LI Xiaozhen, CHEN Xu, YANG Fujia, et al. Preparation of Silver Carp Scale Antifreeze Peptides and Its Improvement Effect on Gel Properties of Frozen-thawed Surimi[J]. Science and Technology of Food Industry, 2023, 44(1): 242−252. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2022040039.
Citation: LI Xiaozhen, CHEN Xu, YANG Fujia, et al. Preparation of Silver Carp Scale Antifreeze Peptides and Its Improvement Effect on Gel Properties of Frozen-thawed Surimi[J]. Science and Technology of Food Industry, 2023, 44(1): 242−252. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2022040039.

Preparation of Silver Carp Scale Antifreeze Peptides and Its Improvement Effect on Gel Properties of Frozen-thawed Surimi

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  • Received Date: April 06, 2022
  • Available Online: November 03, 2022
  • In this study, silver carp scale antifreeze peptides (ScAFPs) were prepared by enzymatic hydrolysis. Taking the freeze-thawing survival rate of Streptococcus thermophilus as the main index and the degree of hydrolysis as the auxiliary index, the optimal enzymolysis preparation process of ScAFPs was obtained through single factor and response surface optimization. At the same time, the basic properties of ScAFPs and their influence on the gel stability of surimi were studied. The results showed that the selected enzyme preparation was trypsin, substrate concentration of 5.0%, enzyme dosage of 3.8%, enzymolysis temperature of 37 ºC, enzymolysis time of 3.5 h. Under these conditions, the frozen survival rate of ScAFPs against Streptococcus thermophilus was 82.19%±1.03% and the degree of hydrolysis was 7.54%±0.43%. The relative molecular weight of ScAFPs was mainly in the range of 180~3000 Da, and its isoelectric point was around 4.2. Moreover, ScAFPs had strong hydrophilicity and good thermal stability, which could effectively reduce the ice crystal content in the system. The effect of ScAFPs on gel properties of freezing-thawing surimi showed that after five freezing-thawing cycles, the decrease of gel whiteness, hardness, chewiness and gel strength of surimi treated by ScAFPs was significantly (P<0.05) lower than that of surimi without cryoprotecter. When the addition of ScAFPs exceeded 2%, the freeze-thaw protection effect of ScAFPs on surimi was better than that of commercial antifreeze agents (4% sucrose and 4% sorbitol mixture). This study lays a theoretical foundation for the high-value utilization of silver carp scales and the application of ScAFPs as a new type of cryoprotectant in frozen surimi and its gel products.
  • [1]
    BANERJEE R, MAHESWARAPPA N B. Superchilling of muscle foods: Potential alternative for chilling and freezing[J]. Critical Reviews in Food Science and Nutrition,2019,59(8):1256−1263. doi: 10.1080/10408398.2017.1401975
    [2]
    UTRERA M, MORCUENDE D, GANHÃO R, et al. Role of phenolics extracting from Rosa canina L. on meat protein oxidation during frozen storage and beef patties processing[J]. Food and Bioprocess Technology,2015,8(4):854−864. doi: 10.1007/s11947-014-1450-3
    [3]
    QI J, LI C B, CHEN Y J, et al. Changes in meat quality of ovine longissimus dorsi muscle in response to repeated freeze and thaw[J]. Meat Science,2012,92(4):619−626. doi: 10.1016/j.meatsci.2012.06.009
    [4]
    DU L H, BETTI M. Chicken collagen hydrolysate cryoprotection of natural actomyosin: Mechanism studies during freeze-thaw cycles and simulated digestion[J]. Food Chemistry,2016,211:791−802. doi: 10.1016/j.foodchem.2016.05.092
    [5]
    WALAYAT N, XIONG H G, XIONG Z Y, et al. Role of cryoprotectants in surimi and factors affecting surimi gel properties: A review[J]. Food Reviews International,2020:1−20.
    [6]
    CHEN X, WU J H, LI X Z, et al. Investigation of the cryoprotective mechanism and effect on quality characteristics of surimi during freezing storage by antifreeze peptides[J]. Food Chemistry,2022,371:131054. doi: 10.1016/j.foodchem.2021.131054
    [7]
    CHEN X, WU J H, CAI X X, et al. Production, structure-function relationships, mechanisms, and applications of antifreeze peptides[J]. Comprehensive Reviews in Food Science and Food Safety,2021,20(1):542−562. doi: 10.1111/1541-4337.12655
    [8]
    CHEN X, WU J H, LI L, et al. Cryoprotective activity and action mechanism of antifreeze peptides obtained from tilapia scales on Streptococcus thermophilus during cold stress[J]. Journal of Agricultural and Food Chemistry,2019,67(7):1918−1926. doi: 10.1021/acs.jafc.8b06514
    [9]
    SONG D H, KIM M, JIN E S, et al. Cryoprotective effect of an antifreeze protein purified from Tenebrio molitor larvae on vegetables[J]. Food Hydrocolloids,2019,94:585−591. doi: 10.1016/j.foodhyd.2019.04.007
    [10]
    DAMODARAN S, WANG S Y. Ice crystal growth inhibition by peptides from fish gelatin hydrolysate[J]. Food Hydrocolloids,2017,70:46−56. doi: 10.1016/j.foodhyd.2017.03.029
    [11]
    WANG S Y, DAMODARAN S. Ice-structuring peptides derived from bovine collagen[J]. Journal of Agricultural and Food Chemistry,2009,57(12):5501−5509. doi: 10.1021/jf900524y
    [12]
    汪少芸, 赵立娜, 周焱富, 等. 食源性明胶多肽的制备、分离及其抗冻活性[J]. 食品科学,2013,34(9):135−139. [WANG S Y, ZHAO L N, ZHOU Y F, et al. Preparation and isolation of food-origin gelatin peptide and ice crystal inhibition[J]. Food Science,2013,34(9):135−139. doi: 10.7506/spkx1002-6630-201309028
    [13]
    洪晶, 汪少芸, 吴金鸿, 等. 食品源抗冻多肽的制备及冰晶抑制作用研究[J]. 中国食品学报,2013,13(1):11−18. [HONG J, WANG S Y, WU J H, et al. Preparation of food derived antifreeze peptides and study on ice crystal inhibition[J]. Journal of Chinese Institute of Food Science and Technology,2013,13(1):11−18. doi: 10.16429/j.1009-7848.2013.01.012
    [14]
    WANG S Y, ZHAO J, CHEN L, et al. Preparation, isolation and hypothermia protection activity of antifreeze peptides from shark skin collagen[J]. LWT-Food Science and Technology,2014,55(1):210−217. doi: 10.1016/j.lwt.2013.07.019
    [15]
    CHEN X, LI L, YANG F J, et al. Effects of gelatin-based antifreeze peptides on cell viability and oxidant stress of Streptococcus thermophilus during cold stage[J]. Food and Chemical Toxicology,2020,136:111056. doi: 10.1016/j.fct.2019.111056
    [16]
    于秀娟, 徐乐俊, 吴反修. 2020年中国渔业统计年鉴[M]. 中国农业出版社, 2020, 30−31

    YU X J, XU L J, WU F X. China fishery statistical yearbook 2020[M]. China Agriculture Press, 2020, 30−31.
    [17]
    PAL G K, SURESH P V. Comparative assessment of physico-chemical characteristics and fibril formation capacity of thermostable carp scales collagen[J]. Materials Science and Engineering: C,2017,70:32−40. doi: 10.1016/j.msec.2016.08.047
    [18]
    于林. 白鲢鱼鳞胶原蛋白复合膜的制备以及保鲜效果研究[D]. 上海: 上海海洋大学, 2017

    YU L. Study on hypophthalmichthys molitrix scale collagen-chitosan blend film and its preservation effects[D]. Shanghai: Shanghai Ocean University, 2017.
    [19]
    LIN J P, CAI X X, TANG M R, et al. Preparation and evaluation of the chelating nanocomposite fabricated with marine algae Schizochytrium sp protein hydrolysate and calcium[J]. Journal of Agricultural and Food Chemistry,2015,63(44):9704−9714. doi: 10.1021/acs.jafc.5b04001
    [20]
    刘聃, 曾凡坤. 花生蛋白多肽饮料肽含量测定重复性差原因研究[J]. 粮食与油脂,2012,25(6):24−27. [LIU D, ZENG F K. Study on reason of repeatability bad on determination of peptide content in peanut protein polypeptide beverage[J]. Cereals & Oils,2012,25(6):24−27. doi: 10.3969/j.issn.1008-9578.2012.06.007
    [21]
    曾茂茂, 王霄, 陈洁. 蛋白质疏水性测定方法的相关性及适用性[J]. 食品科学,2011,32(15):117−120. [ZENG M M, WANG X, CHEN J. Correlation and applicability of different methods for determining protein hydrophobicity[J]. Food Science,2011,32(15):117−120.
    [22]
    WU J H, RONG Y Z, WANG Z W, et al. Isolation and characterisation of sericin antifreeze peptides and molecular dynamics modelling of their ice-binding interaction[J]. Food Chemistry,2015,174:621−629. doi: 10.1016/j.foodchem.2014.11.100
    [23]
    LIN J, HONG H, ZHANG L T, et al. Antioxidant and cryoprotective effects of hydrolysate from gill protein of bighead carp (Hypophthalmichthys nobilis) in preventing denaturation of frozen surimi[J]. Food Chemistry,2019,298:124868. doi: 10.1016/j.foodchem.2019.05.142
    [24]
    YE Y H, LIU X Y, BAI W D, et al. Effect of microwave-ultrasonic combination treatment on heating-induced gel properties of low-sodium tilapia surimi during gel setting stage and comparative analysis[J]. LWT-Food Science and Technology,2022,161:113386. doi: 10.1016/j.lwt.2022.113386
    [25]
    LIU C K, LI W X, LIN B Y, et al. Comprehensive analysis of ozone water rinsing on the water-holding capacity of grass carp surimi gel[J]. LWT-Food Science and Technology,2021,150:111919. doi: 10.1016/j.lwt.2021.111919
    [26]
    LI L, WUJ H, ZHANG L, et al. Investigation of the physiochemical properties, cryoprotective activity and possible action mechanisms of sericin peptides derived from membrane separation[J]. LWT-Food Science and Technology,2017,77:532−541. doi: 10.1016/j.lwt.2016.12.004
    [27]
    BENJAKUL S, SEYMOUR T A, MORRISSEY M T, et al. Physicochemical changes in pacific whiting muscle proteins during iced storage[J]. Journal of Food Science,1997,62(4):729−733. doi: 10.1111/j.1365-2621.1997.tb15445.x
    [28]
    孟一, 张玉华, 许丽丹, 等. 近红外光谱采集方式与样品形态对带鱼新鲜度检测结果的影响[J]. 食品工业科技,2014,35(11):282−287. [MENG Y, ZHANG Y H, XU L D, et al. Effect of different near infrared spectroscopy (NIR) acquisition ways and sample states on the ribbonfish freshness detection results[J]. Science and Technology of Food Industry,2014,35(11):282−287. doi: 10.13386/j.issn1002-0306.2014.11.053
    [29]
    JITTINANDANA S, KENNEY P B, SLIDER S D. Cryoprotectants preserve quality of restructured trout products following freeze-thaw cycling[J]. Journal of Muscle Foods,2005,16(4):354−378. doi: 10.1111/j.1745-4573.2005.00028.x
    [30]
    KORZENIOWSKA M, CHEUNG I W Y, LI CHAN E C Y. Effects of fish protein hydrolysate and freeze-thaw treatment on physicochemical and gel properties of natural actomyosin from pacific cod[J]. Food Chemistry,2013,138(2):1967−1975.
    [31]
    CHEUNG I W Y, LICEAGA A M, LI CHAN E C Y. Pacific hake (Merluccius productus) hydrolysates as cryoprotective agents in frozen pacific cod fillet mince[J]. Journal of Food Science,2009,74(8):588−594. doi: 10.1111/j.1750-3841.2009.01307.x
    [32]
    ZHANG Y, DONG M, ZHANG X, et al. Effects of inulin on the gel properties and molecular structure of porcine myosin: A underlying mechanisms study[J]. Food Hydrocolloids,2020,108:105974. doi: 10.1016/j.foodhyd.2020.105974
    [33]
    周文娟. 鲢鱼酶解产物在冷冻鱼糜中的抗冻机理及其应用[D]. 长沙: 长沙理工大学, 2019

    ZHOU W J. Antifreeze mechanism of hydrolyzed products of silver carp in frozen surimi and its application[D]. Changsha: Changsha University of Science & Technology.
    [34]
    SUN Q X, SUN F D, XIA X F, et al. The comparison of ultrasound-assisted immersion freezing, air freezing and immersion freezing on the muscle quality and physicochemical properties of common carp (Cyprinus carpio) during freezing storage[J]. Ultrasonics Sonochemistry,2019,51:281−291. doi: 10.1016/j.ultsonch.2018.10.006
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