Characterization of β-1,4-D-mannanase from Bacillus subtilis MSJ-5
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摘要: 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32h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。Abstract: The characterization ofβ-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 pH7.0and50℃,and it is stabilized at pH 5.0-7.0.Furthermore,Konjac mannan was efficiently hydrolyzed by the MSJ-5mannanase and its viscosity was reduced significantly,and the product was mainly a mannooligsaccharide.Our results suggest that MSJ-5has the application potential to the feed enzyme preparation and oligosaccharide industry.
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Key words:
- mannanase /
- mannooligsaccharedes /
- dynamic viscosity /
- feed
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