Sericin　peptides　(SPs)　are　a　new　cryoprotectant　with　protecting　abilities　for　organisms　or　biomacromolecule　in　food　stuff　from　freezing　injury　in　subzero　environments.　The　extraction　of　ice-binding　sericin　peptides　(I-SPs)　by　ice　affinity　extraction　adsorption　and　their　cryoprotective　effect　on　Lactobacillus　Delbrueckii　Subsp.　bulgaricus　LB340　LYO　during　frozen　storage　was　studied　in　this　paper.　The　optimal　extraction　conditions　by　application　of　a　new　and　assembled　ice　absorption　apparatus　were　identified　as　temperature　of　-3　A　degrees　C,　SPs　concentration　of　5　mg/mL,　and　extraction　time　of　3　h.　Compared　with　SPs,　I-SPs　were　found　to　be　increased　in　the　contents　of　some　special　amino　acid　residues,　including　Ser,　Thr,　Gly,　and　Ala,　which　might　be　relative　with　the　ice　affinity　as　well　as　the　cryoprotective　activity　of　ice-structuring　proteins.　Meanwhile,　the　molecular　mass　distribution　data　implied　that　the　free　amino　acids　in　the　SPs　could　be　excluded　from　the　ice　affinity　adsorption,　and　peptides　containing　3-6　amino　acid　residues　might　be　more　liable　to　adsorb　to　ice　surface.　Furthermore,　with　addition　of　I-SPs　at　concentrations　of　more　than　0.01　mg/mL,　LB340　strain　had　a　higher　survival　rate　after　frozen　storage　compared　to　the　water　control　as　well　as　SPs　(p　＜　0.05).