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.
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。
