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Effect of ethyleneoxide groups of anionic surfactants on lipase activity

机译:阴离子表面活性剂的环氧乙烷基团对脂肪酶活性的影响

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The use of enzymes in laundry and dish detergent products is growing. Such tendency implies dedicated studies to understand surfactant-enzyme interactions. The interactions between surfactants and enzymes and their impact on the catalytic efficiency represent a central problem and were here evaluated using circular dichroism, dynamic light scattering, and enzyme activity determinations. This work focuses on this key issue by evaluating the role of the ethyleneoxide (EO) groups of anionic surfactants on the structure and activity of a commercial lipase, and by focusing on the protein/surfactant interactions at a molecular level. The conformational changes and enzymatic activity of the protein were evaluated in the presence of sodium dodecyl sulfate (SDS also denoted as SLE0S) and of sodium lauryl ether sulfate with two EO units (SLE2S). The results strongly suggest that the presence of EO units in the surfactant polar headgroup determines the stability and the activity of the enzyme. While SDS promotes enzyme denaturation and consequent loss of activity, SLE2S preserves the enzyme structure and activity. The data further highlights that the electrostatic interactions among the protein groups are changed by the presence of the adsorbed anionic surfactants being such absorption mainly driven by hydrophobic interactions. (c) 2016 American Institute of Chemical Engineers Biotechnol. Prog., 32:1276-1282, 2016
机译:洗衣和餐具洗涤剂产品中酶的使用正在增长。这种趋势意味着需要专门研究来了解表面活性剂-酶的相互作用。表面活性剂和酶之间的相互作用及其对催化效率的影响是一个中心问题,在这里使用圆二色性,动态光散射和酶活性测定进行了评估。这项工作通过评估阴离子表面活性剂的环氧乙烷(EO)基团对商业脂肪酶的结构和活性的作用,以及在分子水平上关注蛋白质/表面活性剂的相互作用,着重解决了这一关键问题。在十二烷基硫酸钠(SDS也称为SLE0S)和具有两个EO单元的月桂基醚硫酸钠(SLE2S)的存在下评估蛋白质的构象变化和酶活性。结果强烈表明表面活性剂极性头基中EO单元的存在决定了酶的稳定性和活性。 SDS促进酶变性并因此失去活性,而SLE2S保留酶的结构和活性。数据进一步突显了蛋白质基团之间的静电相互作用被吸附的阴离子表面活性剂的存在所改变,所述阴离子表面活性剂主要是由疏水相互作用驱动的。 (c)2016美国化学工程师学会生物技术学会。 Prog。,32:1276-1282,2016

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