纤维素酶和β-葡萄糖苷酶共固定在介孔二氧化硅纳米颗粒中用于水解枇杷叶提取的纤维素,Langmuir

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纤维素酶和β-葡萄糖苷酶共固定在介孔二氧化硅纳米颗粒中用于水解枇杷叶提取的纤维素
Langmuir ( IF 3.7 ) Pub Date : 2022-04-27 , DOI: 10.1021/acs.langmuir.2c00053
Giulio Pota ₁ , Antonio Sapienza Salerno ₁ , Aniello Costantini ₁ , Brigida Silvestri ₁ , Jessica Passaro ₁ , Valeria Califano ₂

Affiliation

真菌纤维素酶通常含有减少量的 β-葡萄糖苷酶 (BG)，它不允许有效的纤维素水解。为了解决这个问题，我们通过吸附在具有径向和分级开孔结构的褶皱介孔二氧化硅纳米粒子上实现了一个简单的 β-葡萄糖苷酶和纤维素酶的共固定过程，表现出较小 (WSN) 和较大 (WSN-p) 的褶皱间距. 分别在不同的载体（BG 的 WSN 和 WSN-p 的纤维素酶）上进行固定，同时在同一载体上（WSN-p），并依次在同一载体上（WSN-p）进行固定，以优化它们之间的协同作用纤维素酶和 BG。结果表明，最好的生物催化剂是将BG和纤维素酶同时固定在同一载体（WSN-p）上制备的。在这种情况下，吸附导致 20% 的固定产率，对应于 100 mg/g 载体的酶负载。获得了 82% 的反应产率和 72 μmol/min·g 的活性，评估了从提取的纤维素的水解枇杷叶。所有反应均在 50 °C 的标准温度下进行。在重复使用 9 次循环后，生物催化剂保留了 83% 的初始反应产率。此外，它在很宽的温度范围内比游离酶混合物具有更好的稳定性，在高达 90°C 的条件下保持 72% 的初始反应产率。

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Co-immobilization of Cellulase and β-Glucosidase into Mesoporous Silica Nanoparticles for the Hydrolysis of Cellulose Extracted from Eriobotrya japonica Leaves

Fungal cellulases generally contain a reduced amount of β-glucosidase (BG), which does not allow for efficient cellulose hydrolysis. To address this issue, we implemented an easy co-immobilization procedure of β-glucosidase and cellulase by adsorption on wrinkled mesoporous silica nanoparticles with radial and hierarchical open pore structures, exhibiting smaller (WSN) and larger (WSN-p) inter-wrinkle distances. The immobilization was carried out separately on different vectors (WSN for BG and WSN-p for cellulase), simultaneously on the same vector (WSN-p), and sequentially on the same vector (WSN-p) in order to optimize the synergy between cellulase and BG. The obtained results pointed out that the best biocatalyst is that prepared through simultaneous immobilization of BG and cellulase on the same vector (WSN-p). In this case, the adsorption resulted in 20% yield of immobilization, corresponding to an enzyme loading of 100 mg/g of support. 82% yield of reaction and 72 μmol/min·g activity were obtained, evaluated for the hydrolysis of cellulose extracted from Eriobotrya japonica leaves. All reactions were carried out at a standard temperature of 50 °C. The biocatalyst retained 83% of the initial yield of reaction after 9 cycles of reuse. Moreover, it had better stability than the free enzyme mixture in a wide range of temperatures, preserving 72% of the initial yield of reaction up to 90 °C.

更新日期：2022-04-27

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