Agarases　catalyze　the　hydrolysis　of　agarose　to　oligosaccharides　which　display　an　array　of　biological　and　physiological　functions　with　important　industrial　applications　in　health-related　fields.　In　this　study,　the　gene　encoding　agarase　(Aga-ms-R)　was　cloned　fromMicrobulbifersp.　BN3　strain.　Sequence　alignment　indicated　that　Aga-ms-R　belongs　to　the　GH16　family　and　contains　one　active　domain　and　two　carbohydrate　binding　module　(CBM)　domains.　The　mature　Aga-ms-R　was　expressed　successfully　by　employing　theBrevibacillussystem.　Purified　rAga-ms-R　was　obtained　with　a　specific　activity　of　100.75　U/mg.　rAga-ms-R　showed　optimal　activity　at　50　degrees　C　and　pH　7.0,　and　the　enzyme　activity　was　stable　at　50　degrees　C　and　also　over　the　pH　range　of　5.0-9.0.　After　exposure　of　rAga-ms-R　to　70　degrees　C　for　30　min,　only　partial　enzyme　activity　remained.　Thin　layer　chromatographic　analysis　of　the　enzymatic　hydrolysate　of　agar　obtained　using　rAga-ms-R　disclosed　that　the　hydrolysate　comprised,　in　a　long　intermediate-stage　of　the　hydrolysis　reaction,　mainly　neoagarotetraose　(NA4)　and　neoagarohexaose　(NA6)　but　ultimately,　predominantly　neoagarotetraose　and　trace　amounts　of　neoagarobiose　(NA2).　Hydrolysates　of　the　raw　red　seaweedsGracilaria　sjoestedtiiandGelidium　amansii,　produced　by　incubation　with　rAga-ms-R,　were　mainly　composed　of　neoagarotetraose.　The　results　demonstrate　the　high　efficiency　of　rAga-ms-R　in　producing　neoagaraoligosaccharide　under　low-cost　conditions.