期刊
FOOD CHEMISTRY
卷 194, 期 -, 页码 1245-1253出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2015.08.102
关键词
Ice-binding collagen peptides; Thermal hysteresis activity; Crystallisation inhibition activity; Antifreeze protein; Differential scanning calorimetry; Glass transition temperature
资金
- National High Technology Research and Development Program of China (863 Program) [2013AA102207]
- National Natural Science Funds [31201421, 31101283]
A novel hyperactive ice-binding peptide from porcine collagen was prepared by alkaline protease hydrolysis and a series of column chromatography separations, and then its antifreeze and cryoprotective properties were reported. Using differential scanning calorimetry (DSC), the thermal hysteresis (TH) of ice-binding collagen peptides was closely related to their concentration and crystal fraction. Collagen hydrolysates with maximal TH were obtained by hydrolysis at pH 8.0, DH 15.0%, and 5% alkaline protease at 55 degrees C. After purification by column chromatography, the AP-3 ice-binding collagen peptide (GLLGPLGPRGLL) with 1162.8 Da molecular weights exhibited the highest TH (5.28 degrees C), which can be classified as hyperactive. Recrystallisation and melt-resistance of ice cream were improved by AP-3 ice-binding collagen peptide at 0.2% (w/v) in a similar manner to natural antifreeze proteins. Moreover, the addition of AP-3 collagen peptides in ice cream greatly elevated the glass transition temperature (T-g) to -17.64 degrees C. (C) 2015 Elsevier Ltd. All rights reserved.
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