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Improved performance of lipases immobilized on heterofunctional octyl-glyoxyl agarose beads

机译：改善固定在异官能辛基 - 乙醛琼脂糖珠粒上的脂肪酶的性能

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摘要

A new heterofunctional support, octyl-glyoxyl agarose, is proposed in this study. The supports were prepared by simple periodate oxidation of the commercial octyl-agarose, introducing 25 mu mol of glyoxyl groups per wet gram of support. This support was assayed with three different lipases (those from Candida antarctica (form B), Thermomyces lanuginosus (TLL) or Rhizomucor miehei) and the artificial phospholipase Lecitase Ultra. Used at pH 7, the new support maintained as first immobilization step the lipase interfacial activation. Thus, it was possible to have the purification and immobilization of the enzyme in one step. Moreover, stabilization of the open form of the lipase was achieved. The covalent enzyme/support bonds cannot be obtained if the immobilized enzyme was not incubated at alkaline pH value. This incubation at pH 10 of the previously immobilized enzymes produced a smaller decrease in enzyme activity when compared to the direct immobilization of the enzymes on glyoxyl-agarose at pH 10, because the immobilization via interfacial activation promoted a stabilization of the lipases. Except in the case of TLL (covalent attachment involved 70% of the enzyme molecules), covalent immobilization yield was over 80%. The non-covalent attached enzyme molecules were discarded by washings with detergent solutions and the new biocatalysts were compared to the octyl-agarose immobilized enzymes. While the stability in thermal and organic solvents inactivations was increased for Lecitase Ultra, CALB and RML, TLL improved its stability in organic media but its thermal stability decreased after covalent attachment of the interfacially activated enzyme. This stabilization resulted in octyl-glyoxyllipase preparations which presented higher activity in the presence of organic solvents. Finally, while octyl-agarose released enzyme molecules after incubation at high temperatures or in the presence of organic solvents and detergents, the covalently immobilized enzyme remained attached to the support even after boiling the enzyme in SDS, eliminating the risks of product contamination.
机译：在本研究中提出了一种新的异官能载体，辛基 - 乙二醇基琼脂糖。通过简单的羟基琼脂糖的简单氧化来制备支撑件，以每湿克载体引入25μmmol的乙醛基团。这种载体用三种不同的脂肪酶（来自念珠菌南极（B形），Thermomyces Lanuginosus（TLL）或根茎）和人造磷脂酶羟基钛酶超薄的支持。在pH7中使用，作为第一次固定步骤保持新的载体脂肪酶界面活化。因此，可以在一步中具有酶的纯化和固定。此外，实现了脂肪酶的开放形式的稳定化。如果未在碱性pH值下孵育固定化的酶，则不能获得共价酶/载体键。与pH10在pH10的乙氧基 - 琼脂糖上的直接固定相比，在先前固定化酶的pH10的这种温育产生酶活性较小，因为通过界面活化的固定促进脂肪酶的稳定化。除了TLL的情况（共价附着涉及70％的酶分子），共价固定产率超过80％。通过用洗涤剂溶液洗涤弃去非共价附加的酶分子，并将新的生物催化剂与辛基 - 琼脂糖固定的酶进行比较。虽然热和有机溶剂的稳定性因羟桶酶超高，CALB和RML而升高，但TLL改善了其在有机介质中的稳定性，但在界面活化的酶的共价附着后，其热稳定性降低。该稳定化导致辛基 - 甲基甲基纤维酶制剂在有机溶剂存在下呈现更高的活性。最后，虽然在高温下孵育或在有机溶剂和洗涤剂存在下孵育后八氧琼脂糖释放的酶分子，但即使在SDS中沸腾酶后，共价固定的酶也仍然附着在载体上，消除了产品污染的风险。

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  • 来源
    《RSC Advances》 |2015年第15期|共11页
  • 作者

    Rueda Nazzoly; dos Santos Jose C. S.; Torres Rodrigo; Ortiz Claudia; Barbosa Oveimar; Fernandez-Lafuente Roberto;

  • 作者单位

    Campus UAM CSIC Inst Catalysis Dept Biocatalysis Madrid Spain;

    Campus UAM CSIC Inst Catalysis Dept Biocatalysis Madrid Spain;

    Univ Ind Santander Grp Invest Bioquim &

    Microbiol GIBIM Escuela Quim Bucaramanga Colombia;

    Univ Ind Santander Escuela Bacteriol &

    Lab Clin Bucaramanga Colombia;

    Univ Tolima Fac Ciencias Dept Quim Ibague Colombia;

    Campus UAM CSIC Inst Catalysis Dept Biocatalysis Madrid Spain;

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  • 正文语种 eng
  • 中图分类 化学;
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