Characterization of β-galactosidase from Bacillus coagulans RY237
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摘要: 为研究乳品中具有应用价值的乳糖酶,以乳糖为唯一碳源,用邻硝基苯酚-β-D-半乳糖苷（ONPG）法,从产乳酸的细菌中筛选出了产乳糖酶活力高的菌株RY237,其活性达4.98 U/m L,鉴定为凝结芽孢杆菌。研究了乳糖酶的酶学性质,该酶最适反应温度和最适p H分别为50℃和6.0。该酶在温度4050℃具有良好的稳定性;p H5.58.0表现稳定,p H7.0出现酶活峰值。金属离子Ca2+、K+、Zn2+、Mn2+、Na+、Mg2+对酶活具有抑制作用,Cu2+对酶活具有完全抑制作用,EDTA对酶活具有激活作用。凝结芽孢杆菌RY237乳糖酶活性高、性能优良,具有应用价值。Abstract: A novel lactase-producing bacterium RY237 was selected based on β-galactosidase activity using lactose as sole carbon media, and was identified as Bacillus coagulans RY327. The activity of lactase reached 4.98 U/m L. The optimum temperature and optimum p H of β-galactosidase were 50 ℃ and 6.0, respectively. The enzyme was stable at p H5.5 ~ 8.0, with peak activity at p H7.0, and it was also stable at 4050 ℃. The activity of β-galactosidase was inhibited by Ca2+, K+, Zn2+, Mn2+, Na+, Mg2+and completely inhibited by Cu2+. Its activity was promoted by ethylene diamine tetraacetic acid ( EDTA) .The high activity, thermostability and p H-stability make this enzyme potentially useful in dairy industry.
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