Antifreeze and cryoprotective activities of ice-binding collagen peptides from pig skin

作者：Cao, Hui; Zhao, Ying; Zhu, Yu Bing; Xu, Fei^*; Yu, Jing Song; Yuan, Min

来源：Food Chemistry, 2016, 194: 1245-1253.

DOI：10.1016/j.foodchem.2015.08.102

• Ice-binding collagen peptides
• Thermal hysteresis activity
• Crystallisation inhibition activity
• Antifreeze protein
• Differential scanning calorimetry
• Glass transition temperature

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.

• 出版日期2016-3-1
• 单位上海理工大学