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Characterization of endo-beta-mannanase from Enterobacter ludwigii MY271 and application in pulp industry

机译:路德维氏肠杆菌MY271内切-甘露聚糖酶的表征及其在制浆工业中的应用

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摘要

beta-Mannanases are the second most important enzymes for the hydrolysis of hemicelluloses. An endo-beta-mannanase from Enterobacter ludwigii MY271 was purified at 11.7 +/- 0.2-fold to homogeneity with a final recovery of 15.2 +/- 0.2 %. Using purified beta-mannanase protein and SDS-PAGE, the molecular mass was found to be 43.16 kDa. The optimal pH and temperature of the enzyme was found to be 7.0 and 55 A degrees C, respectively. The beta-mannanase activity was stable over a broad pH range of pH 2.0-10.0. In addition, the purified enzyme was highly activated by several metal ions and chemical reagents, such as Mg2+, l-cysteine, glutathione (GSH) and beta-mercaptoethanol. Whereas the enzyme was strongly inhibited by Hg2+, Cu2+, N-bromosuccinimide (NBS), 1-ethyl-3-(3-dimethyl-amino-propyl)-carbodiimide (EDC), phenylmethanesulfonyl fluoride (PMSF), and sodium dodecyl sulfate (SDS). The beta-mannanase was highly active towards glucomannan, and showed endo-activity by producing a mixture of oligosaccharides. Moreover, the enzyme displayed a classical endo-type mode on mannooligosaccharides. The beta-mannanase coupled with xylanase significantly improved the brightness of kraft pulp, whereas it has no remarkable effect on the tensile strength of the pulp. Our functional studies of the purified beta-mannanase indicate that the enzyme is beneficial to industrial applications, in particular, biotechnological processes, such as food, feed and pulp industry.
机译:β-甘露聚糖酶是第二水解半纤维素的最重要的酶。来自路德维氏肠杆菌MY271的内切-β-甘露聚糖酶以11.7 +/- 0.2倍的纯度被纯化至同质,最终回收率为15.2 +/- 0.2%。使用纯化的β-甘露聚糖酶蛋白和SDS-PAGE,发现分子量为43.16 kDa。发现该酶的最佳pH和温度分别为7.0和55 A℃。 β-甘露聚糖酶活性在pH 2.0-10.0的宽pH范围内稳定。此外,纯化的酶还被几种金属离子和化学试剂(例如Mg2 +,L-半胱氨酸,谷胱甘肽(GSH)和β-巯基乙醇)高度活化。而该酶受到Hg2 +,Cu2 +,N-溴琥珀酰亚胺(NBS),1-乙基-3-(3-二甲基-氨基-丙基)-碳二亚胺(EDC),苯基甲磺酰氟(PMSF)和十二烷基硫酸钠( SDS)。 β-甘露聚糖酶对葡甘露聚糖具有高活性,并通过产生寡糖混合物显示出内在活性。此外,该酶对甘露寡糖表现出经典的内切型模式。 β-甘露聚糖酶与木聚糖酶结合可显着提高牛皮纸浆的亮度,而对纸浆的拉伸强度没有显着影响。我们对纯化的β-甘露聚糖酶的功能研究表明,该酶有益于工业应用,特别是生物技术过程,例如食品,饲料和纸浆工业。

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  • 来源
    《Bioprocess and Biosystems Engineering》 |2017年第1期|35-43|共9页
  • 作者单位

    Hubei Univ Technol, Hubei Prov Cooperat Innovat Ctr Ind Fermentat, Key Lab Fermentat Engn, Minist Educ, Wuhan 430068, Peoples R China;

    Hubei Univ Technol, Hubei Prov Cooperat Innovat Ctr Ind Fermentat, Key Lab Fermentat Engn, Minist Educ, Wuhan 430068, Peoples R China;

    Hubei Univ Technol, Hubei Prov Cooperat Innovat Ctr Ind Fermentat, Key Lab Fermentat Engn, Minist Educ, Wuhan 430068, Peoples R China;

    Hubei Univ Technol, Hubei Prov Cooperat Innovat Ctr Ind Fermentat, Key Lab Fermentat Engn, Minist Educ, Wuhan 430068, Peoples R China;

    Hubei Univ Technol, Hubei Prov Cooperat Innovat Ctr Ind Fermentat, Key Lab Fermentat Engn, Minist Educ, Wuhan 430068, Peoples R China;

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  • 正文语种 eng
  • 中图分类
  • 关键词

    End-beta-mannanases; Enterobacter ludwigii MY271; Characterization; Oligosaccharides production;

    机译:β-甘露聚糖末端酶;路德维氏肠杆菌MY271;表征;寡糖生产;

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