Electronic waste has become a global concern, as it has been steadily increasing over the years. The lack of regulation and appropriate processing facilities has rendered these wastes an environmental hazard. However, they represent excellent alternative sources of precious metals, which are highly in demand in various industries. Adsorption has been a popular method for metal removal/recovery because of several advantages, such as ease of use and low cost. In this regard, it is crucial to develop an inexpensive and functionalized adsorbent to selectively adsorb precious metals. Thus, silica, which is derived from rice husk and is abundantly present in Indonesia, was functionalized using an ionic liquid (SiRH_Im) and used for Au(III) adsorption from a simulated mobile phone leach liquor. SiRH_Im exhibited a high adsorption capacity (232.5 mg g-1). The Au(III) adsorption kinetic suitably fitted with the pseudo-second-order kinetic model. The Au(III) adsorption followed a chemisorption route that suited the monolayer model. Thomas' and Yoon-Nelson's models were well suited for the continuous Au(III) behavior. Selective recovery of Au(III) from SiRH_Im was achieved via sequential desorption. SiRH_Im also showed excellent reusability, as indicated by a negligible decrease in adsorptive performance over three cycles. The functionalization of silica derived from rice husk using an ionic liquid led to the successful creation of a solid adsorbent with a high adsorption capacity toward precious metals present in a simulated leach solution. Our results highlight the benefit of the functionalization of biomass through the immobilization of an ionic liquid toward the enhancement of its adsorption capability.
Enzymatic halogenation captures scientific interest considering its feasibility in modifying compounds for chemical diversity. Currently, majority of flavin-dependent halogenases (F-Hals) were reported from bacterial origin, and as far as we know, none from lichenized fungi. Fungi are well-known producers of halogenated compounds, so using available transcriptomic dataset of Dirinaria sp., we mined for putative gene encoding for F-Hal. Phylogenetic-based classification of the F-Hal family suggested a non-tryptophan F-Hals, similar to other fungal F-Hals, which mainly act on aromatic compounds. However, after the putative halogenase gene from Dirinaria sp., dnhal was codon-optimized, cloned, and expressed in Pichia pastoris, the ~63 kDa purified enzyme showed biocatalytic activity towards tryptophan and an aromatic compound methyl haematommate, which gave the tell-tale isotopic pattern of a chlorinated product at m/z 239.0565 and 241.0552; and m/z 243.0074 and 245.0025, respectively. This study is the start of understanding the complexities of lichenized fungal F-hals and its ability to halogenate tryptophan and other aromatic. compounds which can be used as green alternatives for biocatalysis of halogenated compounds.
Cellobiohydrolases catalyze the processive hydrolysis of cellulose into cellobiose. Here, a Trichoderma virens cDNA predicted to encode for cellobiohydrolase (cbhI) was cloned and expressed heterologously in Aspergillus niger. The cbhI gene has an open reading frame of 1518 bp, encoding for a putative protein of 505 amino acid residues with a calculated molecular mass of approximately 54 kDa. The predicted CbhI amino acid sequence has a fungal type carbohydrate binding module separated from a catalytic domain by a threonine rich linker region and showed high sequence homology with glycoside hydrolase family 7 proteins. The partially purified enzyme has an optimum pH of 4.0 with stability ranging from pH 3.0 to 6.0 and an optimum temperature of 60 °C. The partially purified CbhI has a specific activity of 4.195 Umg-1 and a low Km value of 1.88 mM when p-nitrophenyl-β-D-cellobioside (pNPC) is used as the substrate. The catalytic efficiency (kcat/Km) was 5.68 × 10-4 mM-1s-1, which is comparable to the CbhI enzymes from Trichoderma viridae and Phanaerochaete chrysosporium. CbhI also showed activity towards complex substrates such as Avicel (0.011 Umg-1), which could be useful in complex biomass degradation. Interestingly, CbhI also exhibited a relatively high inhibition constant (Ki) for cellobiose with a value of 8.65 mM, making this enzyme more resistant to end-product inhibition compared to other fungal cellobiohydrolases.