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Immobilised Enzyme Technologies for the Removal of Water Pollutants and Toxic Contaminants
Published in S Rangabhashiyam, V Ponnusami, Pardeep Singh, Biotechnological Approaches in Waste Management, 2023
Nur Izyan Wan Azelee, Nor Hasmaliana Abdul Manas, Nurrulhidayah Salamun, Mohd Akmali Mokhter, Muhammad Abd Hadi Bunyamin, Nurul Elia Aqila Abu Rahim, Siti Fatimah Zaharah Mohd Fuzi, Masngut
Considering the active development of human and veterinary medicines, and growing expanse of antibiotics, drugs and hormones, sewage disposal of these pharmaceutical wastes into the environment (rivers, lakes and soil) is a serious issue of concern. Chlortetracycline, carbamazepine, diclofenac, oestrogen and ibuprofen are examples of hormones and drugs that are identified to influence aquatic life (Yusuf, 2020). Current waste treatment method does not completely remove trace amounts of these compounds. New and more efficient methods to remove them are required. Researchers and industries have shown an escalating interest to efficiently remove these compounds, which may include the application of immobilised enzymes (Naghdi et al., 2017). Pharmaceutical active compounds in the wastewater were numerously reported to be successfully degraded by immobilised oxidoreductases (Becker et al., 2017; García-Delgado et al., 2018; Garcia et al., 2019; Lacerda et al., 2019; Naghdi et al., 2017; Simón Herrero et al., 2019; Taheran et al., 2017; Wen et al., 2019; Xu et al., 2015; Yusuf, 2020). Oxidoreductase enzymes are among the best candidates due to their capability to oxidise pollutant compounds (Yusuf, 2020). Laccase gained a great interest among other oxidoreductase enzymes, since it only needs a simple co-substrate which is oxygen (Yusuf, 2020). Therefore, laccase is suitable for wide applications as it has low specificity with the capability to use oxygen as the electron acceptor and high pollutant removal yield.
Microbial Intervention for Degradation of Agricultural Wastes
Published in Rouf Ahmad Bhat, Moonisa Aslam Dervash, Khalid Rehman Hakeem, Khalid Zaffar Masoodi, Environmental Biotechnology, 2022
Tawseef Ahmad Mir, Muatasim Jan, Mir Sajad Rabani
Laccase enzyme contains copper in its crystalline structure and associated with family oxidase. Laccase is generally present in fungi, bacteria, and a number of plants. Pycnoporous cinnabarinus species is found to produce a better quality of laccase, which can degrade lignin to a greater extent (Geng and Li, 2002). Almost every type of white-rot fungi has the capability of producing good amount lac, which can show improved functions in presence of copper. Induction of lac was shown in presence of some aromatic materials such as VA and two to five xylidine (Isroi et al., 2011). Streptomyces lavendulae and S. cinnamensis are some of the bacterial species that have the capability to lignin peroxidases, which can degrade lignin like substances (Jing, 2010). Versatile peroxidase, another type of lignin degrading enzyme, has as many activities like that of lignin peroxidases, these are confirmed in a number of Pleurotus spp. and also in Bjerkandera adusta (Ayala Aceves et al., 2001).
Other Modification Processes
Published in Dick Sandberg, Andreja Kutnar, Olov Karlsson, Dennis Jones, Wood Modification Technologies, 2021
Dick Sandberg, Andreja Kutnar, Olov Karlsson, Dennis Jones
Laccase has been shown to occur in a wide range of organisms with bacterial, insect, plant and fungal origins (Arregui et al., 2019). They are typical components of white rot fungi and the related group of litter-decomposing fungi which cause lignin degradation. The fungal sources identified include Trametes versicolor, Trametes pubsecens and Pleurotus ostreatus, each recognised for its wood degradation ability. At the time of publication, Novozymes had a commercially available laccase (marketed as Novozym™ 51003), derived from Aspergillus oryzea (a filamentous fungus used in East Asia to ferment soybeans to make soy sauce and fermented bean paste, and also to saccharify rice, other grains, and potatoes to make alcoholic beverages such as sake and shochn). Harris (2017) published a thorough overview of the isolation and uses of laccase.
Effects of potential inducers to enhance laccase production and evaluating concomitant enzyme immobilisation
Published in Environmental Technology, 2023
Gülten Yüksek, Didem Okutman Taş, Emine Ubay-Cokgor, J. Peter Jones, Mathilde Gosselin, Hubert Cabana
The instability, difficult reusability, and high cost of laccases make it challenging to implement laccase-based technologies at the industrial level. However, immobilisation – attaching laccase to a solid material – can enhance its stability and reusability, ultimately lowering its cost [2,4, 22]. Immobilisation methods like cross-linking, covalent binding, adsorption, and entrapment significantly impact the stability and activities of immobilised enzymes. Laccase can be immobilised on various solid supports, including chitosan, metal oxides, and inorganic materials like silica [2]. Researchers have been searching for new materials that meet laccase immobilisation requirements and offer simplicity and efficiency [22,30,31], such as mesoporous silica with its stable mesostructure, high surface area, pore volume, particle size, and biocompatibility [32–35]. The combined effects of laccase induction and immobilisation are essential in enhancing enzyme activity, stability, and overall performance [2,36]. By examining these methods’ collective impact, we can thoroughly comprehend their influence on laccase. Integrating these strategies optimises laccase production, extends enzyme lifespan, and improves catalytic efficiency providing promising opportunities for biotechnological and industrial applications [36].
Extremozymes used in textile industry
Published in The Journal of The Textile Institute, 2022
Priyanka Kakkar, Neeraj Wadhwa
Laccase is an oxidoreductase enzyme which has the ability to oxidize phenolic and non-phenolic compound into dimers, oligomers and polymers. It is used for the biodegradation or decolourization of synthetic dyes and their derivatives (Singh & Gupta, 2020). Thermostable laccases has been isolated from Bacillus subtilis, Aquifex aeolicus VF5(15) and Thermus thermophiles HB strain 27. Genes encoding for laccase in Thermus thermophiles HB 27 were cloned in a vector pET28a and get transformed into E.coli BL21 (DE3) and TthLAC was produced by induction with IPTG i.e. heterologous overexpression. TthLAC was purified and different assays at different environment conditions were performed. It was seen that TthLAC is thermostable, can be produced at low cost and can work under alkali conditions. Thermostable characteristic of laccase is due to its kinetic stability i.e. slow unfolding with optimal activity at 60 °C temperature and pH 6. It can be used in redox and oxidation application involving decolourization of dyes, delignification of biomass (Kumari et al., 2018).
Optimization of spore laccase production by Bacillus amyloliquefaciens isolated from wastewater and its potential in green biodecolorization of synthetic textile dyes
Published in Preparative Biochemistry & Biotechnology, 2021
Magda A. El-Bendary, Safaa M. Ezzat, Emad A. Ewais, Mohamed A. Al-Zalama
Laccases (benzenediol: oxygen oxidoreductases, EC 1.10.3.2) are important enzymes in many industries and biotechnological applications.[1] Laccase is a multicopper oxidoreductase enzyme that catalyzes the oxidation of phenolic and nonphenolic compounds while concomitantly reducing molecular oxygen to water. Laccases have many potential applications such as textile processing, detoxification of industrial effluents and pollutants, detoxification of lignocellulose hydrolysates in fuel ethanol production, delignification of pulp for paper manufacture, catalysis of grafting process in the development of novel polymers, production of fiber boards, utilization in biosensors for monitoring phenolic pollutants and drugs, elimination of undesirable phenolics and synthesis of natural products.[2]