SHI Qiuyan, LIN Duanquan, HE Wenxiong, et al. Effects of Pre-freezing and Vacuum Freeze-drying on Physicochemical Properties and Gelling Characteristics of Myofibrillar Protein from Nemipterus virgatus[J]. Science and Technology of Food Industry, 2025, 46(9): 1−11. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2024040160.
Citation: SHI Qiuyan, LIN Duanquan, HE Wenxiong, et al. Effects of Pre-freezing and Vacuum Freeze-drying on Physicochemical Properties and Gelling Characteristics of Myofibrillar Protein from Nemipterus virgatus[J]. Science and Technology of Food Industry, 2025, 46(9): 1−11. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2024040160.

Effects of Pre-freezing and Vacuum Freeze-drying on Physicochemical Properties and Gelling Characteristics of Myofibrillar Protein from Nemipterus virgatus

More Information
  • Received Date: April 09, 2024
  • Available Online: February 28, 2025
  • To investigate the effects of vacuum freeze-drying on the properties of frozen surimi powder, myofibrillar protein (MP) from Nemipterus virgatus was taken as the research object. The changes of physicochemical properties of MP during the processes of pre-freezing and vacuum freeze-drying, and the effect of transglutaminase (TGase) on the gelling characteristics of MP were investigated. The results showed that compared with the untreated group, the turbidity and particle size of MP treated by pre-freezing and vacuum freeze-drying increased significantly (P<0.05) with the decreased solubility by 32.3% and 42.0%, indicating that proteins aggregation occurred during the processing. The decreased total sulfhydryl content by 27.3% and 45.35%, and the increased carbonyl content by 112.2% and 181.5%, respectively, showing that oxidative denaturation occurred. The content of α-helix structure decreased and the maximum endogenous fluorescence intensity of MP treated by pre-freezing and vacuum freeze-drying decreased from 5879 to 5487 and 4144, respectively, revealing that the ordered structure of protein was destroyed and the microenvironment was changed. The gels prepared by the untreated group had the highest storage modulus G′ value, followed by the pre-freezing treatment group and then the vacuum freeze-drying group. The addition of TGase could improve the rheological properties of MP. The gel network structure of MP was clearly visible in the untreated group, and the uneven network structure appeared in the pre-freezing group, while the vacuum freeze-drying group could not form gel network structure. The addition of TGase promoted the formation of denser and more uniform gel network structure of MP. In summary, the pre-freezing stage and the drying stage in the vacuum freeze-drying could affect the physicochemical properties and gelling characteristics of MP, in which the freezing denaturation of MP caused by the pre-freezing treatment had a significant impact on the aggregation and oxidation of MP, while the dehydration denaturation of MP during the drying phase had a more pronounced effect on the structure of MP. Furthermore, the addition of TGase could improve the gelling characteristics of MP after the pre-freezing and vacuum freeze-drying treatments.
  • [1]
    刘艺杰. 鳙鱼(Aristichthys nobilis)和秘鲁鱿鱼(Dosidicus gigas)肌肉蛋白质理化特性及凝胶特性的研究[D]. 青岛:中国海洋大学, 2007. [LIU Y J. Study on the protein character and gel property of bighead carp and gaint squid[D]. Qingdao:Ocean University of China, 2007.]

    LIU Y J. Study on the protein character and gel property of bighead carp and gaint squid[D]. Qingdao: Ocean University of China, 2007.
    [2]
    NURUL H, AMINAH A, BABJI A S. Functional properties of surimi powder from three Malaysian marine fish[J]. International Journal of Food Science & Technology,2001,36:401−406.
    [3]
    GUO X J, SHI L, XIONG S B, et al. Gelling properties of vacuum-freeze dried surimi powder as influenced by heating method and microbial transglutaminase[J]. LWT-Food Science and Technology,2019,99:105−111. doi: 10.1016/j.lwt.2018.09.050
    [4]
    毕金峰, 冯舒涵, 金鑫, 等. 真空冷冻干燥技术与产业的发展及趋势[J]. 核农学报,2022,36(2):414−421. [BI J F, FENG S H, JIN X, et al. Current status and development trend of freeze drying technology and industry[J]. Journal of Nuclear Agricultural Sciences,2022,36(2):414−421.] doi: 10.11869/j.issn.100-8551.2022.02.0414

    BI J F, FENG S H, JIN X, et al. Current status and development trend of freeze drying technology and industry[J]. Journal of Nuclear Agricultural Sciences, 2022, 36(2): 414−421. doi: 10.11869/j.issn.100-8551.2022.02.0414
    [5]
    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.
    [6]
    CHEN P, QIU Y J, CHEN S J, et al. Insights into the effects of different drying methods on protein oxidation and degradation characteristics of golden pompano (Trachinotus ovatus)[J]. Frontiers in Nutrition,2022,9:1063836. doi: 10.3389/fnut.2022.1063836
    [7]
    YANG H J, CHEN Z Z, WANG H F, et al. Uncovering the rheological properties basis for freeze drying treatment-induced improvement in the solubility of myofibrillar proteins[J]. Current Research in Food Science,2024,8:100651. doi: 10.1016/j.crfs.2023.100651
    [8]
    SANTHI D, KALAIKANNAN A, MALAIRAJ P, et al. Application of microbial transglutaminase in meat foods:A review[J]. Critical Reviews in Food Science and Nutrition,2017,57(10):2071−2076. doi: 10.1080/10408398.2014.945990
    [9]
    CHIN K B, GO M Y, XIONG Y L. Konjac flour improved textural and water retention properties of transglutaminase-mediated, heat-induced porcine myofibrillar protein gel:Effect of salt level and transglutaminase incubation[J]. Meat Science,2009,81(3):565−572. doi: 10.1016/j.meatsci.2008.10.012
    [10]
    冯倩. 转谷氨酰胺酶改性对白鲢鱼肌原纤维蛋白凝胶特性及体外消化特性的影响[D]. 上海:上海海洋大学, 2023. [FENG Q. Effects of transglutaminase modification on gel properties and in vitro digestibility of myofibrillar protein of silver carp (Hypophthalmichthys molitrix)[D]. Shanghai:Shanghai Ocean University, 2023.]

    FENG Q. Effects of transglutaminase modification on gel properties and in vitro digestibility of myofibrillar protein of silver carp (Hypophthalmichthys molitrix)[D]. Shanghai: Shanghai Ocean University, 2023.
    [11]
    钟坦君. 没食子酸的添加对金线鱼鱼糜凝胶特性的影响及体外消化产物活性研究[D]. 湛江:广东海洋大学, 2022. [ZHONG T J. Effect of gallic acid addition on gel properties and the activity of digesting products in vitro of Nemipterus virgatus surimi gel[D]. Zhanjiang:Guangdong Ocean University, 2022.]

    ZHONG T J. Effect of gallic acid addition on gel properties and the activity of digesting products in vitro of Nemipterus virgatus surimi gel[D]. Zhanjiang: Guangdong Ocean University, 2022.
    [12]
    JIANG X J, ZHANG Z J, CAI H N, et al. The effect of soybean trypsin inhibitor on the degradation of myofibrillar proteins by an endogenous serine proteinase of crucian carp[J]. Food Chemistry,2006,94(4):498−503. doi: 10.1016/j.foodchem.2004.11.046
    [13]
    DU X, ZHAO M N, PAN N, et al. Tracking aggregation behaviour and gel properties induced by structural alterations in myofibrillar protein in mirror carp (Cyprinus carpio) under the synergistic effects of pH and heating[J]. Food Chemistry,2021,362:130222. doi: 10.1016/j.foodchem.2021.130222
    [14]
    LIU R, ZHAO S M, YANG H, et al. Comparative study on the stability of fish actomyosin and pork actomyosin[J]. Meat Science,2011,88(2):234−240. doi: 10.1016/j.meatsci.2010.12.026
    [15]
    LI J, DAI Z C, CHEN Z H, et al. Improved gelling and emulsifying properties of myofibrillar protein from frozen shrimp (Litopenaeus vannamei) by high-intensity ultrasound[J]. Food Hydrocolloids,2023,135:108188. doi: 10.1016/j.foodhyd.2022.108188
    [16]
    LIU G, XIONG Y L, BUTTERFIELD D A. Chemical, physical, and gel-forming properties of oxidized myofibrils and whey- and soy-protein isolates[J]. Journal of Food Science,2000,65(5):811−818. doi: 10.1111/j.1365-2621.2000.tb13592.x
    [17]
    LEVINE R L, GARLAND D, OLIVER C N, et al. Determination of carbonyl content in oxidatively modified proteins[J]. Methods in Enzymology,1990,186:464−478.
    [18]
    CAO Y G, XIONG Y L. Chlorogenic acid-mediated gel formation of oxidatively stressed myofibrillar protein[J]. Food Chemistry,2015,180:235−243. doi: 10.1016/j.foodchem.2015.02.036
    [19]
    RIEBROY S, BENJAKUL S, VISESSANGUAN W, et al. Acid-induced gelation of natural actomyosin from Atlantic cod (Gadus morhua) and burbot (Lota lota)[J]. Food Hydrocolloids,2009,23(1):26−39. doi: 10.1016/j.foodhyd.2007.11.010
    [20]
    WALAYAT N, TANG W, NAWAZ A, et al. Influence of Konjac oligo-glucomannan as cryoprotectant on physicochemical and structural properties of silver carp surimi during fluctuated frozen storage[J]. LWT-Food Science and Technology,2022,164:113641. doi: 10.1016/j.lwt.2022.113641
    [21]
    LAEMMLI U K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4[J]. Nature,1970,227(5259):680−685. doi: 10.1038/227680a0
    [22]
    FAN M C, HUANG Q L, ZHONG S Y, et al. Gel properties of myofibrillar protein as affected by gelatinization and retrogradation behaviors of modified starches with different crosslinking and acetylation degrees[J]. Food Hydrocolloids,2019,96:604−616. doi: 10.1016/j.foodhyd.2019.05.045
    [23]
    SUN L C, LIN Y C, LIU W F, et al. Effect of pH shifting on conformation and gelation properties of myosin from skeletal muscle of blue round scads (Decapterus maruadsi)[J]. Food Hydrocolloids,2019,93:137−145. doi: 10.1016/j.foodhyd.2019.02.026
    [24]
    UTRERA M, MORCUENDE D, ESTÉVEZ M. Temperature of frozen storage affects the nature and consequences of protein oxidation in beef patties[J]. Meat Science,2014,96(3):1250−1257. doi: 10.1016/j.meatsci.2013.10.032
    [25]
    BAO P Q, CHEN L, HU Y, et al. L-Arginine and L-lysine retard aggregation and polar residue modifications of myofibrillar proteins:Their roles in solubility of myofibrillar proteins in frozen porcine Longissimus lumborum[J]. Food Chemistry,2022,393:133347. doi: 10.1016/j.foodchem.2022.133347
    [26]
    孔令圆. 干切牛肉冷冻干燥中低能耗高速率干燥条件的动态研究[D]. 银川:宁夏大学, 2015. [KONG L Y. Dynamic study on operation conditions for low energy consumption and high drying rate during freezing drying of cooked beef slice[D]. Yinchuan:Ningxia University, 2015.]

    KONG L Y. Dynamic study on operation conditions for low energy consumption and high drying rate during freezing drying of cooked beef slice[D]. Yinchuan: Ningxia University, 2015.
    [27]
    AN Y Q, YOU J, XIONG S B, et al. Short-term frozen storage enhances cross-linking that was induced by transglutaminase in surimi gels from silver carp (Hypophthalmichthys molitrix)[J]. Food Chemistry,2018,257:216−222. doi: 10.1016/j.foodchem.2018.02.140
    [28]
    李可, 张俊霞, 王欣瑶, 等. 不同超声波功率处理对类PSE鸡肉肌原纤维蛋白结构和乳化稳定性的影响[J]. 食品科学,2023,44(13):23−31. [LI K, ZHANG J X, WANG X Y, et al. Effects of ultrasound treatment at different powers on the structure and emulsifying properties of PSE-Like chicken myofibrillar protein[J]. Food Science,2023,44(13):23−31.] doi: 10.7506/spkx1002-6630-20220624-269

    LI K, ZHANG J X, WANG X Y, et al. Effects of ultrasound treatment at different powers on the structure and emulsifying properties of PSE-Like chicken myofibrillar protein[J]. Food Science, 2023, 44(13): 23−31. doi: 10.7506/spkx1002-6630-20220624-269
    [29]
    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 and Food Chemistry,2019,67(20):5866−5873. doi: 10.1021/acs.jafc.9b01239
    [30]
    DESCALZO A M, SANCHO A M. A review of natural antioxidants and their effects on oxidative status, odor and quality of fresh beef produced in Argentina[J]. Meat Science,2008,79(3):423−436. doi: 10.1016/j.meatsci.2007.12.006
    [31]
    LEE S, CHOI Y S, JO K, et al. Processing characteristics of freeze-dried pork powder for meat emulsion gel[J]. Food Science of Animal Resources,2021,41(6):997−1011. doi: 10.5851/kosfa.2021.e51
    [32]
    LEYGONIE C, BRITZ T J, HOFFMAN L C. Meat quality comparison between fresh and frozen/thawed ostrich M. iliofibularis[J]. Meat Science,2012,91(3):364−368. doi: 10.1016/j.meatsci.2012.02.020
    [33]
    TANG X L, PIKAL M J. Design of freeze-drying processes for pharmaceuticals:Practical advice[J]. Pharmaceutical Research,2004,21(2):191−200. doi: 10.1023/B:PHAM.0000016234.73023.75
    [34]
    蔡联辉, 曾虹燕, 蔡西玲, 等. 莲子蛋白组分二级结构的研究[J]. 光谱学与光谱分析,2011,31(9):2394−2398. [CAI L H, ZENG H Y, CAI X L, et al. Second structure of the protein factions from lotus seeds[J]. Spectroscopy and Spectral Analysis,2011,31(9):2394−2398.]

    CAI L H, ZENG H Y, CAI X L, et al. Second structure of the protein factions from lotus seeds[J]. Spectroscopy and Spectral Analysis, 2011, 31(9): 2394−2398.
    [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,2020,308:125592. doi: 10.1016/j.foodchem.2019.125592
    [36]
    CHEN X, XU X L, HAN M Y, et al. Conformational changes induced by high-pressure homogenization inhibit myosin filament formation in low ionic strength solutions[J]. Food Research International,2016,85:1−9. doi: 10.1016/j.foodres.2016.04.011
    [37]
    WANG Z M, HE Z F, GAN X, et al. The effects of lipid oxidation product acrolein on the structure and gel properties of rabbit meat myofibrillar proteins[J]. Food Biophysics,2018,13(4):374−386. doi: 10.1007/s11483-018-9543-6
    [38]
    GONG K J, SHI A M, LIU H Z, et al. Emulsifying properties and structure changes of spray and freeze-dried peanut protein isolate[J]. Journal of Food Engineering,2016,170:33−40. doi: 10.1016/j.jfoodeng.2015.09.011
    [39]
    SHI J, ZHANG L T, LU H, et al. Protein and lipid changes of mud shrimp (Solenocera melantho) during frozen storage:Chemical properties and their prediction[J]. International Journal of Food Properties,2017,20(sup2):2043−2056.
    [40]
    ZOU Y, YANG H, ZHANG M H, et al. The influence of ultrasound and adenosine 5'-monophosphate marination on tenderness and structure of myofibrillar proteins of beef[J]. Asian-Australasian Journal of Animal Sciences,2019,32(10):1611−1620. doi: 10.5713/ajas.18.0780
    [41]
    ZHANG R R, XIONG S B, YOU J, et al. Effects of ozone treatments on the physicochemical changes of myofibrillar proteins from silver carp (Hypophthalmichthys molitrix) during frozen storage[J]. Journal of Food Quality,2017,2017:1−9.
    [42]
    VATE N K, BENJAKUL S. Combined effect of squid ink tyrosinase and tannic acid on heat induced aggregation of natural actomyosin from sardine[J]. Food Hydrocolloids,2016,56:62−70. doi: 10.1016/j.foodhyd.2015.12.009
    [43]
    WANG G, LIU M M, CAO L W, et al. Effects of different NaCl concentrations on self-assembly of silver carp myosin[J]. Food Bioscience,2018,24:1−8. doi: 10.1016/j.fbio.2018.05.002
    [44]
    YANG Y, LIU X Y, XUE Y, et al. The process of heat-induced gelation in Litopenaeus vannamei[J]. Food Hydrocolloids,2020,98:105260. doi: 10.1016/j.foodhyd.2019.105260
    [45]
    GUO Z B, LI Z Y, WANG J Y, et al. Gelation properties and thermal gelling mechanism of golden threadfin bream myosin containing CaCl2 induced by high pressure processing[J]. Food Hydrocolloids,2019,95:43−52. doi: 10.1016/j.foodhyd.2019.04.017
    [46]
    ZHAO Y Y, HOU Q, CAO S M, et al. Effect of regenerated cellulose fiber on the properties and microstructure of emulsion model system from meat batters[J]. Food Hydrocolloids,2019,87:83−89. doi: 10.1016/j.foodhyd.2018.07.044
    [47]
    DEJONG G A H, KOPPELMAN S J. Transglutaminase catalyzed reactions:Impact on food applications[J]. Journal of Food Science,2002,67(8):2798−2806. doi: 10.1111/j.1365-2621.2002.tb08819.x
    [48]
    CAO Y G, HAN X R, YUAN F, et al. Effect of combined treatment of L-arginine and transglutaminase on the gelation behavior of freeze-damaged myofibrillar protein[J]. Food & Function,2022,13(3):1495−1505.
    [49]
    ZHOU F B, ZHAO M M, ZHAO H F, et al. Effects of oxidative modification on gel properties of isolated porcine myofibrillar protein by peroxyl radicals[J]. Meat Science,2014,96(4):1432−1439. doi: 10.1016/j.meatsci.2013.12.001
    [50]
    杨领. TG酶-木薯淀粉对金线鱼鱼糜3D打印特性的影响[D]. 锦州:渤海大学, 2020. [YANG L. Effects of transglutamianse and cassava starch on 3D printing characteristics of Nemipterus virgatus surimi[D]. Jingzhou:Bohai University, 2020.]

    YANG L. Effects of transglutamianse and cassava starch on 3D printing characteristics of Nemipterus virgatus surimi[D]. Jingzhou: Bohai University, 2020.
    [51]
    BORDERÍAS A J, TOVAR C A, DOMÍNGUEZ-TIMÓN F, et al. Characterization of healthier mixed surimi gels obtained through partial substitution of myofibrillar proteins by pea protein isolates[J]. Food Hydrocolloids,2020,107:105976. doi: 10.1016/j.foodhyd.2020.105976
    [52]
    GUL O, SARICAOGLU F T, MORTAS M, et al. Effect of high pressure homogenization (HPH) on microstructure and rheological properties of hazelnut milk[J]. Innovative Food Science & Emerging Technologies,2017,41:411−420.
    [53]
    LEITE T S, AUGUSTO P E D, CRISTIANINI M. Processing frozen concentrated orange juice (FCOJ) by high pressure homogenization (HPH) technology:Changes in the viscoelastic properties[J]. Food Engineering Reviews,2015,7(2):231−240. doi: 10.1007/s12393-014-9082-y
    [54]
    LI G S, CHEN Y T, XUAN S F, et al. Rheological properties and structure of myofibrillar protein extracted from Oratosquilla oratoria muscle as affected by ultra-high pressure[J]. International Journal of Food Properties,2019,22(1):1310−1321. doi: 10.1080/10942912.2019.1642915
    [55]
    WU M G, CAO Y, LEI S M, et al. Protein structure and sulfhydryl group changes affected by protein gel properties:Process of thermal-induced gel formation of myofibrillar protein[J]. International Journal of Food Properties,2019,22(1):1834−1847. doi: 10.1080/10942912.2019.1656231
    [56]
    INGADOTTIR B, KRISTINSSON H G. Gelation of protein isolates extracted from tilapia light muscle by pH shift processing[J]. Food Chemistry,2010,118(3):789−798. doi: 10.1016/j.foodchem.2009.05.064

Catalog

    Article Metrics

    Article views (25) PDF downloads (2) Cited by()

    /

    DownLoad:  Full-Size Img  PowerPoint
    Return
    Return