Volume 10 Issue 4
Aug.  2014
Turn off MathJax
Article Contents
Abstract
References
Related Articles
PAN Chuang, SHOICHIRO Ishizaki, JI Hongwu. β crustacyanin isolated from white leg shrimp (Litopenaeus vannamei) shell by pH-shift processing[J]. South China Fisheries Science, 2014, 10(4): 64-69. DOI: 10.3969/j.issn.2095-0780.2014.04.011
Citation: PAN Chuang, SHOICHIRO Ishizaki, JI Hongwu. β crustacyanin isolated from white leg shrimp (Litopenaeus vannamei) shell by pH-shift processing[J]. South China Fisheries Science, 2014, 10(4): 64-69. DOI: 10.3969/j.issn.2095-0780.2014.04.011
shu

β crustacyanin isolated from white leg shrimp (Litopenaeus vannamei) shell by pH-shift processing

  • 1.

    Guangdong Provincial Key Lab. of Aquatic Product Processing and Safety, Key Lab. of Advanced Processing of Aquatic Products of Guangdong Higher Education Institution, College of Food Science and Technology, Guangdong Ocean University, Zhanjiang 524088, China

  • 2.

    Marine Biomaterial and Functional Biochemistry, Department of Food Science and Technology, Tokyo University of Marine Science and Technology, Minato, Tokyo 108-8477, Japan

More Information
  • Received Date: January 13, 2014
  • Revised Date: March 07, 2014
    Graphical Abstract
    • Abstract

  • We analyzed the effect of pH-shift processing method on isolation of β crustacyanin from white leg shrimp (Litopenaeus vannamei) shell. The recovery rate, purity and secondary structure content of protein were selected as separation characteristics; the protein was recovered by pH-shifting at a 1.0 interval via acid and alkali. Under these conditions, the protein recovery rate reached 47.5% with purity of 78.23%;the molecular weight was 45 000 Da analyzed by SDS-PAGE and Size Exclusion Chromatography; the maximum and minimum solubilities were obtained at pH 3.0 (60.5%), 11.0 (55.7%) and 5.0 (15.4%), respectively; the iso-electric point determined by Isoelectric Focusing Electrophoresis was about 5.6. Secondary structure content obtained by circular dichroism spectroscopy and spectrum revealed that β crustacyanin mainly existed in α helix form and contained nearly 70.1% α helices via pH-shift processing.

    • FullText(HTML)
    • References (26)
  • [1]
    HULTIN H O, KELLEHER S D. Process for isolating a protein composition from a muscle source and protein composition: US, DE19976027039[P]. 1997-10-09. https://www.freepatentsonline.com/6005073.html
    [2]
    UNDELAND I, KELLEHER S D, HULTIN H O. Recovery of functional proteins from herring (Clupea harengus) light muscle by an acid or alkaline solubilization process [J]. J Agric Food Chem, 2002, 50 (25): 7371-7379. doi: 10.1021/jf020199u
    [3]
    CHOI Y J, PARK J W. Acid-aided protein recovery from enzyme-rich Pacific whiting [J]. J Food Sci, 2002, 67 (8): 2962-2967. doi: 10.1111/j.1365-2621.2002.tb08846.x
    [4]
    KRISTINSSON H, DEMIR N. Functional fish protein ingredients from fish species of warm and temperate waters: comparison of acid- and alkali-aided processing vs. conventional surimi processing[C]. Advances in Seafood Byproducts 2002 Conference Proceedings. Anchorage: Alaska Sea Grant College Program University of Alaska, 2003: 277-295.
    [5]
    YONGSAWATDIGUL J, PARK J W. Effects of alkali and acid solubilization on gelation characteristics of rockfish muscle proteins [J]. J Food Sci, 2004, 69(7): 499-505. doi: 10.1111/j.1365-2621.2004.tb13642.x
    [6]
    MIRELES DeWITT C A, NABORS R L, KLEINHOLZ C W. Pilot pant scale production of protein from catfish treated by acid solubilization/isoelectric precipitation [J]. J Food Sci, 2007, 72 (6): 351-355. doi: 10.1111/j.1750-3841.2007.00407.x
    [7]
    NOLSOE H, UNDELAND I. The acid and alkaline solubilization process for the isolation of muscle proteins: state of the art [J]. Food Bioprocess Tech, 2009, 2 (1): 1-27. doi: 10.1007/s11947-008-0088-4
    [8]
    GIGLIOTTI J C, JACZYNSKI J, TOU J C. Determination of the nutritional value, protein quality and safety of krill protein concentrate isolated using an isoelectric solubilization/precipitation technique [J]. Food Chem, 2008, 111 (1): 209-214. doi: 10.1016/j.foodchem.2008.03.030
    [9]
    AMAROWICZ R, SYNOWIECKI J, SHAHIDI F. Sephadex LH-20 separation of pigments from shells of red sea urchin (Strongylocentrotus franciscanus) [J]. Food Chem, 1994, 51(2): 227-229. doi: 10.1016/0308-8146(94)90262-3
    [10]
    TANAKA Y, MATSUGUCHI H, KATAYAMA T, et al. The biosynthesis of astaxanthin. ⅩⅥ. The carotenoids in crustacean [J]. Comp Biochem Phys B, 1976, 54(3): 391-394. doi: 10.1016/0305-0491(76)90263-7
    [11]
    胡雅馨, 惠伯棣, 李阳. 食用虾中虾青素类化合物的含量和组成[J]. 食品科学, 2007, 28(8): 389-392. doi: 10.3321/j.issn:1002-6630.2007.08.094
    [12]
    CIANCI M, RIZKALLAH P J, OLCZAK A, et al. Structure of lobster apocrustacyanin A1 using softer X-rays [J]. Acta Crystallographica D, 2001, 57(9): 1219-1229. doi: 10.1107/S0907444901009350
    [13]
    黄卉, 李来好, 杨贤庆, 等. 对虾产品质量分级要素及评价技术[J]. 中国水产科学, 2010, 17(6): 1371-1376. https://d.wanfangdata.com.cn/periodical/zgsckx201006030
    [14]
    ZAGALSKY P F. Invertebrate carotenoproteins [J]. Method Enzymol, 1985, 111(9): 216-247. https://www.sciencedirect.com/science/article/pii/S0076687985110116
    [15]
    李芳, 刘俊荣, 梁姗姗, 等. 南极磷虾蛋白质的分离特性及其组分分析[J]. 大连海洋大学学报, 2013, 28(2): 191-194. doi: 10.3969/j.issn.2095-1388.2013.02.015
    [16]
    CLARKE D T. Circular dichroism and its use in protein folding studies [J]. Curr Protoc Protein Sci, 2012, 28: 1-17. doi: 10.1007/978-1-60327-223-0_5
    [17]
    JASCO Corporation [Z]. J-700 for Windows Software Manual, 1995: 10.
    [18]
    TIMME E, WALWYN D, BAILEY A. Characterisation of the carotenoprotein found in carapace shells of Jasus lalandii [J]. Comp Biochem Phys B, 2009, 153(1): 39-42. doi: 10.1016/j.cbpb.2009.01.007
    [19]
    CHAYEN N E, CIANCI M, GROSSMANN J G, et al. Unravelling the structural chemistry of the colouration mechanism in lobster shell [J]. Acta Crystallogr D, 2003, 59(12): 2072-2082. doi: 10.1107/S0907444903025952
    [20]
    SREERAMA N, WOODY R W. Computation and analysis of protein circular dichroism spectra [J]. Meth Enzymol, 2004, 383(13): 318-351. doi: 10.1016/S0076-6879(04)83013-1
    [21]
    KRISTINSSON H G, LIANG Y. Effect of pH-shift processing and surimi processing on Atlantic croaker muscle proteins [J]. J Food Sci, 2006, 71(5): 304-312. doi: 10.1111/j.1750-3841.2006.00046.x
    [22]
    PALAFOX H, CÓRDOVA-MURUETA J H, NAVARRETE del TORO M A, et al. Protein isolates from jumbo squid (Dosidicus gigas) by pH-shift processing [J]. Process Biochem, 2009, 44(5): 584-587. doi: 10.1016/j.procbio.2009.02.011
    [23]
    刘俊荣, 贺凌, 汪涛, 等. 不同pH条件下罗非鱼肌肉蛋白分离效果及其功能特性的研究[J]. 水产科学, 2010, 29(6): 317-320. doi: 10.3969/j.issn.1003-1111.2010.06.002
    [24]
    KRISTINSSON H G, THEODORE A E, DEMIR N, et al. A comparative study between acid-and alkali-aided processing and surimi processing for the recovery of proteins from channel catfish muscle [J]. J Food Sci, 2005, 70(4): 298-306. doi: 10.1111/j.1365-2621.2005.tb07177.x
    [25]
    张祥刚, 周爱梅, 林晓霞, 等. 南美白对虾虾头、虾壳化学成分的对比研究[J]. 现代食品科技, 2009, 25(3): 224-227. doi: 10.3969/j.issn.1673-9078.2009.03.002
    [26]
    CHEN Y C, JACZYNSKI J. Protein recovery from rainbow trout (Oncorhynchus mykiss) processing byproducts via isoelectric solubilization/precipitation and its gelation properties as affected by functional additives[J]. J Agric Food Chem, 2007, 55(22): 9079-9088. https://pubmed.ncbi.nlm.nih.gov/17902629/
    • Related Articles

  • Related Articles

    [1]LU Chen, HU Xiao, CHEN Shengjun, WU Yanyan, HUANG Hui, XIANG Huan, QI Bo, DENG Jianchao. Preparation, in vitro activity and physicochemical properties of collagenase inhibitory peptide from tilapia skin[J]. South China Fisheries Science, 2024, 20(2): 150-159. DOI: 10.12131/20230205
    [2]LENG Meng, LIN Duanquan, WENG Ling, ZHANG Lingjing, MIAO Song, CAO Minjie, SUN Lechang. Enzymatic extraction and physicochemical properties of Porphyra haitanensis protein[J]. South China Fisheries Science, 2023, 19(3): 140-150. DOI: 10.12131/20220242
    [3]HUO Yumei, HU Xiao, WU Yanyan, JIANG Jinjin. Preparation, separation and physicochemical properties of α-glucosidase inhibitory peptides from Miichthys miiuy[J]. South China Fisheries Science, 2023, 19(3): 98-109. DOI: 10.12131/20220269
    [4]WANG Lunan, YANG Shaoling, QI Bo, YANG Xianqing, LI Chunsheng, MA Haixia, HU Xiao. Effect of three modification methods on physicochemical properties of agar[J]. South China Fisheries Science, 2021, 17(2): 97-103. DOI: 10.12131/20200197
    [5]HUANG Haichao, WANG Jinxu, PAN Chuang, YANG Xianqing, QI Bo, LI Laihao, ZHAO Yongqiang. Degradation of Porphyra haitanensis polysaccharide by ultrasonic assisted hydrogen peroxide method and its antioxidant activity analysis[J]. South China Fisheries Science, 2020, 16(1): 110-119. DOI: 10.12131/20190220
    [6]LI Shasha, CAO Yucheng, HU Xiaojuan, LI Zhuojia, XU Yu, YANG Keng, XU Chuangwen, WEN Guoliang. Optimization for cultivation parameters of Bacillus sp. A4 using response surface methodology[J]. South China Fisheries Science, 2017, 13(5): 85-93. DOI: 10.3969/j.issn.2095-0780.2017.05.012
    [7]LI Laihao, YE Ge, HAO Shuxian, WEI Ya, HUANG Hui, LIN Wanling, CEN Jianwei. Comparison on quality of tilapia under two kinds of culture modes[J]. South China Fisheries Science, 2013, 9(5): 1-6. DOI: 10.3969/j.issn.2095-0780.2013.05.001
    [8]WANG Yajun, LIN Wenhui, WU Shuqin, PAN Houjun, SHI Cunbin. Preliminary study of restoration methods for sediment of Siniperca chuatsi ponds[J]. South China Fisheries Science, 2010, 6(5): 7-12. DOI: 10.3969/j.issn.1673-2227.2010.05.002
    [9]PENG Wen, JIANG Jing-zhe, WANG Jiang-yong, DING Xue-juan. Effect of physicochemical factors on phenoloxidase activity of hemocyanin from abalone Haliotis diversicolor[J]. South China Fisheries Science, 2010, 6(2): 1-6. DOI: 10.3969/j.issn.1673-2227.2010.02.001
    [10]ZHANG Li, LIU Li, YUAN Yuan, GU Ji-rui, WU Jiang, XIE Xian-lian, XU Heng. Study on an agglutinin isolated from serum of Spinibarbus sinensis[J]. South China Fisheries Science, 2006, 2(6): 39-44.

  • Cited by

    Periodical cited type(18)

    1. 任梦婷，孙若文，尹涛，尤娟，熊善柏. 鲢鱼鳞冻预制菜的熬煮工艺优化及其凝胶特性. 华中农业大学学报. 2023(01): 170-177 .
    2. 李佳，陶晓倩，张强，雷静文，程岚，张纯刚. 温度对明胶膜性能影响的研究进展. 食品研究与开发. 2023(24): 172-178 .
    3. 李娜，李向力，张亚勋，王珂，闫格，高火亮. 驴皮制胶过程中重金属的去除. 中国食品添加剂. 2022(04): 28-33 .
    4. 任章睿，熊善柏，胡杨，尹涛，李金玲，安玥琦. 真空浸渍处理对调理草鱼片品质的影响. 食品安全质量检测学报. 2020(12): 3831-3839 .
    5. 窦鑫，黄克辉，魏涯，吴燕燕，张钰婷. 海鲈鱼鳞胨工艺技术优化及品质分析. 食品与发酵工业. 2020(22): 147-152 .
    6. 吴燕燕，赵志霞，李来好，林婉玲，邓建朝，杨贤庆. 响应面法优化复合咸味剂腌制罗非鱼片的工艺. 水产学报. 2019(02): 532-546 .
    7. 曾少葵，吴文龙，章超桦，王瑶珠，苏伟明. 金鲳鱼皮明胶流变性质. 广东海洋大学学报. 2019(06): 108-114 .
    8. 韩霜，马良，杨晖，黄丹丹，张宇昊. 大目金枪鱼皮明胶的理化性质及结构分析. 食品科学. 2018(10): 40-45 .
    9. 陈正平，熊磊，卢玉婷，李敏，曾芳，蒋柏泉. 热水法提取鳙鱼鱼鳞明胶的工艺优化和产品分析. 食品工业. 2018(10): 128-132 .
    10. 吴锁连，康怀彬，李冬姣. 鱼鳞有效成分提取技术的研究进展. 安徽农业科学. 2017(27): 110-112+141 .
    11. 赵志霞，吴燕燕，李来好，陈胜军，林婉玲，邓建朝. 低盐罗非鱼片快速腌制的工艺研究. 南方水产科学. 2017(06): 105-114 . 本站查看
    12. 吴燕燕，朱小静，李来好，杨贤庆，陈胜军，林婉玲，魏涯. 养殖日本真鲈和大口黑鲈原料特性比较. 海洋渔业. 2016(05): 507-515 .
    13. 李晓，王颖，李红艳，吴志宏，刘天红，孙元芹，刘伟. 多棘海盘车体壁脱钙工艺的研究. 食品工业科技. 2016(10): 307-310+315 .
    14. 杨丽芝，杨贤庆，黄卉，李来好，邓建朝，赵永强，杨少玲. 响应面法优化南海鸢乌贼墨汁多糖提取工艺. 食品工业科技. 2016(18): 292-296 .
    15. 孙蕾蕾，黄卉，李来好，杨贤庆，郝淑贤，魏涯，杨少玲，胡晓. 冰藏罗非鱼片能量代谢酶与品质的相关性分析. 食品工业科技. 2015(11): 70-74 .
    16. 樊世芳，王利强，游柳青，卢立新，郑琪欢. 鱼鳞胶原蛋白的研究进展. 包装工程. 2014(23): 6-12 .
    17. 周婉君，李来好，吴燕燕，郝淑贤，岑剑伟，魏涯，林婉玲，杨少玲. 罗非鱼休闲食品的工艺技术研究. 食品工业科技. 2014(18): 256-259+263 .
    18. 张强，王倩倩，陆剑锋，吕顺，叶应旺，姜绍通，林琳. 水产动物明胶的研究进展. 明胶科学与技术. 2013(03): 147-153 .

    Other cited types(14)

Catalog

    Get Citation
    PDF
    XML
    Article views (3385) PDF downloads (1718) Cited by(32)
    Related

    Supported by: Beijing Renhe Information Technology Co., Ltd.  

    /

    DownLoad:  Full-Size Img  PowerPoint
    Return
    Return