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Frontiers of Chemical Science and Engineering

ISSN 2095-0179

ISSN 2095-0187(Online)

CN 11-5981/TQ

Postal Subscription Code 80-969

2018 Impact Factor: 2.809

Front. Chem. Sci. Eng.    2009, Vol. 3 Issue (4) : 383-385    https://doi.org/10.1007/s11705-009-0249-7
Research articles
Purification of ice structuring protein complexes from winter wheat using Triton X-114 phase partitioning
Huaneng XU,Haiying CHEN,Weining HUANG,
State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi 214122, China;
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Abstract Ice structuring proteins (ISPs) isolated from the cold-acclimated plants have a great potential in improving the quality of frozen foods. The purification of ISP complexes from winter wheat was achieved using an aqueous two-phase system of Triton X-114. The highly reactive phenols were removed, and the ISP complexes remained in the aqueous phase after phase separation. The ISP complexes treated by this procedure retained higher thermal hysteresis activity than those treated by ammonium sulfate method. The phase separation technique provides a simple and mild way for removing phenols from ISP complexes.
Issue Date: 05 December 2009
 Cite this article:   
Haiying CHEN,Huaneng XU,Weining HUANG. Purification of ice structuring protein complexes from winter wheat using Triton X-114 phase partitioning[J]. Front. Chem. Sci. Eng., 2009, 3(4): 383-385.
 URL:  
https://academic.hep.com.cn/fcse/EN/10.1007/s11705-009-0249-7
https://academic.hep.com.cn/fcse/EN/Y2009/V3/I4/383
Kristiansen E, Zachariassen K E. The mechanism by which fishantifreeze proteins cause thermal hysteresis. Cryobiology, 2005, 51: 262–280

doi: 10.1016/j.cryobiol.2005.07.007
Feeney R E, Yeh Y. Antifreeze proteins: currentstatus and possible food uses. Trends inFood Science and Technology, 1998, 9: 102–106

doi: 10.1016/S0924-2244(98)00025-9
Zhang C, Zhang H, Wang L. Effect of carrot (Daucus carota) antifreeze proteinson the fermentation capacity of frozen dough. Food Research International, 2007, 40: 763–769

doi: 10.1016/j.foodres.2007.01.006
Hon W C, Griffith M, Chong P, Yang D S C. Extractionand isolation of antifreeze proteins from winter rye (Secale cereale L.) leaves. Plant Physiology, 1994, 104: 971–980
Kuiper M J, Lankin C, Gauthier S Y, Walker V K, Davies P L. Purification of antifreeze proteins byadsorption to ice. Biochemical and BiophysicalResearch Communications, 2003, 300: 645–648

doi: 10.1016/S0006-291X(02)02900-5
Simpson D J, Smallwood M, Twigg S, Doucet C J, Ross J, Bowles D J. Purification and characterization of an antifreeze protein from Forsythia suspense (L.). Cryobiology, 2005, 51: 230–234

doi: 10.1016/j.cryobiol.2005.06.005
Yu X M, Griffith M. Antifreeze proteins in winterrye leaves form oligomeric complexes. PlantPhysiology, 1999, 119: 1361–1369

doi: 10.1104/pp.119.4.1361
Sanchez-Ferrer A, Perez-Gilabert M, Nunez E, Bru R, Garcia-Carmona F. Triton X-114 phase partitioningin plant protein purification. Journalof Chromatography A, 1994, 668: 75–83

doi: 10.1016/0021-9673(94)80094-4
Zhang C, Zhang H, Wang L, Zhang J, Yao H. Purification of antifreeze protein fromwheat bran (Triticum aestivum L.) based on its hydrophilicity andice-binding capacity. Journal of Agricultraland Food Chemistry, 2007, 55: 7654–7658

doi: 10.1021/jf0715065
Kidron M, Harel M, Mayer A M. Catechol oxidase activity in grapes and wine. American Journal of Enology and Viticulture, 1978, 219: 30–35
Raymond J A, DeVries A L. Adsorption inhibition asa mechanism of freezing resistance in polar fishes. Proceedings of the National Academy of Sciences (USA), 1977, 74: 2589–2593

doi: 10.1073/pnas.74.6.2589
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