Preparation and Characterization of Carrageenase Immobilized onto Polyethyleneimine-Modified Pomelo Peel
2
조회
0
다운로드
0
인용
0
참고문헌
키워드
초록
In this study, carrageenase immobilization was evaluated with a concise and efficient strategy. Pomelo peel cellulose (PPC) modified by polyethyleneimine (PEI) using the physical absorption method was used as a carrier to immobilize carrageenase and achieved repeated batch catalysis. In addition, various immobilization and reaction parameters were scrutinized to enhance the immobilization efficiency. Under the optimized conditions, the enzyme activity recovery rate was more than 50% and 4.1 times higher than immobilization with non-modified pomelo peels. The optimum temperature and pH of carrageenase after immobilization by PEI-modified pomelo peel, at 60°C and 7.5 respectively, were in line with the free enzyme. The temperature resistance was reduced, inconsistent with free enzyme, and pH resistance was increased. A significant loss of activity (46.8%) was observed after reusing it thrice under optimal reaction conditions. In terms of stability, the immobilized enzyme conserved 76.0% of the initial enzyme activity after 98 days of storage. Furthermore, a modest decrease in the kinetic constant (Km) value was observed, indicating the improved substrate affinity of the immobilized enzyme. Therefore, modified pomelo peel is a verified and promising enzyme immobilization system for the synthesis of inorganic solvents.
Abstract
In this study, carrageenase immobilization was evaluated with a concise and efficient strategy. Pomelo peel cellulose (PPC) modified by polyethyleneimine (PEI) using the physical absorption method was used as a carrier to immobilize carrageenase and achieved repeated batch catalysis. In addition, various immobilization and reaction parameters were scrutinized to enhance the immobilization efficiency. Under the optimized conditions, the enzyme activity recovery rate was more than 50% and 4.1 times higher than immobilization with non-modified pomelo peels. The optimum temperature and pH of carrageenase after immobilization by PEI-modified pomelo peel, at 60°C and 7.5 respectively, were in line with the free enzyme. The temperature resistance was reduced, inconsistent with free enzyme, and pH resistance was increased. A significant loss of activity (46.8%) was observed after reusing it thrice under optimal reaction conditions. In terms of stability, the immobilized enzyme conserved 76.0% of the initial enzyme activity after 98 days of storage. Furthermore, a modest decrease in the kinetic constant (Km) value was observed, indicating the improved substrate affinity of the immobilized enzyme. Therefore, modified pomelo peel is a verified and promising enzyme immobilization system for the synthesis of inorganic solvents.
참고문헌 (42)
- Dae H Kang, "Synergistic effect of the enzyme complexes comprising agarase, carrageenase and neoagarobiose hydrolase on degradation of the red algae", Bioresour. Technol, 250, pp.666~672 (2018)
- Liao YC, "Algae-derived hydrocolloids in foods : applications and health-related issues", Bioengineered, 12, pp.3787~3801 (2021)
- Torres MD, "Integral utilization of red seaweed for bioactive production", Mar. Drugs, 17, pp.314~ (2019)
- Kalitnik AA, "Carrageenanolytic enzymes from marine bacteria associated with the red alga Tichocarpus crinitus", J. Appl. Phycol, 30, pp.2071~2081 (2018)
- Khan RS, "Recent trends using natural polymeric nanofibers as supports for enzyme immobilization and catalysis", Biotechnol. Bioeng, 120, pp.22~40 (2023)
- Zdarta J, "A general overview of support materials for enzyme immobilization : characteristics, properties, practical utility", Catalysts, 8, pp.92~119 (2018)
- Guisan JM, "Enzyme immobilization strategies for the design of robust and efficient biocatalysts", Curr. Opin. Green Sustain. Chem, 35, pp.100593~ (2022)
- Verma NK, "Comparative study of covalent and hydrophobic interactions for α-amylase immobilization on cellulose derivatives", Int. J. Biol. Macromol, 174, pp.134~143 (2021)
- Cheng H, "Multifaceted applications of cellulosic porous materials in environment, energy, and health", Progress Polym. Sci, 106, pp.101253~ (2020)
- Bayazidi P, "Immobilization of lysozyme on bacterial cellulose nanofibers : characteristics, antimicrobial activity and morphological properties", Int. J. Biol. Macromol, 107, pp.2544~2551 (2018)
- Liu Y, "Isolation and characterization of microcrystalline cellulose from pomelo peel", Int. J. Biol. Macromol, 111, pp.717~721 (2018)
- Zhu L, "An environmentally friendly carbon aerogels derived from waste pomelo peels for the removal of organic pollutants", oils, 2017, pp.241, 285~292
- Virgen-Ortiz JJ, "Polyethylenimine : a very useful ionic polymer in the design of immobilized enzyme biocatalysts", J. Mater. Chem B, 5, pp.7461~7490 (2017)
- Ghriga MA, "Review of recent advances in polyethylenimine crosslinked polymer gels used for conformance control applications", Polym. Bulletin, 76, pp.6001~6029 (2019)
- Velasco-Lozano S, "Co-immobilized phosphorylated cofactors and enzymes as self-sufficient heterogeneous biocatalysts for chemical processes", Angewandte Chemie Int. Ed, 56, pp.771~775 (2017)
- Bezerra RM, "Lemos TLG, et al. 2020. A new heterofunctional support for enzyme immobilization: PEI functionalized Fe3O4 MNPs activated with divinyl sulfone. Application in the immobilization of lipase from Thermomyces lanuginosus", Enzyme Microb. Technol, 138, pp.560~571 (2020)
- Zaak H, "Coimmobilization of enzymes in bilayers using pei as a glue to reuse the most stable enzyme : preventing pei release during inactivated enzyme desorption", Process Biochem, 61, pp.95~101 (2017)
- Lopez-Tejedor D, "Efficient purification of a highly active H-subunit of tyrosinase from Agaricus bisporus", Protein Expr. Purif, 145, pp.64~70 (2018)
- Jain A, "Basic Techniques in Biochemistry, Microbiology and Molecular", pp.181~183 (2020), Humanna Press
- Xiao L, "Utilization of pomelo peels to manufacture value-added products : a review", Food Chem, 351, pp.129247~ (2021)
- Girelli AM, "Eggshell membrane as feedstock in enzyme immobilization", J. Biotechnol, 325, pp.241~249 (2021)
- Cai Q, "Enhanced activity and stability of industrial lipases immobilized onto spherelike bacterial cellulose", Int. J. Biol. Macromol, 109, pp.1174~1181 (2018)
- Cao SL, "Preparation and characterization of immobilized lipase from Pseudomonas cepacia onto magnetic cellulose nanocrystals", Sci. Rep, 6, pp.20420~ (2016)
- Baldikova E, "Magnetically modified bacterial cellulose : a promising carrier for immobilization of affinity ligands, enzymes, and cells", Mater. Sci. Eng. C Mater. Biol. Appl, 71, pp.214~221 (2017)
- Drozd R, "The application of magnetically modified bacterial cellulose for immobilization of laccase", Int. J. Biol. Macromol, 108, pp.462~470 (2018)
- Liu DM, "Advances on methods and easy separated support materials for enzymes immobilization", TrAC Trends Anal. Chem, 102, pp.332~342 (2018)
- Marques Netto CG, "Carbon dioxide", methanol conversion cycle based on cascade enzymatic reactions supported on superparamagnetic nanoparticles, 2017, pp.90, 593~606
- Bilal M, "Multi-point enzyme immobilization, surface chemistry, and novel platforms : a paradigm shift in biocatalyst design", Crit. Rev. Biotechnol, 39, pp.202~219 (2019)
- Cui J, "Optimization protocols and improved strategies for metal-organic frameworks for immobilizing enzymes : current development and future challenges", Coord. Chem. Rev, 370, pp.22~41 (2018)
- Hoarau M, "Immobilized enzymes : understanding enzyme–surface interactions at the molecular level", Org. Biomol. Chem, 15, pp.9539~9551 (2017)
- Zheng F, "Immobilization of laccase onto chitosan beads to enhance its capability to degrade synthetic dyes", Int. Biodeterior. Biodegrad, 110, pp.69~78 (2016)
- Cao YP, "PEI-crosslinked lipase on the surface of magnetic microspheres and its characteristics", Colloids Surf B Biointerfaces, 189, pp.110874~ (2020)
- Bezerra RM, "A new heterofunctional support for enzyme immobilization : PEI functionalized Fe3O4 MNPs activated with divinyl sulfone, application in the immobilization of lipase from Thermomyces lanuginosus", Enzyme Microb. Technol, 138, pp.109560~ (2020)
- Shojaei F, "Characterization of biosynthesized chitosan nanoparticles from Penaeus vannamei for the immobilization of P. vannamei protease: an eco-friendly nanobiocatalyst", Int. J. Food Properties, 20, pp.1413~1423 (2017)
- Yuan H, "Evaluation of nanocellulose carriers produced by four different bacterial strains for laccase immobilization", Carbohydr. Polym, 196, pp.457~464 (2018)
- Mostafa FA, "Immobilization of xylanase on modified grafted alginate polyethyleneimine bead based on impact of sodium cation effect", Int. J. Biol. Macromol, 140, pp.1284~1295 (2019)
- Guo J, "Enhanced production of κ-carrageenase and κ-carrageenan oligosaccharides through immobilization of Thalassospira sp. Fjfst-332 with magnetic Fe3O4-chitosan microspheres", J. Agric. Food Chem, 65, pp.7934~7943 (2017)
- Mohammadi M, "Activated alginate-montmorillonite beads as an efficient carrier for pectinase immobilization", Int. J. Biol. Macromol, 137, pp.253~260 (2019)
- Deng Z, "Immobilization of pectinases into calcium alginate microspheres for fruit juice application", Food Hydrocolloids, 89, pp.691~699 (2019)
- Kaur P, "Characterization of magnetic nanoparticle–immobilized cellulases for enzymatic saccharification of rice straw", Biomass Convers. Biorefinery, 11, pp.955~969 (2021)
- Nimkande, VD, "Screening, identification, and characterization of lipase-producing halotolerant Bacillus altitudinis Ant19 from Antarctic soil", Arch. Microbiol, 205, pp.113~ (2023)
- Hosseini A, "Immobilization of α-amylase in ethylcellulose electrospun fibers using emulsion-electrospinning method", Carbohydr. Polym, 278, pp.118919~ (2022)