Investigation of the physiochemical properties, cryoprotective activity and possible action mechanisms of sericin peptides derived from membrane separation
Sericin peptides (3K-SP) were rich in some amino acids associated with the cryoprotective activity. 3K-SP induced ice to melt at lower temperatures and in a shorter time compared to control solution. 3K-SP inhibited ice recrystallization by maintaining irregular ice crystals as smaller sizes. 3K-SP provided high cryogenic optimal protection of L. Bulgaricus cells at 1.0 mg/mL and pH 7.0. 3K-SP exerted cryoprotection by making cells in a glassy matrix and keeping the membrane integrity.