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Updated: Jul 12, 2026
Identification of Plant Ice-binding Proteins Through Assessment of Ice-recrystallization Inhibition and Isolation Using Ice-affinity Purification
Published on: May 5, 2017
Purification of antifreeze protein from wheat bran (Triticum aestivum L.) based on its hydrophilicity and ice-binding
Chao Zhang1, Hui Zhang, Li Wang
1State Key Laboratory of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi 214122, China.
Abstract:
Wheat-bran ( Triticum aestivum L.) antifreeze protein ( TaAFP) was purified 323-fold to electrophoretic homogeneity with an overall yield of 1.64% from wheat-bran protein by a specific three-step procedure. The three-step procedure was quicker, cheaper, and more effective than the five-step procedure we used earlier. First, TaAFP was concentrated by a phosphate buffer, on the basis of its strong hydrophilicity that was validated by thermal gravimetric analyses and a surface hydrophobicity analysis. Second, TaAFP was trapped in ice crystals for its specific ice-binding capacity, which was proved by ice-binding protocols. Remarkably, the ice-binding step was the most effective step, and the purification factor of this step was up to 270-fold. Finally, TaAFP was purified by HPLC purification, a complementary step for the specific ice-binding protocol, to electrophoretic homogeneity. Our protocols provide peers a novel and effective way for the search and purification of potential AFPs.
