固定化 Candida rugosa 脂肪酶于聚(3-羟基丁酸-co-羟基戊酸酯)：一种新的环保载体。
Immobilization of Candida rugosa lipase on poly(3-hydroxybutyrate-co-hydroxyvalerate): a new eco-friendly support.
机构信息
Universidade Tiradentes, Av. Murilo Dantas, 300, Bairro Farolândia, Aracaju, SE 49032-490, Brazil.
出版信息
J Ind Microbiol Biotechnol. 2012 Feb;39(2):289-98. doi: 10.1007/s10295-011-1027-3. Epub 2011 Aug 26.
The overall objective of this study is to evaluate the morphological [scanning electron microscopy (SEM)], physicochemical [differential scanning calorimetry (DSC), thermogravimetric analysis (TGA), chemical composition analysis, Fourier-transform infrared spectroscopy (FTIR), nuclear magnetic resonance (NMR)], and biochemical properties of Candida rugosa lipase (CRL) immobilized on a natural biopolymer poly(3-hydroxybutyrate-co-hydroxyvalerate) (PHBV) in aqueous solution. CRL was immobilized by physical adsorption with efficiency of 30%. Compared with free CRL enzyme, there were slight changes in immobilized CRL activity as a function of temperature (from 37°C to 45°C), but a similar optimal pH value of 7.0. Inactivation rate constants for immobilized CRL enzyme were 0.009 and 0.334 h⁻¹, and half-lives were 77 and 2 h at 40°C and 60°C, respectively. Kinetic parameters obtained for immobilized CRL include the Michaelis-Menten constant of K(m) = 213.18 mM and maximum reaction velocity of V(max) = 318.62 U/g. The operational stability of immobilized CRL was tested repeatedly, and after 12 cycles of reuse, the enzyme retained 50% activity. Based on our results, we propose that PHBV-immobilized CRL could serve as a promising biocatalyst in several industrial applications.
本研究的总体目标是评估固定在天然生物聚合物聚（3-羟基丁酸酯-co-羟基戊酸酯）（PHBV）上的 Candida rugosa 脂肪酶（CRL）在水溶液中的形态学（扫描电子显微镜（SEM））、物理化学（差示扫描量热法（DSC）、热重分析（TGA）、化学成分分析、傅里叶变换红外光谱（FTIR）、核磁共振（NMR））和生化特性。CRL 通过物理吸附固定化，效率为 30%。与游离的 CRL 酶相比，固定化 CRL 的活性在温度（37°C 至 45°C）略有变化，但最佳 pH 值相似，为 7.0。固定化 CRL 酶的失活动力学常数分别为 0.009 和 0.334 h⁻¹，半衰期分别为 77 和 2 h，在 40°C 和 60°C 下。固定化 CRL 的动力学参数包括米氏常数 K(m) = 213.18 mM 和最大反应速度 V(max) = 318.62 U/g。固定化 CRL 的操作稳定性经过多次测试，重复使用 12 次后，酶保留了 50%的活性。根据我们的结果，我们提出 PHBV 固定化 CRL 可以作为几种工业应用中的有前途的生物催化剂。
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