Effect of Regulation pH on the Conformation of Myosin from Common Carp at Low Ionic Strength

被引：0
|
作者：
Tian Y. [1 ]
Wang W. [1 ]
Song Y. [1 ]
Liu J. [1 ]
机构：
[1] College of Food Science and Engineering, Dalian Ocean University, Dalian, 116023, Liaoning
来源：
Journal of Chinese Institute of Food Science and Technology | 2019年 / 19卷 / 03期
关键词：
Cleavages site; Conformational; Myosin; PH-shift;
D O I：
10.16429/j.1009-7848.2019.03.010
中图分类号：
学科分类号：
摘要：
In this study, the effect of pH-shift on the conformation of myosin from common carp at low ionic strength was investigated. The results showed that the solubility of the myosin was over 90% at low ionic strength (0.05 mol/L KCl) and extreme acid-Alkali conditions (pH 2.5, pH 3.5, pH 11.5 and pH 12.5). After pH treatment, the Ca2+-ATPase in myosin was inactivated completely, and the recovery was impracticable even if at neutral pH again, it suggested that the head structure of myosin was already devastated. Circular dichroismspectroscopy analysis showed that the content of α-helix scarcely changed, which indicated that pH treatment had no effect on the tail structure of myosin. And we also found that after the process of different pH treatment, the tryptophan fluorescence of myosin was quenched, the surface hydrophobicity was increased, the sulfhydryl content was decreased and a change was induced at chymotrypsin cleavage sites, which indicated that the tertiary structure of myosin was changed. © 2019, Editorial Office of Journal of CIFST. All right reserved.
引用
收藏
页码：86 / 92
页数：6
相关论文
共 23 条
  • [1] Martin-Sanchez A.M., Navarro C., Perez-Alvarez J.A., Et al., Alternatives for efficient and sustainable production of surimi: a review, Comprehensive Reviews in Food Science and Food Safety, 8, 4, pp. 359-374, (2009)
  • [2] Wang H.N., Wu J., Betti M., Chemical, rheological and surface morphologic characterisation of spent hen proteins extracted by ph-shift processing with or without the presence of cryoprotectants, Food Chemistry, 139, 1-4, pp. 710-719, (2013)
  • [3] Omana D.A., Alkali-aided protein extraction from chicken dark meat: textural properties and color characteristics of recovered proteins, Poultry Science, 89, 5, pp. 1056-1064, (2010)
  • [4] Cavonius L.R., Albers E., Undeland I., pH-shift processing of nannochloropsis oculata, microalgal biomass to obtain a protein-enriched food or feed ingredient, Algal Research, 5, 22, pp. 95-102, (2015)
  • [5] Otto R.A., Beamer S., Jaczynski J., Et al., The effect of using citric or acetic acid on survival of Listeria monocytogenes, during fish protein recovery by isoelectric solubilization and precipitation process, Journal of Food Science, 76, 8, pp. 579-583, (2011)
  • [6] Xu Y., Xia W., Jiang Q., Et al., Acid-induced aggregation of actomyosinfrom silver carp (Hypophthalmichthys molitrix), Food Hydrocolloids, 27, 2, pp. 309-315, (2012)
  • [7] Paker I., Beamer S., Jaczynski J., Et al., pH shift protein recovery with organic acids on texture and color of cooked gels, Journal of the Science of Food & Agriculture, 95, 2, pp. 275-280, (2015)
  • [8] Tian Y., Wang W., Yuan C., Et al., Nutritional and digestive properties of protein isolates extracted from the muscle of the common carp using ph-shift processing, Journal of Food Processing & Preservation, 41, 1, (2017)
  • [9] Kristinsson H.G., Hultin H.O., Changes in conformation and subunit assembly of cod myosin at low and high pH and after subsequent refolding, Journal of Agricultural & Food Chemistry, 51, 24, pp. 7187-7196, (2003)
  • [10] Kato S., Konno K., Isolation of carp myosin rod and its structural stability, Nihon-suisan-gakkai-shi, 59, 3, pp. 539-544, (1993)
123