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首页> 外文期刊>The journal of physical chemistry, B. Condensed matter, materials, surfaces, interfaces & biophysical >Solvent Stability Study with Thermodynamic Analysis and Superior Biocatalytic Activity of Burkholderia cepacia Lipase Immobilized on Biocompatible Hybrid Matrix of Poly(vinyl alcohol) and Hypromellose
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Solvent Stability Study with Thermodynamic Analysis and Superior Biocatalytic Activity of Burkholderia cepacia Lipase Immobilized on Biocompatible Hybrid Matrix of Poly(vinyl alcohol) and Hypromellose

机译:聚乙烯醇和羟丙甲纤维素生物相容性杂化基质上固定的洋葱伯克霍尔德氏菌脂肪酶的热力学分析和优异的生物催化活性的溶剂稳定性研究

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In the present study, we have synthesized a biocompatible hybrid carrier of hypromellose (HY) and poly(vinyl alcohol) (PVA) for immobilization of Burkholderia cepacia lipase (BCL). The immobilized biocatalyst HY:PVA:BCL was subjected to determination of half-life time (tau) and deactivation rate constant (K-D) in various organic solvents. Biocatalyst showed higher tau-value in a nonpolar solvent like cyclohexane (822 h) as compared to that of a polar solvent such as acetone (347 h), which signifies better compatibility of biocatalyst in the nonpolar solvents. Furthermore, the K-D-value was found to be less in cyclohexane (0.843 x 10(-3)) as compared to acetone (1.997 x 10(-3)), indicating better stability in the nonpolar solvents. Immobilized-BCL (35 mg) was sufficient to achieve 99% conversion of phenethyl butyrate (natural constituent of essential oils and has wide industrial applications) using phenethyl alcohol (2 mmol) and vinyl butyrate (6 mmol) at 44 degrees C in 3 h. The activation energy (E-a) was found to be lower for immobilized-BCL than crude-BCL, indicating better catalytic efficiency of immobilized lipase BCL. The immobilized-BCL reported 6-fold superior biocatalytic activity and 8 times recyclability as compared to crude-BCL. Improved catalytic activity of immobilized enzyme in nonpolar media was also supported by thermodynamic activation parameters such as enthalpy (Delta H-double dagger), entropy (Delta S-double dagger) and Gibbs free energy (Delta G(double dagger)) study, which showed that phenethyl butyrate synthesis catalyzed by immobilized-BCL was feasible as compared to crude-BCL. The present work explains a thermodynamic investigation and superior biocatalytic activity for phenethyl butyrate synthesis using biocompatible immobilized HY:PVA:BCL in nonaqueous media for the first time.
机译:在本研究中,我们已经合成了羟丙甲纤维素(HY)和聚乙烯醇(PVA)的生物相容性杂合载体,用于固定洋葱伯克霍尔德菌脂肪酶(BCL)。对固定化的生物催化剂HY:PVA:BCL进行各种有机溶剂中的半衰期(tau)和失活速率常数(K-D)的测定。与极性溶剂(如丙酮)(347 h)相比,非极性溶剂(如环己烷)(822 h)中的生物催化剂显示出更高的tau值,这表明生物催化剂在非极性溶剂中具有更好的相容性。此外,与丙酮(1.997 x 10(-3))相比,发现环己烷中的K-D值(0.843 x 10(-3))较小,表明在非极性溶剂中具有更好的稳定性。使用苯乙醇(2 mmol)和丁酸乙烯酯(6 mmol)在44°C下3小时,固定化的BCL(35 mg)足以实现丁酸苯乙基丁酯(精油的天然成分,具有广泛的工业应用)的99%转化率。已发现固定化BCL的活化能(E-a)低于粗制BCL,表明固定化脂肪酶BCL的催化效率更高。固定的BCL报告的生物催化活性是粗BCL的6倍,可回收性是其8倍。焓(ΔH-双匕首),熵(ΔS-双匕首)和吉布斯自由能(ΔG(双匕首))等热力学活化参数也支持固定化酶在非极性介质中的催化活性的提高。结果表明,与粗BCL相比,固定化BCL催化丁酸苯乙酯的合成是可行的。本工作首次解释了在非水介质中首次使用生物相容性固定化HY:PVA:BCL进行丁酸苯乙酯热合成的热力学研究和优异的生物催化活性。

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