Membrane-bound polyphenol oxidase （mPPO） in Fuji apple （Malus domestica Borkh. cv. Red Fuji） （mPPO） accounted for about 90% of apple polyphenol oxidase， while there was little knowledge about mPPO properties and functions. In this paper， we analyzed bioinformatics of mPPO （including amino acid composition and properties， secondary structure， trans-membrane structure， subcellular localization， etc.） based on the prophase of mPPO primary sequence， using prediction technology， in order to provide new ideas to study mPPO structure and provide a theoretical basis for exploring the role of mPPO in apple postharvest physiology. The results showed that： the highest level of amino acid content in mPPO was Thr（8.7%）， followed by the Asp （7.8%） and Leu （7.8%）. There were no Pyl and Sec. Histidine （His） Play an important role on mPPO function while its content is just 2.5%. From the result of amino acid composition， the proportion of hydrophobic amino acids in mPPO was above 40% and the exposed surfaces （exposed） residues was 45.74%. Theory of mPPO stability index was 41.72， which indicates that the mPPO was an unstable protein. The secondary structure of mPPO showed that the alpha helix was 18.67%， and beta folding structure content was 23.33%， the rest of the random coil was 58.00%. mPPO protein did not contain 310 spiral， spiral， Pi beta bridge， beta Angle， bending structure， and other structures. The calculation of sub-cellular localization indicated that mPPO from Fuji was a hydrophobic membrane protein in chloroplast with a 39 amino acid residues signal peptide and two extracellular membrane peptides （82-97 for N-， 548-567 for C-）.