Evaluation of gel properties of heat-induced surimi of Ictalurus punctatus from four genealogies
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摘要: 斑点叉尾鮰 (Ictalurus punctatus) 刺少肉多，非常适合加工为鱼糜产品。为了评价不同家系斑点叉尾鮰鱼糜的加工特性，选取“江丰1号”鮰鱼的4个家系 (DZ1-1、KB4-1、K2-1、46-1) 鱼背肌肉为研究对象，经漂洗、斩拌、脱水、精滤等工艺制备成鱼糜，再通过二段式加热制成热诱导鱼糜凝胶。通过测定鱼糜蛋白的热稳定性以及鱼糜凝胶的白度、质构特性、持水性和凝胶强度等理化指标，分析不同家系鮰鱼鱼糜热诱导凝胶特性的差异。结果显示，DZ1-1家系鱼糜肌原纤维蛋白与其他家系相比热稳定性较高，β-折叠和β-转角结构相对含量较高，从而影响了热诱导鱼糜凝胶品质。各家系制备的热诱导鱼糜凝胶在白度上无显著性差异，持水性均大于80%。DZ1-1家系的凝胶强度为2.7×102 g∙cm，优于其他家系，而硬度、弹性和胶黏性与KB4-1家系无差异，但显著优于其他2个家系。综上，DZ1-1家系较适合作为鱼糜加工原料。Abstract: Ictalurus punctatus has less fishbones and more meat, very suitable for being processed into surimi products. In order to evaluate the processing characteristics of surimi of I. punctatus from different genealogies, we selected the dorsal muscle of the four genealogies of "Jiangfeng No.1" I. punctatus (DZ1-1, KB4-1, K2-1, 46-1) which were prepared into surimi after rinsing, chopping, dewatering and refined filtration, and heated them at two stages to make heat-induced surimi gels. By measuring the thermal stability of surimi protein, physical and chemical properties of the surimi gels, such as whiteness, texture, water holding capacity and gel strength, we analyzed the heat-induced gels of I. punctatus from different genealogies. The results show that compared with the other genealogies, the surimi myofibrillar protein of DZ1-1 genealogy had higher thermal stability, and the relative content of β-folding and β-turning structure was higher, which affected the gel quality of heat-induced surimi. There are no significant differences in the whiteness of heat induced surimi gels prepared by different genealogies of I. punctatus, with water holding capacity over 80%. The gel strength of the DZ1-1 genealogy was 2.7×102 g∙cm, which was better than other genealogies, while the hardness, springiness and gumminess of the DZ1-1 genealogy were not different from the KB4-1 genealogy, but significantly better than the other two genealogies. In conclusion, the DZ1-1 genealogy is more suitable for surimi processing.
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Key words:
- Ictalurus punctatus /
- Genealogy /
- Surimi /
- Thermal induced gel properties
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图 2 4个家系鮰鱼鱼糜储能模量G'和损耗角tanδ
Figure 2. Storage modulus G' and tanδ of four genealogies of I. punctatus surimi
图 3 4个家系鮰鱼鱼糜凝胶持水性和白度
注：图中相同小写字母或无字母表示差异不显著 (P>0.05)，不同小写字母表示差异显著 (P<0.05)，下图同此。
Figure 3. Water holding capacity and whiteness of four genealogies of I. punctatus surimi gels
Note: Values with the same or no superscripts have no significant differences (P>0.05); different superscripts indicate significant differences (P<0.05). The same case in the following figure.
图 4 4个家系鮰鱼鱼糜凝胶微观结构
Figure 4. Microstructures of four genealogies of I. punctatus surimi gels
图 5 4个家系鮰鱼鱼糜拉曼光谱
Figure 5. Raman spectra of four genealogies of I. punctatus surimi gels
图 6 4个家系鮰鱼鱼糜蛋白酰胺I区二级结构相对含量
Figure 6. Secondary structure contents from amide I band region of four genealogies of I. punctatus surimi proteins
表 1 4个不同家系鮰鱼鱼糜的基本成分质量分数
Table 1. Mass fractions of basic ingredients of surimi from four genealogies of I. punctatus
% 家系Genealogy 水分Moisture 粗蛋白Crude protein 粗脂肪Crude fat 灰分Ash K2-1 77.13±1.65a 15.72±0.89a 2.59±0.31a 1.82±0.16a KB4-1 76.21±1.51a 15.96±0.75a 2.41±0.28a 1.87±0.13a DZ1-1 78.35±1.67a 15.25±1.01a 2.96±0.24a 1.70±0.14a 46-1 73.14±1.95b 15.79±0.83a 2.69±0.19a 1.76±0.11a 注：表格中同列肩标相同小写字母或无字母表示差异不显著 (P>0.05)，不同小写字母表示差异显著 (P<0.05)，下表同此。 Note: Values with the same or no superscripts within the same column have no significant differences (P>0.05); different superscripts indicate significant differences (P<0.05). The same case in the following tables. 
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表 2 40~50 ℃不同家系鮰鱼鱼糜肌肉蛋白的热特性
Table 2. Thermal characteristics of surimi from four genealogies of I. punctatus at 40–50 ℃
家系Genealogy 起始温度Initial temperature/℃ 峰值温度Peak temperature/℃ 终止温度Final temperature/℃ 总变性热焓Total denaturation enthalpy/(10−2 J·g−1) K2-1 40.03 46.64 52.42 1.14 KB4-1 39.66 45.85 50.52 0.87 DZ1-1 38.02 47.54 51.05 1.39 46-1 38.33 46.06 51.27 1.20
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表 3 50~60 ℃不同家系鮰鱼鱼糜肌肉蛋白的热特性
Table 3. Thermal characteristics of surimi from four genealogies of I. punctatus at 50–60 ℃
家系Genealogy 起始温度Initial temperature/℃ 峰值温度Peak temperature/℃ 终止温度Final temperature/℃ 总变性热焓Total denaturation enthalpy/(10−2 J·g−1) K2-1 52.42 55.63 59.04 0.14 KB4-1 51.09 55.58 58.09 0.36 DZ1-1 52.15 57.93 61.74 1.65 46-1 51.67 56.35 59.03 0.49
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表 4 60~80 ℃不同家系鮰鱼鱼糜肌肉蛋白的热特性
Table 4. Thermal characteristics of muscles from four genealogies of I. punctatus at 60–80 ℃
家系Genealogy 起始温度Initial temperature/℃ 峰值温度Peak temperature/℃ 终止温度Final temperature/℃ 总变性热焓Total denaturation enthalpy/(10−2 J·g−1) K2-1 59.78 71.27 73.03 0.21 KB4-1 60.39 68.32 73.55 1.94 DZ1-1 63.51 67.18 72.39 0.56 46-1 60.43 67.68 74.46 1.89
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表 5 4个家系鮰鱼鱼糜凝胶凝胶强度和质构特性
Table 5. Gel strength and texture characteristics of four genealogies of I. punctatus surimi gels
家系Genealogy 凝胶强度Gel strength/(102 g·cm) 硬度Hardness/kg 回复性Resilience/% 内聚性
Cohesiveness弹性Springness/% 胶黏性Gumminess/kg 咀嚼性Chewiness/kg K2-1 2.45±0.12ab 5.46±0.91b 36.28±0.51b 0.70±0.010b 88.01±0.82a 3.85±0.61b 3.34±0.55b KB4-1 2.20±0.15b 6.87±0.33a 34.78±0.35c 0.68±0.010c 86.69±1.6a 4.62±0.24a 4.04±0.24ab DZ1-1 2.71±0.32a 6.88±0.49a 37.59±0.73b 0.71±0.010ab 87.48±1.8a 4.80±0.38a 4.22±0.39a 46-1 2.38±0.41ab 5.34±0.54b 38.15±0.32a 0.72±0.010a 88.99±0.63a 3.81±0.35b 3.36±0.30b
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[1] 仪淑敏, 姬颖, 姜天舒, 等. 鳀鱼鱼肉与白鲢鱼鱼糜混合热聚集行为分析[J]. 食品工业科技, 2020, 41(14): 8-14. doi: 10.13386/j.issn1002-0306.2020.14.002 [2] YI S M, LI Q, QIAO C P, et al. Myofibrillar protein conformation enhance gel properties of mixed surimi gels with Nemipterus virgatus and Hypophthalmichthys molitrix[J]. Food Hydrocoll, 2020, 106(9): 105924. [3] CAO H W, FAN D M, JIAO X D, et al. Effects of microwave combined with conduction heating on surimi quality and morphology[J]. J Food Eng, 2018, 228(7): 1-11. [4] XIE Y S, YU X L, WANG Z M, et al. The synergistic effects of myofibrillar protein enrichment and homogenization on the quality of cod protein gel[J]. Food Hydrocoll, 2022, 127(6): 107468. [5] 陈方雪, 周明珠, 邓祎, 等. 电子束辐照处理对鮰鱼冷藏期间品质的影响[J]. 肉类研究, 2021, 35(6): 57-62. doi: 10.7506/rlyj1001-8123-20210401-090 [6] 钟立强, 王明华, 陈校辉, 等. 世界斑点叉尾鮰产业近况I: 美国斑点叉尾鮰产业现状与展望[J]. 水产养殖, 2017, 38(5): 1-5. doi: 10.3969/j.issn.1004-2091.2018.09.003 [7] 钟立强, 王明华, 陈校辉, 等. 世界斑点叉尾鮰产业近况II: 中国斑点叉尾鮰产业发展与展望[J]. 水产养殖, 2018, 39(9): 7-11. doi: 10.3969/j.issn.1004-2091.2018.09.003 [8] ZHANG S Y, CHEN X H, WANG M H, et al. Development and characterization of ten polymorphic SNP markers in growth-related genes for the channel catfish, Ictalurus punctatus (Rafinesque, 1818)[J]. J Appl Ichthyol, 2016, 32(6): 1248-1251. doi: 10.1111/jai.13194 [9] 张世勇, 刘洪岩, 王江, 等. 基于微卫星标记的斑点叉尾鮰家系鉴定技术及应用[J]. 水生生物学报, 2020, 45(2): 327-333. [10] 刘芳芳, 林婉玲, 韩迎雪, 等. 5种淡水鱼鱼糜凝胶基本特性研究[J]. 南方水产科学, 2021, 17(2): 114-121. doi: 10.12131/20200220 [11] 刘海梅, 熊善柏, 张丽, 等. 鲢肌球蛋白热诱导的凝胶化温度[J]. 水产学报, 2010, 34(4): 643-647. [12] 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 Hydrocoll, 2019, 96(11): 604-616. [13] GAO R C, SHI T, SUN Q C, et al. Effects of l-arginine and l-histidine on heat-induced aggregation of fish myosin: bighead carp (Aristichthys nobilis)[J]. Food Chem, 2019, 295(10): 320-326. [14] PETCHARAT T, BENJAKUL S. Effect of gellan incorporation on gel properties of bigeye snapper surimi[J]. Food Hydrocoll, 2017, 77(4): 746-753. [15] CAO H W, FAN D M, JIAO X D, et al. Heating surimi products using microwave combined with steam methods: study on energy saving and quality[J]. Innov Food Sci Emerg Technol, 2018, 47: 231-240. doi: 10.1016/j.ifset.2018.03.003 [16] 于加美, 高瑞昌, 石彤, 等. 高脱乙酰度魔芋葡甘聚糖对鲢鱼鱼糜凝胶特性的影响[J]. 现代食品科技, 2019, 35(8): 48-54. doi: 10.13982/j.mfst.1673-9078.2019.8.008 [17] LIU J H, LUO Y H, GU S Q, et al. Physicochemical, conformational and functional properties of silver carp myosin glycated with konjac oligo-glucomannan: implications for structure-function relationships[J]. Food Hydrocoll, 2017, 72: 136-144. doi: 10.1016/j.foodhyd.2017.05.040 [18] 高文宏, 叶瑞森, 潘廷跳, 等. 基于拉曼光谱解析冻藏过程中鱼糜蛋白的结构变化[J]. 食品科学, 2018, 39(24): 71-77. doi: 10.7506/spkx1002-6630-201824012 [19] 乐贻荣, 肖炜, 邹芝英, 等. 奥尼罗非鱼肌肉营养成分分析和营养价值评定[J]. 中国农学通报, 2015, 31(11): 88-93. doi: 10.11924/j.issn.1000-6850.2014-2485 [20] 付湘晋, 许时婴, 王璋, 等. 酸碱对鲢鱼肌原纤维蛋白热变性、聚集、胶凝性质的影响[J]. 食品科学, 2008, 29(6): 100-103. doi: 10.3321/j.issn:1002-6630.2008.06.016 [21] ZHOU A M, SOOTTAWAT B, PAN K, et al. Cryoprotective effects of trehalose and sodium lactate on tilapia (Sarotherodon nilotica) surimi during frozen storage[J]. Food Chem, 2005, 96(1): 96-103. [22] 邵颖, 王小红, 吴文锦, 等. 5种淡水鱼肌肉热特性比较研究[J]. 食品科学, 2016, 37(19): 106-111. doi: 10.7506/spkx1002-6630-201619018 [23] 吕梁玉, 罗华彬, 吕鸣春, 等. 电子束辐照对梅鱼鱼糜化学作用力、流变及其凝胶特性的影响[J]. 食品科学, 2018, 39(19): 7-12. doi: 10.7506/spkx1002-6630-201819002 [24] CHEN X, XU X L, LIU D M, et al. Rheological behavior, conformational changes and interactions of water-soluble myofibrillar protein during heating[J]. Food Hydrocoll, 2018, 77: 524-533. doi: 10.1016/j.foodhyd.2017.10.030 [25] NIU H L, LI Y, HAN J C, et al. Gelation and rheological properties of myofibrillar proteins influenced by the addition of soybean protein isolates subjected to an acidic pH treatment combined with a mild heating[J]. Food Hydrocoll, 2017, 70(9): 269-276. [26] SUN F Y, HUANG Q L, HU T, et al. Effects and mechanism of modified starches on the gel properties of myofibrillar protein from grass carp[J]. Int J Biol Macromol, 2014, 64(2): 17-24. [27] 应月, 于加美, 朱杰, 等. 基于原料种类差异的淡水鱼鱼糜水凝胶比较分析[J]. 现代食品科技, 2021, 37(12): 162-168, 328. doi: 10.13982/j.mfst.1673-9078.2021.12.0424 [28] 孙静文. 不同漂洗对草鱼和白鲢鱼糜蛋白及其凝胶性能的影响[D]. 武汉: 华中农业大学, 2016: 41. [29] GU R J, XIAO X H, SUN J W, et al. Effects of rice residue on physicochemical properties of silver carp surimi gels[J]. Int J Food Prop, 2018, 21(1): 1743-1754. doi: 10.1080/10942912.2016.1214146 [30] HUANG J J, BAKRY A M, ZENG S W, et al. Effect of phosphates on gelling characteristics and water mobility of myofibrillar protein from grass carp (Ctenopharyngodon idellus)[J]. Food Chem, 2019, 272: 84-92. doi: 10.1016/j.foodchem.2018.08.028 [31] 李文协, 李学鹏, 刘慈坤, 等. 臭氧水漂洗对鲅鱼鱼糜品质及肌原纤维蛋白氧化的影响[J]. 食品工业科技, 2020, 41(16): 7-15. doi: 10.13386/j.issn1002-0306.2020.16.002 [32] SHAO J H, ZOU Y F, XU X L, et al. Evaluation of structural changes in raw and heated meat batters prepared with different lipids using Raman spectroscopy[J]. Food Res Int, 2011, 44(9): 2955-2961. doi: 10.1016/j.foodres.2011.07.003 [33] 畅鹏, 谢艳英, 王浩, 等. 热处理温度及时间对镜鲤鱼肌原纤维蛋白热聚集行为的影响[J]. 食品科学, 2021, 42(1): 101-107. doi: 10.7506/spkx1002-6630-20191213-152 [34] 王飞, 筴金华, 张艳红, 等. 尼萨F2家系后代与混合后代幼鱼耐盐及生长比较[J]. 华北农学报, 2013, 28(S1): 278-282. doi: 10.7668/hbnxb.2013.S1.052 [35] 秦钦, 陈校辉, 蒋广震, 等. 5个黄颡鱼家系组幼鱼生长、体组成和消化酶活力的比较[J]. 基因组学与应用生物学, 2018, 37(2): 768-773. doi: 10.13417/j.gab.037.000768 [36] NUNEZ-FLORES R, CANDO D, BORDERIAS A J, et al. Importance of salt and temperature in myosin polymerization during surimi gelation[J]. Food Chem, 2018, 239(1): 1226-1234. [37] YI S M, LI Q, QIAO C P, et al. Myofibrillar protein conformation enhance gel properties of mixed surimi gels with Nemipterus virgatus and Hypophthalmichthys molitrix[J]. Food Hydrocoll, 2020, 106: 105924. doi: 10.1016/j.foodhyd.2020.105924 [38] 韩敏义. 肌原纤维蛋白结构与热诱导凝胶功能特性关系研究——低场NMR和拉曼光谱法[D]. 南京: 南京农业大学, 2009: 90. [39] BEATTIE R J, BELL S J, FARMER L J, et al. Preliminary investigation of the application of Raman spectroscopy to the prediction of the sensory quality of beef silverside[J]. Meat Sci, 2004, 66(4): 903-913. doi: 10.1016/j.meatsci.2003.08.012 -
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