UV-H2O2 degradation of methyl orange catalysed by H3PW12O40/activated clay.

A catalyst consisting of phosphotungstic acid (H3PW12O40) combined with activated clay was prepared by the impregnation method, and an experiment was carried out to evaluate the catalytic activity of the H3PW12O40/activated clay for the degradation of methyl orange (MO) in the UV-H2O2 process. The degradation ratio of MO can be affected by H2O2 concentration, reaction time, catalyst dosage, pH and temperature. The reaction temperature should be controlled at less than 70 degrees C, and the catalyst has a wide applicable pH range in the UV-H2O2 process. Hydroxyl radicals were generated in the UV-H2O2 system under the action of H3PW12O40/activated clay, and MO was degraded by hydroxyl radicals. Compared with traditional catalysts used in UV-H2O2 systems, H3PW12O40/activated clay has certain advantages for its practical application.

Immobilization of Candida cylindracea Lipase by Covalent Attachment on Glu-Modified Bentonite.

Alkaline Ca-bentonite, obtained upon acid activation and base load of natural bentonite, has a good anion exchange capability. Glu-modified alkaline Ca-bentonites were further prepared by covalent binding with glutamic acid for the immobilization of lipase OF from Candida cylindracea. The obtained immobilized lipase demonstrated a significantly higher catalytic activity than that of unmodified alkaline Ca-bentonite, giving a specific activity of 62.1 U mg-1 protein, twice that of the unmodified carrier, and a total activity of 391.2 U g-1 support, retaining ~ 82.3% of the activity after being reused five times for olive oil emulsion hydrolysis. X-ray diffraction and Fourier transform infrared spectroscopy assays demonstrated the successful immobilization of the lipase on the surface of the bentonite. Upon immobilization, the thermostability of the lipase improved remarkably. At 50 °C, free lipase retained only 6.0% of its initial activity at 6 h, in comparison with 15% for Ca-Bent-lipase and 50% for Glu-Ca-Bent-lipase after 8 h. The Glu-Ca-Bent-lipase is proved as an effective biocatalyst for the biodiesel preparation, improving the transesterification reaction conversion from 52.8% in the condition of free lipase to 99.9% and keeping at 56.2% after being reused five times, while the free lipase was inactive upon two reuses. The above results provide a new route in the use of inexpensive bentonite for the enzyme immobilization.