A　novel　kind　of　lutein-protein　complex　(LPC)　was　extracted　from　heterotrophic　Chlorella　vulgaris　through　aqueous　extraction.　The　purification　procedure　contained　solubilization　of　thylakoid　proteins　by　a　zwitter-ionic　detergent　CHAPS,　anion　exchange　chromatography　and　gel　filtration　chromatography.　Both　wavelength　scanning　and　HPLC　analysis　confirmed　that　lutein　was　the　major　pigment　of　the　protein-based　complex,　and　the　mass　ratio　of　lutein　and　protein　was　determined　to　be　9.72　:　100.　Besides　showing　lipid　peroxidation　inhibition　activity　in　vitro,　LPC　exerted　significant　antioxidant　effects　against　ABTS　and　DPPH　radicals　with　IC50　of　2.90　and　97.　23　mu　g　mL(-1),　respectively.　Meanwhile,　in　vivo　antioxidant　activity　of　the　complex　was　evaluated　using　the　mice　hepatotoxicity　model;　LPC　significantly　suppressed　the　carbon　tetrachloride-induced　elevation　of　serum　alanine　aminotransferase　(ALT)　and　aspartate　aminotransferase　(AST)　activities,　and　decreased　hepatic　malondialdehyde　(MDA)　levels　and　the　hepatosomatic　index.　Moreover,　LPC　could　effectively　restore　the　activities　of　superoxide　dismutase　(SOD),　catalase　(CAT)　and　glutathione　peroxidase　(GSH-Px)　in　the　treated　mice　livers.　Our　findings　further　the　progress　in　the　research　of　natural　protein-based　lutein　complexes,　suggesting　that　LPC　has　the　potential　in　hepatoprotection　against　chemical　induced　toxicity　and　in　increasing　the　antioxidant　capacity　of　the　defense　systemin　the　human　body.