Scientia Agricultura Sinica ›› 2023, Vol. 56 ›› Issue (22): 4523-4531.doi: 10.3864/j.issn.0578-1752.2023.22.013

• FOOD SCIENCE AND ENGINEERING • Previous Articles     Next Articles

Mechanism of Hydration Environment/Magnetic Field Effects on the Oxidative Stability of Myoglobin

DENG YuShi1(), XIA MinQuan1(), MA Jing1, ZHOU YuanHua2, SUN WeiQing1()   

  1. 1 College of Life Science, Yangzte University, Jingzhou 434020, Hubei
    2 College of Mechanical Engineering, Yangzte University, Jingzhou 434020, Hubei
  • Received:2023-04-25 Accepted:2023-07-03 Online:2023-11-16 Published:2023-11-17


【Objective】To investigate the mechanism of action of hydration environment affecting the oxidative stability of myoglobin (Mb) in the presence of a magnetic field, and to provide a basis for improving the oxidative stability of Mb. 【Method】Two magnetic field environments of low intensity (3 mT) and high intensity (12 mT) were set up at 4 ℃, the magnetic field treated Mb aqueous solution, Mb powder, and deionized water (the magnetic field treated deionized water and then dissolved Mb), respectively, and the magnetic field treatment time was 1 h. The Mb aqueous solution without magnetic field treatment was used as the control. The oxidative stability properties of Mb were analyzed by the relative content of high iron myoglobin, heme iron content and the variation of UV absorption bands, while the changes of Mb secondary structure, tertiary structure and porphyrin iron structure were analyzed by circular dichroism, and Raman spectroscopy and fluorescence spectroscopy techniques were employed to investigate the mechanism of the effect of magnetic field on the oxidative stability of Mb. 【Result】Both magnetic field treatment of Mb powder directly and magnetic field treatment of solvent water followed by dissolution of Mb had no significant effect (P>0.05) on the relative content of methemoglobin, while both 3 mT and 12 mT magnetic field treatment of Mb aqueous solution significantly increased the relative content of methemoglobin. The results of heme iron content and heme Shore band UV absorption showed that the heme porphyrin ring structure was sensitive to the magnetic field environment, and the magnetic field of different intensities had significant damage to the Mb heme structure, while the high intensity magnetic field environment had relatively greater damage to the porphyrin ring structure. Mb tertiary and secondary structure results showed that both 3 mT magnetic field treatment of solvent water before dissolving Mb, and 3 mT and 12 mT magnetic field treatment of Mb aqueous solution significantly promoted the unfolding of Mb secondary structure and oxidative damage of tryptophan and tyrosine residues of side chain groups. Raman spectroscopy results showed that 12 mT magnetic field treatment of Mb aqueous solution induced the cross-linking of Mb through disulfide bonds. 【Conclusion】Hydration in Mb aqueous solution directly affected the effect of magnetic field on the oxidative properties of myoglobin, and magnetic field treatment promoted the oxidation of Mb central iron as well as heme porphyrin ring, probably because the magnetic field changes the physical properties of water molecules, such as dielectricity and degree of ionization, as well as the hydrogen bonding state between Mb and water, which further affected the structure of Mb with the unfolding of α-helix structure and the exposure of side chain groups, accelerating the destruction of heme structure and loss of heme iron, and promoting the oxidation of central iron.

Key words: myoglobin, magnetic field, hydrated environment, oxidation, porphyrin

Fig. 1

Relative content of high iron myoglobin of myoglobin samples Different lowercase letters indicate significant differences between samples (P<0.05). C indicate control; TA1, TA2 indicate Mb powders were treated with 3 mT and 12 mT magnetic fields and then dissolved in deionized water, respectively; TB1, TB2 indicate deionized water was treated with 3 mT and 12 mT magnetic fields and then the untreated Mb powder was dissolved, respectively; TC1, TC2 indicate Mb aqueous solution was treated by 3 mT and 12 mT magnetic field, respectively. The same as below"

Fig. 2

Oxidation Changes of myoglobin Samples in Different Treatments"

Fig. 3

Fluorescence spectra of myoglobin samples"

Fig. 4

Circular dichroism spectrum of myoglobin samples"

Fig. 5

Secondary structure of myoglobin samples"

Fig. 6

Raman spectrum analysis of myoglobin samples"

Table 1

Analysis of Raman spectroscopy on the intermolecular interactions of myoglobin"

处理 Treatment I1450/I1003 I1360/I1340 I850/I830 I759/I1003 I510/I1003
C 5.055±2.432ab 0.742±0.020a 0.882±0.077a 4.760±1.207b 1.651±0.448b
TA1 3.426±0.941b 0.673±0.018c 0.814±0.063a 3.744±0.131b 1.733±1.286b
TA2 5.886±1.783ab 0.721±0.016abc 0.853±0.065a 6.470±1.857ab 1.681±0.249b
TB1 4.708±0.349ab 0.707±0.004abc 0.825±0.052a 5.093±0.840b 2.573±2.616ab
TB2 13.706±6.107a 0.739±0.011ab 0.869±0.063a 15.035±7.358a 1.770±0.373b
TC1 9.287±2.048ab 0.725±0.042abc 0.806±0.053a 9.048±1.991ab 4.935±1.638ab
TC2 8.903±5.916ab 0.683±0.015bc 0.823±0.019a 14.269±2.708a 6.157±0.886a
SHE Z C, HU X, ZHAO X S, REN Z M, DING G J. FTIR investigation of the effects of ultra-strong static magnetic field on the secondary structures of protein in bacteria. Infrared Physics & Technology, 2009, 52(4): 138-142.
SILVA F L, ZIN G, REZZADORI K, LONGO L C, TIGGEMANN L, SANTOS SOARES L, CUNHA PETRUS J C, VLADIMIR DE OLIVEIRA J, DI LUCCIO M. Changes in the physico-chemical characteristics of a protein solution in the presence of magnetic field and the consequences on the ultrafiltration performance. Journal of Food Engineering, 2019, 242: 84-93.

doi: 10.1016/j.jfoodeng.2018.08.016
刘勇. 磁场对酶及酶促反应过程的影响[D]. 天津: 天津大学, 2007.
LIU Y. Effect of magnetic field on enzyme and enzymatic reaction process[D]. Tianjin: Tianjin University, 2007. (in Chinese)
于静波. 磁场对脂肪酶和纤维素酶的影响[D]. 天津: 天津大学, 2009.
YU J B. Effect of magnetic field on lipase and cellulase[D]. Tianjin: Tianjin University, 2009. (in Chinese)
ZHONG C W, WAKAYAMA N I. Effect of a high magnetic field on the viscosity of an aqueous solution of protein. Journal of Crystal Growth, 2001, 226(2/3): 327-332.

doi: 10.1016/S0022-0248(01)01269-6
SHOKROLLAHI S, GHANATI F, SAJEDI R H, SHARIFI M. Possible role of iron containing proteins in physiological responses of soybean to static magnetic field. Journal of Plant Physiology, 2018, 226: 163-171.

doi: S0176-1617(18)30168-8 pmid: 29778670
XIA M Q, CHEN Y X, MA J, YIN X L, WANG L, WU W J, XIONG G Q, SUN W Q, ZHOU Y H. Effects of low frequency magnetic field on myoglobin oxidation stability. Food Chemistry, 2020, 309: 125651.

doi: 10.1016/j.foodchem.2019.125651
XIA M Q, CHEN Y X, MA J, YIN X L, LI Z S, XIONG G Q, WANG L, WU W J, SUN W Q, ZHOU Y H. Low frequency magnetic fields modification on hydrogen peroxide oxidized myoglobin-isolate and mechanisms underlying the chain reaction process. Food Chemistry, 2020, 312: 126069.

doi: 10.1016/j.foodchem.2019.126069
ATEF M M, ABD EI-BASET M S, ELL-KAREEM A, AIDA S, FADEL M A. Effects of a static magnetic field on haemoglobin structure and function. International Journal of Biological Macromolecules, 1995, 17(2): 105-111.

pmid: 7547716
柳士鑫. 磁化水性质的变化对蛋白质分子和大肠杆菌蛋白质的影响[D]. 天津: 天津大学, 2007.
LIU S X. Effects of changes in properties of magnetized water on protein molecules and Escherichia coli protein[D]. Tianjin: Tianjin University, 2007. (in Chinese)
ZHENG J B, HAN Y R, GE G, ZHAO M M, SUN W Z. Partial substitution of NaCl with chloride salt mixtures: impact on oxidative characteristics of meat myofibrillar protein and their rheological properties. Food Hydrocolloids, 2019, 96: 36-42.

doi: 10.1016/j.foodhyd.2019.05.003
LIU R, LONERGAN S, STEADHAM E, ZHOU G H, ZHANG W G, HUFF-LONERGAN E. Effect of nitric oxide on myofibrillar proteins and the susceptibility to calpain-1 proteolysis. Food Chemistry, 2019, 276: 63-70.

doi: S0308-8146(18)31770-9 pmid: 30409642
UTRERA M, MORCUENDE D, ESTÉVEZ M. Fat content has a significant impact on protein oxidation occurred during frozen storage of beef patties. LWT - Food Science and Technology, 2014, 56(1): 62-68.

doi: 10.1016/j.lwt.2013.10.040
孙攀. 超声波处理对金枪鱼肌原纤维蛋白理化特性、结构和凝胶特性的影响[D]. 锦州: 渤海大学, 2019.
SUN P. Effects of ultrasonic treatment on physicochemical properties, structure and gel properties of tuna myofibrillar protein[D]. Jinzhou: Bohai University, 2019. (in Chinese)
TANG J, FAUSTMAN C, HOAGLAND T A. Krzywicki revisited: equations for spectrophotometric determination of myoglobin redox forms in aqueous meat extracts. Journal of Food Science, 2006, 69(9): C717-C720.
KRZYWICKI K. The determination of haem pigments in meat. Meat Science, 1982, 7(1): 29-36.

doi: 10.1016/0309-1740(82)90095-X pmid: 22055066
张同刚, 罗瑞明, 李亚蕾, 周亚玲. 基于拉曼光谱法测定冷鲜牛肉中肌红蛋白相对含量. 食品科学, 2018, 39(2): 210-214.

doi: 10.7506/spkx1002-6630-201802033
ZHANG T G, LUO R M, LI Y L, ZHOU Y L. Determination of myoglobin in chilled beef based on Raman spectroscopy. Food Science, 2018, 39(2): 210-214. (in Chinese)

doi: 10.7506/spkx1002-6630-201802033
冯哲, 陈辉, 郭丽萍, 熊双丽, 黄业传. 高压结合热处理对猪肉肌红蛋白的影响. 食品工业科技, 2016, 37(2): 160-164, 175.
FENG Z, CHEN H, GUO L P, XIONG S L, HUANG Y C. Effects of high pressure combined with thermal treatment on myoglobin in pork. Science and Technology of Food Industry, 2016, 37(2): 160-164, 175. (in Chinese)
BENJAKUL S, BAUER F. Biochemical and physicochemical changes in catfish (Silurus glanis Linne) muscle as influenced by different freeze-thaw cycles. Food Chemistry, 2001, 72(2): 207-217.

doi: 10.1016/S0308-8146(00)00222-3
WANG Z M, HE Z F, EMARA A M, GAN X, LI H J. Effects of malondialdehyde as a byproduct of lipid oxidation on protein oxidation in rabbit meat. Food Chemistry, 2019, 288: 405-412.

doi: S0308-8146(19)30492-3 pmid: 30902311
马君燕, 郑学仿, 郭明, 唐乾, 马静, 高大彬, 胡皆汉. 荧光法研究光诱导肌红蛋白的去氧过程. 中国科学B辑, 2008, 38(1): 55-59.
MA J Y, ZHENG X F, GUO M, TANG Q, MA J, GAO D B, HU J H. Study on photo-induced deoxygenation of myoglobin by fluorescence method. Scientia Sinica Chimica, 2008, 38(1): 55-59. (in Chinese)
ZOU Y, XU P P, WU H H, ZHANG M H, SUN Z L, SUN C, WANG D Y, CAO J X, XU W M. Effects of different ultrasound power on physicochemical property and functional performance of chicken actomyosin. International Journal of Biological Macromolecules, 2018, 113: 640-647.

doi: S0141-8130(18)30022-9 pmid: 29428384
BANERJEE S, CHAKRABORTI A S. Structural alterations of hemoglobin and myoglobin by glyoxal: A comparative study. International Journal of Biological Macromolecules, 2014, 66: 311-318.

doi: 10.1016/j.ijbiomac.2014.02.034 pmid: 24613676
ZHU Z H, WANG Y Q, KANG Y J, ZHANG H M, ZHANG Z M, FEI Z H, CAO J. Graphene oxide destabilizes myoglobin and alters its conformation. Carbon, 2017, 114: 449-456.

doi: 10.1016/j.carbon.2016.12.053
XIA M Q, CHEN Y X, GUO J J, FENG X L, YIN X L, WANG L, WU W J, LI Z S, SUN W Q, MA J. Effects of oxidative modification on textural properties and gel structure of pork myofibrillar proteins. Food Research International, 2019, 121: 678-683.

doi: S0963-9969(18)30984-0 pmid: 31108795
XIA W Y, MA L, CHEN X K, LI X Y, ZHANG Y H. Physicochemical and structural properties of composite gels prepared with myofibrillar protein and lecithin at various ionic strengths. Food Hydrocolloids, 2018, 82: 135-143.

doi: 10.1016/j.foodhyd.2018.03.044
LEDWARD D A. Post-slaughter influences on the formation of metyyoglobin in beef muscles. Meat Science, 1985, 15(3): 149-171.

doi: 10.1016/0309-1740(85)90034-8 pmid: 22054503
FAUSTMAN C, SUN Q, MANCINI R, SUMAN S P. Myoglobin and lipid oxidation interactions: Mechanistic bases and control. Meat Science, 2010, 86(1): 86-94.

doi: 10.1016/j.meatsci.2010.04.025 pmid: 20554121
ESTÉVEZ M, CAVA R. Lipid and protein oxidation, release of iron from heme molecule and colour deterioration during refrigerated storage of liver pâté. Meat Science, 2004, 68(4): 551-558.

doi: 10.1016/j.meatsci.2004.05.007 pmid: 22062531
PACE A D, CUPANE A, LEONE M, VITRANO E, CORDONE L. Protein dynamics. Vibrational coupling, spectral broadening mechanisms, and anharmonicity effects in carbonmonoxy heme proteins studied by the temperature dependence of the Soret band lineshape. Biophysical Journal, 1992, 63(2): 475-484.

pmid: 1420893
HERRERO A M. Raman spectroscopy for monitoring protein structure in muscle food systems. Critical Reviews in Food Science and Nutrition, 2008, 48(6): 512-523.

doi: 10.1080/10408390701537385 pmid: 18568857
ZHANG Z Y, YANG Y L, TANG X Z, CHEN Y J, YOU Y. Chemical forces and water holding capacity study of heat-induced myofibrillar protein gel as affected by high pressure. Food Chemistry, 2015, 188: 111-118.

doi: 10.1016/j.foodchem.2015.04.129 pmid: 26041172
王甜甜, 朱逸宸, 谢勇, 周凯, 廖鲜艳, 黄俊逸, 徐宝才. 肌红蛋白在加工贮藏过程中结构与功能特性的变化及其对肉制品色泽的影响研究进展. 食品科学, 2023, 44(3): 393-399.
WANG T T, ZHU Y C, XIE Y, ZHOU K, LIAO X Y, HUANG J Y, XU B C. Research progress on changes in structure and functional properties of myoglobin during processing and storage and their effect on the quality of meat products. Food Science, 2023, 44(3): 393-399. (in Chinese)

doi: 10.7506/spkx1002-6630-20220127-280
丁振瑞, 赵亚军, 陈凤玲, 陈金忠, 段书兴. 磁化水的磁化机理研究. 物理学报, 2011, 60(6): 432-439.
DING Z R, ZHAO Y J, CHEN F L, CHEN J Z, DUAN S X. Magnetization mechanism of magnetized water. Acta Physica Sinica, 2011, 60(6): 432-439. (in Chinese)
朱元保, 颜流水, 曹祉祥, 文陵飞, 陈宗璋. 磁化水的物理化学性能. 湖南大学学报, 1999, 26(1): 21-25, 32.
ZHU Y B, YAN L S, CAO Z X, WEN L F, CHEN Z Z. Physical and chemical properties of magnetized water. Journal of Hunan University, 1999, 26(1): 21-25, 32. (in Chinese)
费庆志. 磁化对水性能的影响. 大连铁道学院学报, 1998(1): 85-89.
FEI Q Z. Influence of water function by magnetizing. Journal of Dalian Railway Institute, 1998(1): 85-89. (in Chinese)
WANG Y K, WEI H N, LI Z W. Effect of magnetic field on the physical properties of water. Results in Physics, 2018, 8: 262-267.

doi: 10.1016/j.rinp.2017.12.022
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