Microsoft Word - 6——黄琳_news_.doc

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1 三疣梭子蟹 (Portunus trituberculatus) 冻藏过程中肌肉蛋白质生化特性的变化黄琳, 张莉, 武丹露 (, ) 摘要 : 以三疣梭子蟹肌肉基本营养成分蛋白质组成肌原纤维蛋白含量 Ca 2+ -ATPase 活性总巯基含量二硫键含量以及肌原纤维蛋白的 SDS-PAGE 分析作为指标, 研究了三疣梭子蟹在不同冻藏温度下肌肉蛋白质生化特征的变化结果表明, 三疣梭子蟹是典型的高蛋白食品 ; 随着冻藏时间的延长, 水溶性蛋白含量先增加后减少, 盐溶性蛋白和不溶性蛋白含量逐渐减少, 碱溶性蛋白含量逐渐增加 ; 肌原纤维蛋白含量 Ca 2+ -ATPase 活性总巯基含量随着冻藏时间的延长, 均呈现下降趋势, 而二硫键含量则呈上升趋势, 且 20 和 40 两组之间差异显著 (P<0.05) SDS-PAGE 分析结果表明, 组成肌原纤维蛋白的各种蛋白质均有不同程度降解, 且 20 比 40 组降解更明显因此, 40 冻藏对梭子蟹肌肉蛋白质生化特性的影响较小关键词 : 三疣梭子蟹 (Portunus trituberculatus); 肌肉 ; 蛋白质 ; 生化特性中图分类号 : TS254.1 文献标识码 : A 文章编号 : (2017) DOI: /hykx , Portunus trituberculatus, (Curstacea) (Decapoda) (Portunidae), [1] ; [2],,, [3],,,, (Argopecten irradiams) [3] (Ophiocephalus argus Cantor) [4] (Metapenaeus ensis) [5] (Scylla serrata) [6] [7] [1] [8] [9],,, 1 材料与方法 1.1 材料与仪器, 120 g ( ); (TEMED) (AP) (SDS)( ); G250 (Tris) ( );, KJELTECTM 8400 ( FOSS ); IKA ( IKA ); : ; : : (ZR2015CM010) [Foundation: Province Natural Science Foundation of Shandong, NO.ZR2015CM010] : (1991-),,,,, : , huanglin0126@163.com;,, qdzhangli@ouc.edu.cn Marine Sciences / Vol. 41, No. 6 /

2 UV-2102C ( ( ) ); Sorvall ST 16R ( THERMO SCIENTIFIC ); DYY-6D ( ) 1.2 实验方法 1.2.1,,, ( 20±0.5) ( 40±0.5), 15 d : GB ; : GB ; : GB/T ; : GB Visessanguan W [10], 2 g, 10 4 (15.6 mmol/l Na 2 HPO 4, 3.5 mmol/l KH 2 PO 4, ph7.5), r/min 1 min, r/min 20 min,, 10 4 (0.45 mol/l KCl, 15.6 mmol/l Na 2 HPO 4, 3.5 mmol/l KH 2 PO 4, ph 7.5), r/min 1 min, 20 s r/min 30 min,, mol/l NaOH, 4 h, r/min 20 min,, Huang [11],, 5 g, 10 4 Tris-maleate (50 mmol/l KCl, 20 mmol/l Tris-maleate, ph 7.0), r/min 20 min,,, 6 4 Tris-maleate (0.6 mol/l KCl, 20 mmol/l Tris-maleate, ph 7.0),, 4 60min, r/min 30 min,, 10, r/min 30 min, mol/l KCl 100, 1mL 5 ml, 595 nm,, Ca 2+ -ATPase Benjakul [6] ; Thannhauser [12] SDS-PAGE 0.6 mol/l KCl 1.0g/L Chomnawang [13] 1.. 1, 5min 5% 12%, 1.3 数据处理 Excel 2007 SPSS 22, 3, (P<0.05); OriginPro 结果与分析 2.1 三疣梭子蟹肌肉基本营养成分 1,, 83.97%,, 5.96%, 表 1 三疣梭子蟹主要营养成分分析 Tab. 1 Nutrition composition of muscle of swimming crab (%) (%) (%) (%) 79.54± ± ± ± 肌肉各组分蛋白质含量的变化 4 1,, 42 / 2017 / 41 / 6

3 52.15%,,,,,, 0~30 d,, [14] 0 4,,, 20 40, 20 40, [15],,, Fig. 1 1 Changes in various muscle protein components in swimming crab during frozen storage 2.3 肌原纤维蛋白含量的变化 2, 45 d,, (P<0.05) 20, 40 45d, %, % [16], : [17],,,,, [18],, d 42 d 23% 47.5% [19] 2.4 肌原纤维蛋白中 Ca 2+ -ATPase 活性的变化, ATPase, Ca 2+, Marine Sciences / Vol. 41, No. 6 /

4 2.5 肌原纤维蛋白中总巯基含量的变化 2 Fig. 2 Changes in myofibrillar protein content in swimming crab during frozen storage Ca 2+ -ATPase [20] 3, 90 d, Ca 2+ -ATPase (P<0.05) 30 d, Ca 2+ -ATPase,, (P<0.05) 90 d, 20 Ca 2+ -ATPase 47.8%, 40 Ca 2+ -ATPase 28.3% Benjakul [8], 20 Ca 2+ -ATPase, [21], Ca 2+ -ATPase , Ca 2+ -ATPase,, ATPase [22] 4,, (P<0.05) 20, 15 d 27.6%, 15 d, 40, 30~45 d, 45 d 40, 20,, [22],, [23] Benjakul [6] 20 12,, 2~12 Ramirez [24] d,, 33%,, 4 Fig. 4 Changes in sulfhydryl group content of myofibrillar protein in swimming crab during frozen storage. 2.6 肌原纤维蛋白中二硫键含量的变化 3 Ca 2+ -ATPase Fig. 3 Changes in Ca 2+ -ATPase activities of myofibrillar protein in swimming crab during frozen storage 5, 20 40, (P<0.05), 0~15 d,, 45 d, 40, 20, 0~15 d 4 5,,, 44 / 2017 / 41 / 6

5 Benjakul [25], 18 24, ( ), Ramirez [24],,, 6 SDS-PAGE Fig. 6 SDS-PAGE of myofibrillar protein of swimming crab during frozen storage. 5 Fig. 5 Changes in disulfide bond content of myofibrillar protein in swimming crab during frozen storage. 2.7 肌原纤维蛋白 SDS-PAGE 电泳 6, SDS-PAGE 10, (myosin heavy chain, MHC) (actin) (actomyosin) (myosin light chain, MLC),,,, kda,,, [26] 3 结论,,,,,, (P<0.05) Ca 2+ -ATPase (P<0.05), 30 d,, 20 40,,,, : [1],,,. F2S [J]., 2013, 37(7): Wang Chunlin, Wu Danhua, Cui Zhaoxia, et al. The effects of morphometric traits on body weight in F2 Population of Swimming crab Portunus trituberculatus[j]. Marine Sciences, 2013, 37(7): [2],,,. [J]., 2010, 34(2): Gao Huan, Zhang Benhou, Chen Baiyao, et al. Analysis on lethal effect of adversity on the Portunus trituberculatus[j]. Marine Sciences, 2010, 34(2): [3],,,. [J]., 2013, 34(22): Cui Ruiying, Jiao Xueqin, Cui Bo, et al. Effects of frozen storage on protein denaturation and structure of Argopecten irradiams muscle[j]. Science and Technology of Food Industry, 2013, 34(22): [4],,,. [J]., 2015(6): 136- Marine Sciences / Vol. 41, No. 6 /

6 147. Que Tingting Zheng Jiawen Chen Shiguo, et al. Effect of super-chilling and frozen on the meat quality of Snakehead[J].Journal of Chinese Institute of Food Science and Technology, 2015(6): [5],,,. [J]., 2015, 2: Zhao Xiaoyu, Xiao Shan, Zhang Duo, et al. The quality changes during Metapenaeus ensis freezing storage[j]. Journal of Dalian Polytechnic University, 2015, 2: [6] Benjakul S, Sutthipan N. Muscle changes in hard and soft shell crabs during frozen storage[j]. LWT-food science and Technology, 2009, 42(3): [7],,,. DNA [J]., 2010, 34(11): Chi Dali, GaoHuan, Shen Songdong, et al. Comparison analysis between purple and tea-green individuals of Portunus trituberculatus using mitochondrial partial genes[j]. Marine Sciences, 2010, 2010, 34(11): [8],,,. [J]., 2009, 33(5): Chen Ping, Li Jitao, Lijian, et al.effect on Antioxidant Enzyme System of Portunus trituberculatus Infected by Vibrio alginolyticus[j]. Marine Sciences, 2009, 33(5): [9],,,. TPA [J]., 2011, 36(3): , 135. Yang Jinsheng, Xia Songyang, Fang Yi, et al. Application of TPA in Portunus pelagicus and different freeze storage temperature on its quality[j]. Food Science and Technology, 2011, 36(3): , 135. [10] Visessanguan W, Benjakul S, Riebroy S, et al. Changes in composition and functional properties of proteins and their contributions to Nhamcharacteristics[J]. Meat Science, 2004, 66: [11] Huang J, Zeng S, Xiong S, et al. Steady, dynamic, and creep-recovery rheological properties of myofibrillar protein from grass carp muscle[j]. Food Hydrocolloids, 2016, 61: [12] Thannhauser T W, Konishi Y, Scheraga H A. Analysis for disulfide bonds in peptides and proteins[j]. Methods in enzymology, 1987, 143: [13] Chomnawang C, Nantachai K, Yongsawatdigul J, et al. Chemical and biochemical changes of hybrid catfish fillet stored at 4 C and its gel properties[j]. Food Chemistry, 2007, 103(2): [14],,,. [J]., 2011, 32(5): Li Jiao, Li Xuepen, Li Jianrong, et al. Biochemical Properties of Muscle Protein from Fenneropenaeus chinensis during Chilled Storage[J]. Food Science, 2011, 32(5): [15],,. [J]., 2006, 27(6): Liu Yijie, Xue Changhu, Li Zhaojie. Study on Change in Physico-chemical Properties of Aristichthysnobilis surimi during frozen-storage[j]. Science and Technology of Food Industry, 2006, 27(6): [16]. [D]., Ren Lina. Study on Frozen Denaturation of Miofibrillar Protein of Silver Carp Muscle[D]. Jiangnan University, [17],,,. [J]., 2013, 31(4): Ding Yi, Huang Li, Xia Xiufang, et al. Effect of Frozen Storage on the Structure and Function of Myofibrillar Protein[J]. Packaging and Food Machinery, 2013, 31(4): [18],. [J]., 2011, 32(7): Guo Yuanyuan, Kong Baohua. Advances in the Research of Denaturation and Change in Physico-chemical Properties of Fish Proteins during Frozen Storage[J]. Food Science, 2011, 32(7): [19] Sych J, Lacroix C, Carrier M. Determination of optimal level of lactitol for surimi[j]. Journal of Food Science, 1991, 56(2): [20] 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): [21],,. [J]., 2004, 27(5): Zeng Mingyong, Huang Hai, Li Bafang. Changes of biochemical properties of Aristichthys nobilis muscle protein during frozen-storage[j]. Journal of Fisheries of China, 2004, 27(5): [22] Jiang S, Hwang D, Chen C. Effect of storage temperatures on the formation of disulfides and denaturation of milkfish actomyosin (Chanos chanos)[j]. Journal of Food Science, 1988, 53(5): [23] Benjakul S, Bauer F. Physicochemical and enzymatic changes of cod muscle proteins subjected to different freeze thaw cycles[j]. Journal of the Science of Food and Agriculture, 2000, 80(8): / 2017 / 41 / 6

7 [24] Ramiarez J A, Martian-Polo M O, Bandman E. Fish myosin aggregation as affected by freezing and initial physical state[j]. Journal of Food Science, 2000, 65(4): [25] Benjakul S, Visessanguan W, Thongkaew C, et al. Comparative study on physicochemical changes of muscle proteins from some tropical fish during frozen storage[j]. Food Research International, 2003, 36(8): [26],,,. - [J]., 2011, 32(13): GuoYuanyuan, Kong Baohua, Xia Xiufang, et al. Effect of Number of Freeze-thaw Cycles on Physico-chemical Characteristics of Carp Muscle[J]. Food Science, 2011, 32(13): Changes in the biochemical properties of muscle protein of swimming crab (Portunus trituberculatus) during frozen storage HUANG Lin, ZHANG Li, WU Dan-lu (Ocean University of China, College of Food Science and Engineering, Qingdao , China) Received: October 7, 2016 Key words: swimming crab (Portunus trituberculatus); muscle; protein; biochemical properties Abstract: This study analyzed the changes in the biochemical characteristics of muscle protein during frozen storage at 20 or 40 based on nutrient composition, protein composition, myofibrillar protein content, Ca 2+ -ATPase activity, sulfhydryl group content, disulfide bond content, and SDS-PAGE analysis of myofibrillar protein of swimming crab. Results showed that the muscle of the swimming crab was a typical food with a high protein content. With extension of the duration of frozen storage, the water-soluble protein content increased and then decreased, the salt-soluble protein and -insoluble protein contents decreased, and the content of alkaline-soluble protein increased gradually. Myofibrillar protein content, Ca 2+ -ATPase activity, and sulfhydryl group content decreased with prolongation of the duration of frozen storage, whereas the disulfide bond content showed an increasing trend, with a significant difference between the two groups at 20 and 40 (p < 0.05). The SDS-PAGE results showed that all types of proteins of myofibrillar protein were degraded to different degrees, and the degradation was more apparent at 20 than at 40. Therefore, frozen storage at 40 has minimal effect on the biochemical characteristics of muscle protein. ( 本文编辑 : 康亦兼 ) Marine Sciences / Vol. 41, No. 6 /

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Microsoft Word - 6——黄 琳_news_.doc

Microsoft Word - 6——黄琳_news_.doc