Food and Fermentation Industries >

2020 , Vol. 46 >Issue 20: 1 - 8

DOI: https://doi.org/10.13995/j.cnki.11-1802/ts.024414

Effects of different ultrasound-assisted thawing methods on the myofibrillar protein of the sea bass (Perca fluviatilis)

  • CAI Luyun ,
  • XU Qing ,
  • CAO Ailing
Expand
  • 1(Ningbo Research Institute, Zhejiang University, Ningbo 315100, China);
    2(College of Biosystems Engineering and Food Science, National & Local Joint Engineering Laboratory of Intelligent Food Techology and Equipment, Zhejiang University, Hangzhou 310058, China);
    3(Hangzhou Customs, Hangzhou 311208, China)

Received date: 2020-05-10

  Revised date: 2020-06-11

  Online published: 2020-11-12

Fold

Abstract

The effects of different thawing methods (ultrasonic microwave thawing, ultrasonic far-infrared thawing, ultrasonic ohmic thawing, ultrasonic vacuum thawing, and ultrasound thawing) on the physicochemical properties of the myofibrillar protein in sea bass were investigated from the protein structure, aggregation degree and oxidation degree. The structural changes of the myofibrillar protein were monitored by Raman spectra, ultraviolet absorption spectra and intrinsic fluorescence spectra. These indicators could help to preliminarily understand the mechanism of myofibrillar protein denaturation caused by different thawing methods at the molecular level. The result of Raman spectra showed that the content of α-helix thawed by ultrasonic microwave thawing was the highest among all thawing methods, which maintaining the protein structure effectively. The ultraviolet absorption spectra and intrinsic fluorescence spectra showed that the ultrasonic microwave thawing could retain the tertiary structure of the protein better, but the structure of the protein thawed by ultrasound was seriously damaged. Particle size, Zeta potential and SDS-PAGE were used to analyze the degree of protein aggregation. Compared with the fresh sample, the particle size and Zeta potential of all the thawing methods were no significantly difference (P>0.05). The electrophoretic band of ultrasonic microwave thawing was the closest to the fresh sample, which indicated the degradation degree of the protein was lower. The contents of total sulfhydryl by ultrasonic far-infrared thawing and ultrasonic microwave thawing were closest to that of the fresh sample, and the solubility by ultrasonic vacuum thawing was the closest to that of the fresh sample. In summary, ultrasonic microwave thawing method is the best to maintain the physicochemical properties of myofibrin.

Key words： sea bass; ultrasound thawing; protein structures; protein aggregation; protein oxidation

Cite this article

CAI Luyun , XU Qing , CAO Ailing . Effects of different ultrasound-assisted thawing methods on the myofibrillar protein of the sea bass (Perca fluviatilis)[J]. Food and Fermentation Industries, 2020 , 46(20) : 1 -8 . DOI: 10.13995/j.cnki.11-1802/ts.024414

References

[1] 谭明堂, 谢晶, 王金锋. 解冻方式对鱿鱼品质的影响[J]. 食品科学, 2019, 40(13): 94-101.
[2] YUAN C H,YU K F,CHEN S S,et al. Effect of freezing rate on the denaturation of myofibrillar proteins[J]. International Journal of Food Science & Technology, 2007, 20(6): 735-744.
[3] SRIKET P, BENJAKUL S, VISESSANGUAN W, et al. Comparative studies on the effect of the freeze-thawing process on the physicochemical properties and microstructures of black tiger shrimp (Penaeus monodon) and white shrimp (Penaeus vannamei) muscle[J]. Food Chemistry, 2006, 104(1): 113-121.
[4] XIA X F, KONG B H, LIU Q, et al. Physicochemical change and protein oxidation in porcine longissimus dorsi as influenced by different freeze-thaw cycles[J]. Meat Science, 2009, 83(2): 239-245.
[5] HOWELL N K, HERMAN H, LI-CHAN E C. Elucidation of protein-lipid interactions in a lysozyme-corn oil system by Fourier transform raman spectroscopy[J]. Journal of Agricultural & Food Chemistry, 2001, 49(3): 1 529-1 533.
[6] LIU G, XIONG Y L, BUTTERFIELD D A, et al. Chemical, physical, and gel-forming properties of oxidized myofibrils and whey- and soy-protein isolates[J]. 2000, 65(5): 811-818.
[7] CAI L Y, ZHANG W D, CAO A L, et al. Effects of ultrasonics combined with far infrared or microwave thawing on protein denaturation and moisture migration of Sciaenops ocellatus (red drum)[J]. Ultrasonics Sonochemistry, 2019, 55: 96-104.
[8] CAI L Y, CAO M J, CAO A L, et al. Ultrasound or microwave vacuum thawing of red seabream (Pagrus major) fillets[J]. Ultrasonics Sonochemistry, 2018, 47: 122-132.
[9] 年琳玉. 鲱鱼抗冻蛋白对真鲷品质特性的影响及抗冻机制研究[D]. 锦州:渤海大学, 2019.
[10] 李秀霞, 马莹莹, 刘宏影, 等. 超声波处理对金枪鱼肌原纤维蛋白理化性质和结构的影响[C]. 中国食品科学技术学会第十六届年会暨第十届中美食品业高层论坛论文摘要集. 北京:中国食品科学技术学会, 2019: 557-558.
[11] ZHANG M C, LI F F, DIAO X P, et al. Moisture migration, microstructure damage and protein structure changes in porcine longissimus muscle as influenced by multiple freeze-thaw cycles[J]. Meat Science, 2017, 133: 10-18.
[12] 李瑞平. 微波场内草鱼鱼肉蛋白营养和结构性质的研究[D]. 南昌:南昌大学, 2015.
[13] COSMIN M,BELICIU, CARMEN I. The effect of protein concentration and heat treatment temperature on micellar casein-soy protein mixtures[J]. Food Hydrocolloids, 2011, 25(6): 1 448-1 460.
[14] 姜晴晴, 吴春华, 董开成, 等. 解冻方式对带鱼蛋白性质及肌肉品质的影响[J]. 中国食品学报, 2016, 16(11): 17-27.
[15] HERRERO A M. Raman spectroscopy for monitoring protein structure in muscle food systems[J]. Critical Reviews in Food Science & Nutrition, 2008, 48(6): 512-523.
[16] 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.
[17] GUO J J, ZHOU Y H, YANG K, et al. Effect of low-frequency magnetic field on the gel properties of pork myofibrillar proteins[J]. Food Chemistry, 2019, 274: 775-781.
[18] JIANG J, CHEN J, XIONG Y L. Structural and emulsifying properties of soy protein isolate subjected to acid and alkaline ph-shifting processes[J]. Journal of Agricultural and Food Chemistry, 2009, 57(16): 7 576-7 583.
[19] RAGONE R, COLONNA G, BALESTRIERI C, et al. Determination of tyrosine exposure in proteins by second-derivative spectroscopy[J]. Biochemistry, 1984, 23(8): 1 871-1 875.
[20] ZHAO J Y, DONG F J, LI Y Y, et al. Effect of freeze-thaw cycles on the emulsion activity and structural characteristics of soy protein isolate[J]. Process Biochemistry, 2015, 50(10): 1 607-1 613.
[21] GUO X, QIU H H, DENG X R, et al. Effect of chlorogenic acid on the physicochemical and functional properties of coregonus peled myofibrillar protein through hydroxyl radical oxidation[J]. Molecules, 2019, 24(17): 3 205.
[22] ZOU Y, YANG H, ZHANG M H, et al. The influence of ultrasound and adenosine 5'-monophosphate marination on tenderness and the structures of myofibrillar proteins of beef[J]. Asian Australasian Journal of Animal Sciences, 2019, 32(10): 1 611-1 620.
[23] CAO M J, WANG J, CAO A L, et al. The impact of recrystallisation on the freeze - thaw cycles of red seabream (Pagrus major) fillets[J]. International Journal of Food Science and Technology. 2019, 54(5): 1 642-1 650.
[24] NIU J Z, ZHAO B F, GUO X J, et al. Effects of vacuum freeze-drying and vacuum spray-drying on biochemical properties and functionalities of myofibrillar proteins from silver carp[J]. Journal of Food Quality, 2019, 2019: 1-8.
[25] CHEN X, XIONG Y L, XU X L. High-pressure homogenization combined with sulfhydryl blockage by hydrogen peroxide enhance the thermal stability of chicken breast myofibrillar protein aqueous solution[J]. Food Chemistry, 2019, 285: 31-38.
[26] ZHENG J B, HAN Y R, GE G, et al. Partial substitution of NaCl with chloride salt mixtures: Impact on oxidative characteristics of meat myofibrillar protein and their rheological properties[J]. Food Hydrocolloids, 2019, 96: 36-42.
[27] SUN W Z, ZHAO M M, YANG B, et al. Oxidation of sarcoplasmic proteins during processing of cantonese sausage in relation to their aggregation behaviour and in vitro digestibility[J]. Meat Science, 2011, 88(3): 462-467.
[28] FU Q Q, LIU R, WANG H O, et al. Effects of oxidation in vitro on structures and functions of myofibrillar protein from beef muscles[J]. Journal of Agricultural & Food Chemistry, 2018, 67(20): 5 866-5 873.
[29] ZHOU L, FENG X, YANG Y L, et al. Effects of high-speed shear homogenization on the emulsifying and structural properties of myofibrillar protein under low-fat conditions[J]. Journal of the Science of Food and Agriculture, 2019, 99(14): 6 500-6 508.
[30] LI F F, WANG B, LIU Q, et al. Changes in myofibrillar protein gel quality of porcine longissimus muscle induced by its stuctural modification under different thawing methods[J]. Meat Science, 2019, 147: 108-115.
[31] GAO W H, HUANG Y P, ZENG X, et al. Effect of soluble soybean polysaccharides on freeze-denaturation and structure of myofibrillar protein of bighead carp surimi with liquid nitrogen freezing[J]. International Journal of Biological Macromolecules, 2019, 135: 839-844.
[32] LIN D Q, ZHANG L T, LI R J, et al. Effect of plant protein mixtures on the microstructure and rheological properties of myofibrillar protein gel derived from red sea bream (Pagrosomus major)[J]. Food Hydrocolloids, 2019, 96: 537-545.
[33] XIA M Q, CHEN Y X, GUO J J, et al. Effects of oxidative modification on textural properties and gel structure of pork myofibrillar proteins[J]. Food Research International, 2019, 121: 678-683.
[34] ZHANG L T, GUI P, ZHANG Y Q, et al. Assessment of structural, textural, and gelation properties of myofibrillar protein of silver carp (Hypophthalmichthys molitrix) modified by stunning and oxidative stress[J]. LWT - Food Science and Technology, 2018, 102: 142-149.
[35] CHENG J R, ZHU M J, LIU X M. Insight into the conformational and functional properties of myofibrillar protein modified by mulberry polyphenols[J]. Food Chemistry, 2020, 308: 125 592.
[36] 李慢. 超声辅助解冻对中国对虾品质影响的研究[D]. 杭州:浙江大学, 2018.
[37] DYMERSKI T, GEιBICKI J, WARDENCKI W, et al. Application of an electronic nose instrument to fast classification of polish honey types[J]. Sensors, 2014, 14(6): 10 709-10 724.
Options
Outlines

/

〈 〉

Powered by Beijing Magtech Co. Ltd,.