Chitinases　play　an　important　role　in　many　industrial　processes,　including　the　preparation　of　oligosaccharides　with　potential　applications.　In　the　present　study,　a　1,713　bp　gene　ofChi1602,　derived　from　a　marine　bacteriumMicrobulbifersp.　BN3,　encoding　a　GH18　family　chitinase,　was　expressed　at　high　levels　inPichia　pastoris.　Distinct　from　most　of　the　marine　chitinases,　the　recombinant　chitinase　1602　exhibited　maximal　activity　at　60　degrees　C　and　over　a　broad　pH　range　between　5.0　and　9.0,　and　was　stable　at　50　degrees　C　and　over　the　pH　range　4.0-9.0.　The　hydrolytic　products　derived　from　colloidal　chitins　comprised　mainly　(GlcNAc)(2)and　GlcNAc,　indicating　that　rChi1602　is　a　GH18　processive　chitinase　in　conformity　with　its　hypothetical　structure.　However,　rChi1602　showed　traces　of　beta-N-acetylglucosaminidase　activity　on　substrates　such　as　powder　chitin,　chitosan,　and　ethylene　glycol　chitin.　The　thermophilic　rChi1602,　which　manifests　adaptation　to　a　wide　pH　range　and　can　be　expressed　at　a　high　level　inP.　pastoris,　is　advantageous　for　applications　in　industrial　processes.