Objective:　Antifreeze　protein　is　becoming　a　popular　research　point　because　it　could　inhibit　ice　crystal　growth,　reduce　damage　of　cell　membranes　and　maintain　products＇　quality　during　food　during　storage　and　handling.　Methods:　This　paper　reports　that　gelatin　peptides　of　a　certain　molecular　size　range　with　compact-packed　structural　domain　derived　from　Papain　hydrolysis　of　bovine　gelatin　are　able　to　inhibit　recrystallization　of　ice　crystals　in　ice　cream　mix　and　show　natural　antifreeze　activity.　Results:　The　optimum　conditions　for　producing　antifreeze　peptides　were　hydrolysis　at　pH　7.0　for　30　min　at　37°C　and　an　Papain　to　gelatin　ratio　of　1:10.　The　gelatin　peptides　were　fractionated　on　size　exclusion　(Sephadex　G-50)　and　ion　exchange　(sulfopropyl-Sephadex　C-25)　columns,　and　the　molecular　mass　distribution　of　the　antifreeze　peptide　fractions　was　determined　by　matrixassisted　laser　desorption　ionization-time-of-flight　(MALDI-TOF)　mass　spectrometry.　The　gelatin　peptide　fractions　in　the　molecular　mass　range　of　700~1318　u　strongly　inhibited　ice　recrystallization　in　ice　cream　mix.　Conclusion:　The　highly　effective　antifreeze　peptide　on　ice　crystal　inhibition　shows　specific　rules　during　cold-heat-stage　cycles,　the　key　approach　is　how　to　control　hydrolysis　conditions.　It　probably　exists　the　surface　hydropholic-complementary　interaction　between　antifreeze　peptide　and　ice　molecules.