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首页> 外文期刊>Bioprocess and Biosystems Engineering >Hydrophobic adsorption in ionic medium improves the catalytic properties of lipases applied in the triacylglycerol hydrolysis by synergism
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Hydrophobic adsorption in ionic medium improves the catalytic properties of lipases applied in the triacylglycerol hydrolysis by synergism

机译:离子介质中的疏水吸附可通过协同作用改善用于三酰基甘油水解的脂肪酶的催化性能

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摘要

It is known that lipases may have their catalytic properties improved by the action of some salts or by the adsorption on hydrophobic supports. However, what we present in this work is more than that: we evaluate the combination of these two factors of hyperactivation of lipases from Acremonium-like ROG 2.1.9, a study that has not been done so far. This work proves that a synergistic effect occurs when the lipases are immobilized on hydrophobic supports at the presence of sodium chloride and are applied in triacylglycerol hydrolysis. This assay made it possible to achieve the highest hyperactivation of 500 % with the lipases immobilized on Phenyl-Sepharose and applied with 0.1 M of sodium chloride. Besides this positive effect on enzyme activity, the use of these two factors led to the thermal stability increasing of the immobilized lipases. For this derivative, the recovered activity was approximately 85 % after 6 h incubated at 55 A degrees C and 1.0 M of the sodium chloride against 50 % of the same derivative without this salt. Furthermore, others assays were performed to prove the evidences about the synergistic effect, showing a promising method to improve the catalytic properties of the lipases from Acremonium-like ROG 2.1.9.
机译:已知脂肪酶可以通过某些盐的作用或通过在疏水性载体上的吸附来改善其催化性能。但是,我们在这项工作中所能提供的不仅是:我们评估了类似Acremonium的ROG 2.1.9中脂肪酶超活化的这两个因素的组合,该研究至今尚未完成。这项工作证明当脂肪酶在氯化钠存在下固定在疏水性载体上并应用于三酰基甘油水解时,会产生协同作用。该测定法使固定在苯基-琼脂糖上的脂肪酶与0.1 M的氯化钠一起应用,可以实现500%的最高超活化。除了对酶活性的这种积极作用外,这两个因素的使用还导致固定化脂肪酶的热稳定性提高。对于此衍生物,在55 A的温度和1.0 M的氯化钠中孵育6小时后,相对于50%的不含该盐的相同衍生物,回收的活性约为85%。此外,进行了其他测定以证明有关协同作用的证据,显示出改善有顶毛状ROG 2.1.9的脂肪酶催化性能的有前途的方法。

著录项

  • 来源
    《Bioprocess and Biosystems Engineering》 |2016年第12期|1933-1943|共11页
  • 作者单位

    UNESP, Dept Chem & Environm Sci, IBILCE, Rua Cristovao Colombo 2265, BR-15054000 Sao Jose Do Rio Preto, SP, Brazil;

    UNESP, Dept Biol, IBILCE, Rua Cristovao Colombo 2265, BR-15054000 Sao Jose Do Rio Preto, SP, Brazil;

    UNESP, Dept Biochem & Chem Technol, IQ, Rua Prof Francisco Degni 55, BR-14800060 Araraquara, SP, Brazil;

    UNESP, Dept Biol, IBILCE, Rua Cristovao Colombo 2265, BR-15054000 Sao Jose Do Rio Preto, SP, Brazil;

    UNESP, Dept Biol, IBILCE, Rua Cristovao Colombo 2265, BR-15054000 Sao Jose Do Rio Preto, SP, Brazil;

    UNESP, Dept Chem & Environm Sci, IBILCE, Rua Cristovao Colombo 2265, BR-15054000 Sao Jose Do Rio Preto, SP, Brazil;

    CSIC, Dept Catalysis, Campus Univ Autonoma, Madrid 28049, Spain;

    UNESP, Dept Chem & Environm Sci, IBILCE, Rua Cristovao Colombo 2265, BR-15054000 Sao Jose Do Rio Preto, SP, Brazil;

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  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

    Lipases; Immobilization; Hyperactivation; Synergism; Hydrolysis;

    机译:脂肪酶;固定化;过度活化;协同作用;水解;

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