Dipartimento di Scienze Chimiche, Università di Napoli Federico II, via Cynthia 4, 80126 Napoli, Italy.
Istituto di Ricerche sulla Combustione, Consiglio Nazionale delle Ricerche, Piazzale V. Tecchio 80, 80125 Napoli, Italy.
Biomed Res Int. 2014;2014:308613. doi: 10.1155/2014/308613. Epub 2014 May 8.
In the present study, a crude laccase preparation from Pleurotus ostreatus was successfully immobilized on perlite, a cheap porous silica material, and tested for Remazol Brilliant Blue R (RBBR) decolourisation in a fluidized bed recycle reactor. Results showed that RBBR decolourisation is mainly due to enzyme action despite the occurrence of dye adsorption-related enzyme inhibition. Fine tuning of immobilization conditions allowed balancing the immobilization yield and the resulting rate of decolourisation, with the adsorption capacity of the solid biocatalyst. In the continuous lab scale reactor, a maximum conversion degree of 56.1% was achieved at reactor space-time of 4.2 h. Stability and catalytic parameters of the immobilized laccases were also assessed in comparison with the soluble counterparts, revealing an increase in stability, despite a reduction of the catalytic performances. Both effects are most likely ascribable to the occurrence of multipoint attachment phenomena.
在本研究中，成功地将糙皮侧耳（Pleurotus ostreatus）粗酶制剂固定在珍珠岩上，一种廉价的多孔硅材料，并在流化床循环反应器中测试其对活性艳蓝 RBBR 的脱色作用。结果表明，尽管存在染料吸附相关的酶抑制作用，但 RBBR 的脱色主要归因于酶的作用。通过微调固定化条件，可以平衡固定化收率和由此产生的脱色速率与固体生物催化剂的吸附能力。在连续的实验室规模反应器中，在反应器时空为 4.2 h 时，达到了 56.1%的最大转化率。与可溶性酶相比，还评估了固定化漆酶的稳定性和催化参数，发现稳定性增加，尽管催化性能有所降低。这两种效应很可能归因于多点附着现象的发生。
