Abstract
Studied, the inhibitory effect of DS on thermal aggregation of tilapia myosin (2.0 mg/mL) in low ionic strength (1, 50, 150 mmol/L KCl) during the heat treatment (40～80 ℃, 1 ℃/min). The result showed that the myosin had poor solubility in 1 mmol/L KCl. While, with the icreased of ionic strengths, myosin fibrils could dissociate in 50 and 150 mmol/L KCl. After heating, the myosin filaments disappeared, and the heads and tails of myosin aggregated seriously, resulting in the solubility and the content of α-helix decreased significantly. After adding 0.4 mg/mL DS, the change of turbidity, solubility and α-helix content was not obvious in the range of 40～80 ℃. Compared to the samples without DS, the solubility, ζ-potential were higher at the same temperature (P＜0.05). The results suggested that the strong electrostatic interaction between DS and myosin can effectively inhibit the thermal denaturation of myosin under low ionic strength.
Publication Date
12-28-2018
First Page
5
Last Page
10
DOI
10.13652/j.issn.1003-5788.2018.12.001
Recommended Citation
Ting, LI; Chunxia, ZHOU; Rui, FENG; and Pengzhi, HONG
(2018)
"Inhibition of heat-induced aggregation of Tilapia myosin by dextran sulfate at low ionic strength,"
Food and Machinery: Vol. 34:
Iss.
12, Article 1.
DOI: 10.13652/j.issn.1003-5788.2018.12.001
Available at:
https://www.ifoodmm.cn/journal/vol34/iss12/1
References
[1] LANIER T C, CARVAJAL P, YONGSAWATDIGUL J, et al. Surimi gelation chemistry[M]. 3rd ed. Boca Raton: CRC Press, 2013: 435-489.
[2] WANG Guan, LIU Man-man, CAO Li-wei, et al. Effects of different NaCl concentrations on self-assembly of silver carp myosin[J]. Food Bioscience, 2018, 24: 1-8.
[3] KUROIWA T, KOBAYASHI I, CHUAH A M, et al. Formulation and stabilization of nano-/microdispersion systems using naturally occurring edible polyelectrolytes by electrostatic deposition and complexation[J]. Advances in Colloid & Interface Science, 2015, 226(Pt A): 86-100.
[4] SNCHEZ M, ARANDA F J, ESPUNY M J, et al. Thermodynamic and structural changes associated with the interaction of a dirhamnolipid biosurfactant with bovine serum albumin[J]. Langmuir the Acs Journal of Surfaces & Colloids, 2008, 24(13): 6 487-6 495.
[5] ZARAGOZA A, TERUEL J A, ARANDA F J, et al. Interac-tion of a Rhodococcus sp. trehalose lipid biosurfactant with model proteins: thermodynamic and structural changes[J]. Langmuir the Acs Journal of Surfaces & Colloids, 2012, 28(2): 1 381-1 390.
[6] TAKAI E, YOSHIZAWA S, EJIMA D, et al. Synergistic solubilization of porcine myosin in physiological salt solution by arginine[J]. International Journal of Biological Macromolecules, 2013, 62(11): 647-651.
[7] GAO Rui-chang, WANG Yan-ming, MU Jian-lou, et al. Effect of L-histidine on the heat-induced aggregation of bighead carp (Aristichthys nobilis) myosin in low/high ionic strength solution[J]. Food Hydrocolloids, 2018, 75: 174-181.
[8] 时娇娇. 蛋白稳定剂对罗非鱼肌球蛋白热变性聚集的抑制及机理[D]. 湛江: 广东海洋大学, 2016.
[9] 石彤. 氨基酸对花鲢肌球蛋白热聚集行为影响的研究[D]. 镇江: 江苏大学, 2017: 18-24.
[10] BONGKOSH V, UMUT Y, JOHNN C, et al. Interactions between β-lactoglobulin and dextran sulfate at near neutral pH and their effect on thermal stability[J]. Food Hydrocolloids, 2009, 23(6): 1 511-1 520.
[11] CHUNG K, KIM J, CHO B K, et al. How does dextran sulfate prevent heat induced aggregation of protein? The mechanism and its limitation as aggregation inhibitor[J]. Biochimica Et Biophysica Acta, 2007, 1 774(2): 249-257.
[12] 洪伟. pH值条件诱导鳄蛇鲻肌球蛋白分子展开/折叠行为的研究[D]. 湛江: 广东海洋大学, 2014: 10-11.
[13] LOWRY O H, ROSEBROUGH N J, FARR A L, et al. Protein measurement with the folin phenol reagent[J]. Journal of Biological Chemistry, 1951, 193(1): 265-275.
[14] 周春霞, 时娇娇, 付苇娅, 等. 赖氨酸和精氨酸对三种离子强度下罗非鱼肌球蛋白溶解度及构象的影响[J]. 现代食品科技, 2016(12): 99-104.
[15] OGAWA M, KANAMARU J, MIYASHITA H, et al. Alpha-helical structure of fish actomyosin: changes during setting[J]. Journal of Food Science, 1995, 60(2): 297-299.
[16] 施小迪, 郭顺堂. 稀释介质种类对豆乳蛋白胶体粒子zeta电位测定效果的影响[J]. 农业工程学报, 2016, 32(7): 270-275.
[17] HAYAKAWA T, ITO T, WAKAMATSU J, et al. Myosin filament depolymerizes in a low ionic strength solution containing L-histidine[J]. Meat Science, 2010, 84(4): 742-746.
[18] 范成成. 阴离子表面活性剂与无机盐相互作用的理论研究[D]. 青岛: 中国石油大学(华东), 2014: 14-19.
[19] DICKINSON E. Hydrocolloids at interfaces and the influence on the properties of dispersed systems[J]. Food Hydrocolloids, 2003, 17(1): 25-39.
[20] 赵晓阳, 李可, 邹玉峰, 等. 组氨酸与氯化钾混合液对兔肉肌球蛋白特性的影响[J]. 食品科学, 2014, 35(9): 6-10.
[21] CHEN Xing, ZOU Yu-feng, HAN Min-yi, et al. Solubilisation of myosin in a solution of low ionic strength L-histidine Significance of the imidazole ring[J]. Food Chemistry, 2016, 196: 42-49.
[22] SONG Xiao-zhou, ZHOU Cheng-jun, FU Feng, et al. Effect of high-pressure homogenization on particle size and film properties of soy protein isolate[J]. Industrial Crops & Products, 2013, 43(1): 538-544.
[23] 齐宝坤, 李杨, 王中江, 等. 不同品种大豆分离蛋白Zeta电位和粒径分布与表面疏水性的关系[J]. 食品科学, 2017, 38(3): 114-118.
[24] TENG Zi, LUO Yang-chao, WANG Qin. Nanoparticles synthesized from soy protein: preparation, characterization, and application for nutraceutical encapsulation[J]. Journal of Agricultural & Food Chemistry, 2012, 60(10): 2 712-2 720.
[25] LIU Ru, ZHAO Si-ming, YANG Hong, et al. Comparative study on the stability of fish actomyosin and pork actomyosin[J]. Meat Science, 2011, 88: 234-240.
[26] MASATO S, EISUKE T, DAISUKE E, et al. Heat-induced formation of myosin oligomer-soluble filament complex in high-salt solution[J]. International Journal of Biological Macromolecules, 2015, 73: 17-22.
[27] SALMINEN H, WEISS J. Electrostatic adsorption and stability of whey protein-pectin complexes on emulsion interfaces[J]. Food Hydrocolloids, 2014, 35(1): 410-419.