the increased solubility of chicken myosin.Also,aromatic hydrophobic,reactive and total sulfhydryl content of myosin were investigate to comprehensive study the mechanism of L-Arg/L-Lys on the myosin solubility.The main results of the study were as follows:1.Effects of L-Arg/L-Lys on the extraction of salt soluble protein from chicken breast and its heat induced gelation properties of the corresponding protein.(1)The addition of L-Arg/L-Lys effectively promoted the extraction of protein.The results of SDS-PAGE further indicated that L-Arg/L-Lys mainly promoted the extraction of salt soluble protein.(2)DSC results showed that the protein extracted with L-Arg/L-Lys had three denaturation temperature points during heating,which corresponded to myosin head,myosin tail and / or sarcoplasmic protein and actin,respectively.(3)Rheological results showed that the protein extracted with L-Arg/L-Lys had four distinct temperature ranges during heating,and had a significantly higher G0 value in the whole process of heating and cooling.(4)The protein extracted with L-Arg/L-Lys had better thermal induced gel properties,and the corresponding gels showed obviously higher water holding capacity(WHC)and gel strength,but decreased cooking loss(CL).(5)SEM results showed that the protein extracted with L-Arg/L-Lys had better capacity to form a continuous three-dimensional network gel structure.The addition of L-Arg/L-Lys promoted the extraction of salt soluble protein from chicken breast and made the protein extracts have better heat induced gel properties,resulting in better WHC and texture properties.2.The effect of L-Arg/L-Lys on the solubility of myosin(1)Raman spectroscopy and Infrared spectroscopy analysis showed that the addition of L-Arg/L-Lys(0.05%,w/w)did not change the patterns of Infrared spectra and Raman spectra of myosin,However,the changes of myosin conformation and microenvironment are induced.Meanwhile,L-Arg/L-Lys can inhibit the aggregation of myosin,which leading to the increased myosin solubility.(2)The endogenous fluorescence spectroscopy analysis showed that the addition of L-Arg/L-Lys(0.05%,w/w)reduced the endogenous fluorescence intensity of myosin and led to a slight red shift of the wavelength of the maximum fluorescence(λmax).(3)Surface hydrophobicity analysis indicated that the myosin added with L-Arg/L-Lys(0.05%,w/w)showed obviously increased surface hydrophobicity content when use ANS as probe,but significantly decreased surface hydrophobicity content with PRODAN as probe.(4)The addition of L-Arg/L-Lys(0.05%,w/w)significantly increased the reactive sulfhydryl content of myosin,but showed insignificant changes in total sulfhydryl content.This results suggested that L-Arg/L-Lys may caused the degeneration and unfolding of myosin,resulting in more reactive sulfhydryl exposure.However,this process does not involve breakage or formation of the disulfide bonds.(5)The results of CD spectra showed that the addition of L-Arg/L-Lys(0.05%,w/w)reduced the a-helix content of myosin.The addition of L-Arg/L-Lys(0.05%,w/w)induces changes in myosin conformation and microenvironment,and inhibits myosin aggregation,resulting in the increased myosin solubility. |
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