title: Development of horseradish peroxidase-based cross-linked enzyme aggregates and their environmental exploitation for bioremediation purposes.
abstract: In the present study, horseradish peroxidase (HRP), in-house isolated crude cocktail enzyme, from Armoracia rusticana was cross-linked using a new type of cross-linking agent, i.e., ethylene glycol-bis [succinic acid N-hydroxysuccinimide, (EG-NHS)], which is mild in nature as compared to the glutaraldehyde (GA). The HRP-immobilized cross-linked enzyme aggregates (HRP-CLEAs) were developed using a wider range of EG-NHS and notably no adverse effect was observed. In a comparative evaluation, in the case of EG-NHS, a high-level stability in the residual activity was recorded, whereas a sharp decrease was observed in the case of glutaraldehyde. Following initial cross-linker evaluation, the HRP-CLEAs were tested to investigate their bio-catalytic efficacy for bioremediation purposes using a newly developed packed bed reactor system (PBRS). A maximal of 94.26% degradation of textile-based methyl orange dye was recorded within the shortest time frame, following 91.73% degradation of basic red 9, 84.35% degradation of indigo, 81.47% degradation of Rhodamin B, and 73.6% degradation of Rhodamine 6G, respectively, under the same working environment. Notably, the HRP-CLEAs retained almost 60% of its original activity after methyl orange dye degradation in seven consecutive cycles using PBRS. Furthermore, after HRP-CLEAs-mediated treatment in the PBRS, a significant toxicity reduction in the dye samples was recorded as compared to their pristine counterparts. In conclusion, the results suggest that the newly developed HRP-CLEAs have a great potential for industrial exploitation, to tackle numerous industrial dye-based emergent pollutants.
authors.affiliation: State Key Laboratory of Microbial Metabolism, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, 200240, China. Electronic address: bilaluaf@hotmail.com.
authors.forename: Muhammad
authors.initials: M
authors.lastname: Bilal
authors.affiliation: ENCIT - Science, Engineering and Technology School, Tecnologico de Monterrey, Ave. Eugenio Garza Sada 2501, Monterrey, N.L., CP 64849, Mexico. Electronic address: hafiz.iqbal@my.westminster.ac.uk.
authors.forename: Hafiz M N
authors.initials: HM
authors.lastname: Iqbal
authors.affiliation: State Key Laboratory of Microbial Metabolism, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, 200240, China.
authors.forename: Hongbo
authors.initials: H
authors.lastname: Hu
authors.affiliation: State Key Laboratory of Microbial Metabolism, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, 200240, China.
authors.forename: Wei
authors.initials: W
authors.lastname: Wang
authors.affiliation: State Key Laboratory of Microbial Metabolism, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, 200240, China.
authors.forename: Xuehong
authors.initials: X
authors.lastname: Zhang
mesh_terms: D001673:Biodegradation, Environmental; D004396:Coloring Agents / Q000737:chemistry*; D052918:Environmental Restoration and Remediation / Q000379:methods*; D006735:Horseradish Peroxidase / Q000737:chemistry*; D010084:Oxidation-Reduction; D014874:Water Pollutants, Chemical / Q000737:chemistry*
chemical_list: D004396:Coloring Agents; D014874:Water Pollutants, Chemical; D006735:Horseradish Peroxidase
keywords: Biodegradation; Crosslinking; Enzymatic catalysis; Green chemistry; Horseradish peroxidase