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

卷:194

Cao, Hui ; Zhao, Ying ; Zhu, Yu Bing ; Xu, Fei ; Yu, Jing Song ; Yuan, Min

Univ Shanghai Sci & Technol

关键词: Ice-binding collagen peptides;    Thermal hysteresis activity;    Crystallisation inhibition activity;    Antifreeze protein;    Differential scanning calorimetry;    Glass transition temperature;   

DOI  :  10.1016/j.foodchem.2015.08.102

学科分类：食品科学和技术

【 摘 要 】

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.