The characterization of β-1 ,4-D-mannanase producd by MSJ-5, isolated from konjac soil, was investigated.Cultivating in shake-flask at 32℃ for 32 h,the enzyme activity reached the highest value and then the mount ofβ-1,4-D-mannanase peaked.In addition,the optimum conditions for the enzymatic activity are pH7.0 and 50℃,and it is stabilized at pH 5.0 -7.0. Furthermore,Konjac mannan was efficiently hydrolyzed by the MSJ-5 mannanase and its viscosity was reduced significantly,and the product was mainly a mannooligsaccharide.Our results suggest that MSJ-5 has the application potential to the feed enzyme preparation and oligosaccharide industry.%对土壤中分离的1株产β-甘露聚糖酶的枯草芽孢杆菌 MSJ-5进行产酶性质的研究。菌株 MSJ-5在发酵培养基中培养32 h 达到产酶高峰。β-甘露聚糖酶为粗酶液的主要组分，酶学性质的研究显示该酶最适反应温度为50℃，最适反应 pH 为7．0，在 pH 5．0～7．0能保持较好的稳定性。水解魔芋甘露聚糖及水解产物分析试验结果表明菌株 MSJ-5产生的β-甘露聚糖酶对魔芋甘露聚糖有显著降粘效果，水解产物以甘露寡糖为主。研究结果显示，菌株 MSJ-5产生的β-甘露聚糖酶有应用到饲料添加和功能性寡糖行业的潜力。
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