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中国精品科技期刊2020
李文婷, 边斐, 王翠萍, 陈高, 张燕, 朱友峰, 王世荣, 岳寿松. 凝结芽孢杆菌RY237 β-半乳糖苷酶酶学性质研究[J]. 华体会体育, 2017, (14): 111-115. DOI: 10.13386/j.issn1002-0306.2017.14.022
引用本文: 李文婷, 边斐, 王翠萍, 陈高, 张燕, 朱友峰, 王世荣, 岳寿松. 凝结芽孢杆菌RY237 β-半乳糖苷酶酶学性质研究[J]. 华体会体育, 2017, (14): 111-115. DOI: 10.13386/j.issn1002-0306.2017.14.022
LI Wen-ting, BIAN Fei, WANG Cui-ping, CHEN Gao, ZHANG Yan, ZHU You-feng, WANG Shi-rong, YUE Shou-song. Characterization of β-galactosidase from Bacillus coagulans RY237[J]. Science and Technology of Food Industry, 2017, (14): 111-115. DOI: 10.13386/j.issn1002-0306.2017.14.022
Citation: LI Wen-ting, BIAN Fei, WANG Cui-ping, CHEN Gao, ZHANG Yan, ZHU You-feng, WANG Shi-rong, YUE Shou-song. Characterization of β-galactosidase from Bacillus coagulans RY237[J]. Science and Technology of Food Industry, 2017, (14): 111-115. DOI: 10.13386/j.issn1002-0306.2017.14.022

凝结芽孢杆菌RY237 β-半乳糖苷酶酶学性质研究

Characterization of β-galactosidase from Bacillus coagulans RY237

  • 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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