（狼尾草）过氧化物酶交联聚集体的合成与表征及其在靛蓝胭脂红脱色中的应用。
Synthesis and Characterization of Cross-Linked Aggregates of Peroxidase from (Guinea Grass) and Their Application for Indigo Carmine Decolorization.
机构信息
Grupo de Investigación en Materiales Porosos con Aplicaciones Ambientales y Tecnológicas, Departamento de Química, Universidad del Tolima, Ibagué 730006299, Colombia.
Grupo de Investigación en Bioquímica y Microbiología, Escuela de Química, Universidad Industrial de Santander, Bucaramanga 680002, Colombia.
出版信息
Molecules. 2024 Jun 6;29(11):2696. doi: 10.3390/molecules29112696.
We present the synthesis of a cross-linking enzyme aggregate (CLEAS) of a peroxidase from (Guinea Grass) (GGP). The biocatalyst was produced using 50%/ ethanol and 0.88%/ glutaraldehyde for 1 h under stirring. The immobilization yield was 93.74% and the specific activity was 36.75 U mg. The biocatalyst surpassed by 61% the free enzyme activity at the optimal pH value (pH 6 for both preparations), becoming this increase in activity almost 10-fold at pH 9. GGP-CLEAS exhibited a higher thermal stability (2-4 folds) and was more stable towards hydrogen peroxide than the free enzyme (2-3 folds). GGP-CLEAS removes over 80% of 0.05 mM indigo carmine at pH 5, in the presence of 0.55 mM HO after 60 min of reaction, a much higher value than when using the free enzyme. The operational stability showed a decrease of enzyme activity (over 60% in 4 cycles), very likely related to suicide inhibition.
我们介绍了一种过氧化物酶交联酶聚集体（CLEAS）的合成，该酶来自 （Guinea Grass）（GGP）。该生物催化剂是使用 50%/乙醇和 0.88%/戊二醛在搅拌下反应 1 小时制备的。固定化产率为 93.74%，比活为 36.75 U mg。在最佳 pH 值（两种酶制剂的 pH 值均为 6）下，生物催化剂的活性超过游离酶的 61%，在 pH 值为 9 时，这种活性增加近 10 倍。GGP-CLEAS 的热稳定性更高（2-4 倍），对过氧化氢的稳定性也高于游离酶（2-3 倍）。在 pH 5 下，在 0.55 mM HO 的存在下，GGP-CLEAS 在 60 分钟的反应时间内可去除超过 80%的 0.05 mM 靛蓝胭脂红，这一去除率远高于使用游离酶时的去除率。操作稳定性显示酶活性下降（4 个循环中超过 60%），这很可能与自杀抑制有关。
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