Exploration of Pleurotus ostreatus as a biological agent in the degradation of persistent plastics like polyethylene, polystyrene, polyvinyl chloride, and polyethylene terephthalate, revealing a promising avenue toward mitigating the environmental impacts of plastic pollution. Leveraging the intrinsic enzymatic capabilities of this fungus, mainly its production of laccase, presents a sustainable and eco-friendly approach to breaking down complex polymer chains into less harmful constituents. This review focused on enhancements in the strain\'s efficiency through genetic engineering, optimized culture conditions, and enzyme immobilization to underscore the potential for scalability and practical application of this bioremediation process. The utilization of laccase from P. ostreatus in plastic waste management demonstrates a vital step forward in pursuing sustainable environmental solutions. By using the potential of fungal bioremediation, researchers can move closer to a future in which the adverse effects of plastic pollution are significantly mitigated, benefiting the health of our planet and future generations.

Immobilized laccases are widely used as green biocatalysts for bioremediation of phenolic pollutants and wastewater treatment. Metal-organic frameworks (MOFs) show potential application for immobilization of laccase. Their unique adsorption properties provide a synergic effect of adsorption and biodegradation. This review focuses on bioremediation of wastewater pollutants using laccase-MOF composites, and summarizes the current knowledge and future perspective of their biodegradation and the enhancement strategies of enzyme immobilization. Mechanistic strategies of preparation of laccase-MOF composites were mainly investigated via physical adsorption, chemical binding, and de novo/co-precipitation approaches. The influence of architecture of MOFs on the efficiency of immobilization and bioremediation were discussed. Moreover, as sustainable technology, the integration of laccases and MOFs into wastewater treatment processes represents a promising approach to address the challenges posed by industrial pollution. The MOF-laccase composites can be promising and reliable alternative to conventional techniques for the treatment of wastewaters containing pharmaceuticals, dyes, and phenolic compounds. The detailed exploration of various immobilization techniques and the influence of MOF architecture on performance provides valuable insights for optimizing these composites, paving the way for future advancements in environmental biotechnology. The findings of this research have the potential to influence industrial wastewater treatment and promoting cleaner treatment processes and contributing to sustainability efforts.

Despite their widespread applications in sectors such as pulp and paper, textile, food and beverage, pharmaceuticals, and biofuel production, laccases encounter challenges related to their activity and stability under varying reaction conditions. This review accumulates data on the complex interplay between laccase characteristics and reaction conditions for maximizing their efficacy in diverse biotechnological processes. Benefits of organic media such as improved substrate selectivity and reaction control, and their risks such as enzyme denaturation and reduced activity are reported. Additionally, the effect of reaction conditions such as pH and temperature on laccase activity and stability are gathered and reported. Sources like Bacillus pumilus, Alcaligenes faecalis, Bacillus clausii, and Bacillus tequilensis SN4 are producing laccases that are both thermo-active and alkali-active. Additionally, changes induced by the presence of various substances within reaction media such as metals, inhibitors, and organic solvents are also reported. Bacillus pumilus and Bacillus licheniformis LS04 produce the most resistant laccases in this case. Finally, the remarkable laccases have been highlighted and the proper laccase source for each industrial application is suggested.
UNASSIGNED: The online version contains supplementary material available at 10.1007/s13205-024-04015-5.

The chronic lack of effective disposal of pollutants has resulted in the detection of a wide variety of EPs in the environment, with concentrations high enough to affect ecological health. Laccase, as a versatile oxidase capable of catalyzing a wide range of substrates and without producing toxic by-products, is a potential candidate for the biodegradation of pollutants. Immobilization can provide favorable protection for free laccase, improve the stability of laccase in complex environments, and greatly enhance the reusability of laccase, which is significant in reducing the cost of industrial applications. This study introduces the properties of laccase and subsequently elaborate on the different support materials for laccase immobilization. The research advances in the degradation of EDs, PPCPs, and PAHs by immobilized laccase are then reviewed. This review provides a comprehensive understanding of laccase immobilization, as well as the advantages of various support materials, facilitating the development of more economical and efficient immobilization systems that can be put into practice to achieve the green degradation of EPs.

The contamination of wastewater with textile dyes has emerged as a pressing environmental concern due to its persistent nature and harmful effects on ecosystems. Conventional dye treatment methods have proven inadequate in effectively breaking down complex dye molecules. However, a promising alternative for textile dye degradation lies in the utilization of white rot fungi, renowned for their remarkable lignin-degrading capabilities. This review provides a comprehensive analysis of the potential of white rot fungi in degrading textile dyes, with a particular focus on their ligninolytic enzymes, specifically examining the roles of lignin peroxidase (LiP), manganese peroxidase (MnP), and laccase in the degradation of lignin and their applications in textile dye degradation. The primary objective of this paper is to elucidate the enzymatic mechanisms involved in dye degradation, with a spotlight on recent research advancements in this field. Additionally, the review explores factors influencing enzyme production, including culture conditions and genetic engineering approaches. The challenges associated with implementing white rot fungi and their ligninolytic enzymes in textile dye degradation processes are also thoroughly examined. Textile dye contamination poses a significant environmental threat due to its resistance to conventional treatment methods. White rot fungi, known for their ligninolytic capabilities, offer an innovative approach to address this issue. The review delves into the intricate mechanisms through which white rot fungi and their enzymes, including LiP, MnP, and laccase, break down complex dye molecules. These enzymes play a pivotal role in lignin degradation, a process that can be adapted for textile dye removal. The review also emphasizes recent developments in this field, shedding light on the latest findings and innovations. It discusses how culture conditions and genetic engineering techniques can influence the production of these crucial enzymes, potentially enhancing their efficiency in textile dye degradation. This highlights the potential for tailored enzyme production to address specific dye contaminants effectively. The paper also confronts the challenges associated with integrating white rot fungi and their ligninolytic enzymes into practical textile dye degradation processes. These challenges encompass issues like scalability, cost-effectiveness, and regulatory hurdles. By acknowledging these obstacles, the review aims to pave the way for practical and sustainable applications of white rot fungi in wastewater treatment. In conclusion, this comprehensive review offers valuable insights into how white rot fungi and their ligninolytic enzymes can provide a sustainable solution to the urgent problem of textile dye-contaminated wastewater. It underscores the enzymatic mechanisms at play, recent research breakthroughs, and the potential of genetic engineering to optimize enzyme production. By addressing the challenges of implementation, this review contributes to the ongoing efforts to mitigate the environmental impact of textile dye pollution. PRACTITIONER POINTS: Ligninolytic enzymes from white rot fungi, like LiP, MnP, and laccase, are crucial for degrading textile dyes. Different dyes and enzymatic mechanisms is vital for effective wastewater treatment. Combine white rot fungi-based strategies with mediator systems, co-culturing, or sequential treatment approaches to enhance overall degradation efficiency. Emphasize the broader environmental impact of textile dye pollution and position white rot fungi as a promising avenue for contributing to mitigation efforts. This aligns with the overarching goal of sustainable wastewater treatment practices and environmental conservation. Consider scalability, cost-effectiveness, and regulatory compliance to pave the way for sustainable applications that can effectively mitigate the environmental impact of textile dye pollution.

The degradation of aflatoxins using nonpathogenic microbes and their enzymes is emerging as a safe and economical alternative to chemical and physical methods for the detoxification of aflatoxins in food and feeds. Many bacteria and fungi have been identified as aflatoxin degraders. This review is focused on the chemical identification of microbial degradation products and their degradation pathways. The microbial degradations of aflatoxins are initiated by oxidation, hydroxylation, reduction, or elimination reactions mostly catalyzed by various enzymes belonging to the classes of laccase, reductases, and peroxidases. The resulting products with lesser chemical stability further undergo various reactions to form low molecular weight products. Studies on the chemical and biological nature of degraded products of aflatoxins are necessary to ensure the safety of the decontamination process. This review indicated the need for an integrated approach including decontamination studies using culture media and food matrices, proper identification and toxicity profiling of degraded products of aflatoxins, and interactions of microbes and the degradation products with food matrices for developing practical and effective microbial detoxification process.

Laccases are natural catalysts with remarkable catalytic activity. However, their application is limited by their lack of stability. Metal-organic frameworks (MOFs) have emerged as a promising alternative for enzyme immobilization. Enzymes can be immobilized in MOFs via two approaches: postsynthetic immobilization and in situ immobilization. In postsynthetic immobilization, an enzyme is embedded after MOF formation by covalent interactions or adsorption. In contrast, in in situ immobilization, a MOF is formed in the presence of an enzyme. Additionally, MOFs have exhibited intrinsic enzyme-like activity. These materials, known as nanozymes when they have the ability to replace enzymes in certain catalytic processes, have multiple key advantages, such as low cost, easy preparation, and large surface areas. This review presents a general overview of the most recent advances in both enzyme@MOF biocatalysts and MOF-based nanozymes in different applications, with a focus on laccase, which is one of the most widely investigated enzymes with excellent industrial potential.

Laccase genes produce laccase enzymes that play a crucial role in the production of lignin and oxidation reactions within plants. Lignin is a complex polymer that provides structure and toughness to the cell walls of numerous fruit plants. The LAC genes that encode laccase enzymes play vital roles in plant physiology, including the synthesis of pigments like PA that contribute to the colors of fruits, and in defending against pathogens and environmental stresses. They are crucial for fruit development, ripening, structural maintenance in plants, and adaptation to various environmental factors. As such, these genes and enzymes are essential for plant growth and development, as well as for various biotechnological applications in environmental remediation and industrial processes. This review article emphasizes the significance of genes encoding laccase enzymes during fruit growth, specifically pertaining to the strengthening of the endocarp through lignification. This process is crucial for ensuring fruit defense and optimizing seed scattering. The information gathered in this article will aid breeders in producing future fruit-bearing plants that are resistant to disease, cost-effective, and nutrient-rich.

Industrialization and other human activity represent significant environmental hazards. Toxic contaminants can harm a comprehensive platform of living organisms in their particular environments. Bioremediation is an effective remediation process in which harmful pollutants are eliminated from the environment using microorganisms or their enzymes. Microorganisms in the environment often create a variety of enzymes that can eliminate hazardous contaminants by using them as a substrate for development and growth. Through their catalytic reaction mechanism, microbial enzymes may degrade and eliminate harmful environmental pollutants and transform them into non-toxic forms. The principal types of microbial enzymes which can degrade most hazardous environmental contaminants include hydrolases, lipases, oxidoreductases, oxygenases, and laccases. Several immobilizations, genetic engineering strategies, and nanotechnology applications have been developed to improve enzyme performance and reduce pollution removal process costs. Until now, the practically applicable microbial enzymes from various microbial sources and their ability to degrade multipollutant effectively or transformation potential and mechanisms are unknown. Hence, more research and further studies are required. Additionally, there is a gap in the suitable approaches considering toxic multipollutants bioremediation using enzymatic applications. This review focused on the enzymatic elimination of harmful contaminants in the environment, such as dyes, polyaromatic hydrocarbons, plastics, heavy metals, and pesticides. Recent trends and future growth for effectively removing harmful contaminants by enzymatic degradation are also thoroughly discussed.

Laccase is a multi-copper enzyme widely expressed in fungi, higher plants, and bacteria which facilitates the direct reduction of molecular oxygen to water (without hydrogen peroxide production) accompanied by the oxidation of an electron donor. Laccase has attracted attention in biotechnological applications due to its non-specificity and use of molecular oxygen as secondary substrate. This review discusses different applications of laccase in various sectors of food, paper and pulp, waste water treatment, pharmaceuticals, sensors, and fuel cells. Despite the many advantages of laccase, challenges such as high cost due to its non-reusability, instability in harsh environmental conditions, and proteolysis are often encountered in its application. One of the approaches used to minimize these challenges is immobilization. The various methods used to immobilize laccase and the different supports used are further extensively discussed in this review.