Dye effluents released from numerous dye-utilizing industries are harmful towards the environment and living things. Consequently, existence of dye effluent in environmental water bodies is becoming a growing concern to environmentalists and civilians. A long term sustainable and efficient dye effluent treatment method should be established to eliminate this issue. Dye wastewater should be treated first before release to minimize its negative impacts towards the environment and living things. However, due to lack of information on efficient dye removal methods, it is difficult to decide on a single technique that resolves the prevailing dye effluent issue. Therefore, this paper reviews existing research papers on various biological, chemical and physical dye removal methods to find its efficiency through percentage of dye removal. Although there are numerous existing tried and tested methods to accomplish dye removal, most of them have a common disadvantage which is the generation of secondary pollution to the environment. This paper highlights enzyme degradation (biological) and adsorption (physical) dye removal as these are known as one of the most efficient dye removal techniques these days. This paper also suggests the usage of a combined adsorbent as it is envisioned that this technique has better efficiency and is able to remove dyes at a faster rate.

Efficiency of various recent wastewater dye removal methods: A review

The current demands of sustainable green methodologies have increased the use of enzymatic technology in industrial processes. Employment of enzyme as biocatalysts offers the benefits of mild reaction conditions, biodegradability and catalytic efficiency. The harsh conditions of industrial processes, however, increase propensity of enzyme destabilization, shortening their industrial lifespan. Consequently, the technology of enzyme immobilization provides an effective means to circumvent these concerns by enhancing enzyme catalytic properties and also simplify downstream processing and improve operational stability. There are several techniques used to immobilize the enzymes onto supports which range from reversible physical adsorption and ionic linkages, to the irreversible stable covalent bonds. Such techniques produce immobilized enzymes of varying stability due to changes in the surface microenvironment and degree of multipoint attachment. Hence, it is mandatory to obtain information about the structure of the enzyme protein following interaction with the support surface as well as interactions of the enzymes with other proteins. Characterization technologies at the nanoscale level to study enzymes immobilized on surfaces are crucial to obtain valuable qualitative and quantitative information, including morphological visualization of the immobilized enzymes. These technologies are pertinent to assess efficacy of an immobilization technique and development of future enzyme immobilization strategies.

https://www.tandfonline.com/doi/pdf/10.1080/13102818.2015.1008192

An overview of technologies for immobilization of enzymes and surface analysis techniques for immobilized enzymes

Sol-gel based materials for biomedical applications

Enzymatic catalytic processes possess great potential in chemical manufacturing, including pharmaceuticals, fuel production and food processing. However, the engineering of enzymes is severely hampered due to their low operational stability and difficulty of reuse. Here, we develop a series of stable metal-organic frameworks with rationally designed ultra-large mesoporous cages as single-molecule traps (SMTs) for enzyme encapsulation. With a high concentration of mesoporous cages as SMTs, PCN-333(Al) encapsulates three enzymes with record-high loadings and recyclability. Immobilized enzymes that most likely undergo single-enzyme encapsulation (SEE) show smaller Km than free enzymes while maintaining comparable catalytic efficiency. Under harsh conditions, the enzyme in SEE exhibits better performance than free enzyme, showing the effectiveness of SEE in preventing enzyme aggregation or denaturation. With extraordinarily large pore size and excellent chemical stability, PCN-333 may be of interest not only for enzyme encapsulation, but also for entrapment of other nanoscaled functional moieties.

/pdf/stable-metal-organic-frameworks-containing-single-molecule-eni225t3f5.pdf

Stable metal-organic frameworks containing single-molecule traps for enzyme encapsulation

Enzymatic biodiesel: Challenges and opportunities

The current demands of the world’s biotechnological industries are enhancement in enzyme productivity and development of novel techniques for increasing their shelf life. These requirements are inevitable to facilitate large-scale and economic formulation. Enzyme immobilization provides an excellent base for increasing availability of enzyme to the substrate with greater turnover over a considerable period of time. Several natural and synthetic supports have been assessed for their efficiency for enzyme immobilization. Nowadays, immobilized enzymes are preferred over their free counterpart due to their prolonged availability that curtails redundant downstream and purification processes. Future investigations should endeavor at adopting logistic and sensible entrapment techniques along with innovatively modified supports to improve the state of enzyme immobilization and provide new perspectives to the industrial sector.

/pdf/enzyme-immobilization-an-overview-on-techniques-and-support-23u8nfucrt.pdf

Yamuna Rani Sriramulu Rajaram

Papers

Enzyme immobilization: an overview on techniques and support materials.