Sustainable pretreatment method of lignocellulosic depolymerization for enhanced ruminant productivity using laccase protein immobilized agarose beads.
Crop residues
Immobilization
Laccase
Nutrition
Ruminants
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
27 10 2024
27 10 2024
Historique:
received:
09
06
2024
accepted:
11
10
2024
medline:
28
10
2024
pubmed:
28
10
2024
entrez:
28
10
2024
Statut:
epublish
Résumé
Laccase, the selectively lignin degrader, vital to the initiation of lignocellulosic deconstruction was immobilized onto activated agarose beads to increase its reuse potential. Laccase cross-linked beads (~ 3.42 mm) recorded a specific activity of 23 Umg
Identifiants
pubmed: 39465312
doi: 10.1038/s41598-024-76278-0
pii: 10.1038/s41598-024-76278-0
doi:
Substances chimiques
Laccase
EC 1.10.3.2
Lignin
9005-53-2
lignocellulose
11132-73-3
Enzymes, Immobilized
0
Sepharose
9012-36-6
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
25617Subventions
Organisme : Indian Council of Agricultural Research
ID : F.No. 9(2)2016-ES-HRD
Informations de copyright
© 2024. The Author(s).
Références
Kwami Afedzi, A. E., Rattanaporn, K. & Parakulsuksatid, P. Impeller selection for mixing high-solids lignocellulosic biomass in stirred tank bioreactor for ethanol production. Bioresource Technol. Rep. 17. https://doi.org/10.1016/j.biteb.2021.100935 (2022).
Amidon, T. E. & S.Liu. Water-based woody biorefinery. Biotechnol. Adv. 27, 542–550 (2009).
The International Renewable Energy Agency (IRENA). Global bioenergy supply and demand projections. http://www.irena.org/ (2015)
Prasad, S. et al. Sustainable utilization of crop residues for energy generation: A life cycle assessment (LCA) perspective. Bioresour. Technol. 303 (2020).
Jönsson, L. J. & Martín, C. Pretreatment of lignocellulose: Formation of inhibitory by-products and strategies for minimizing their effects. Bioresour. Technol. 199, 103–112. https://doi.org/10.1016/j.biortech.2015.10.009 (2016).
doi: 10.1016/j.biortech.2015.10.009
pubmed: 26482946
Zanellati, A. et al. Screening and evaluation of phenols and furans degrading fungi for the biological pretreatment of lignocellulosic biomass. Int. Biodeterior. Biodegradation. 161. https://doi.org/10.1016/j.ibiod.2021.105246 (2021).
Sheldon, R. A. Enzymatic Conversion of First- and second-generation sugars. In: (ed Vaz, J.) S. Biomass and Green Chemistry. Springer, Cham. https://doi.org/10.1007/978-3-319-66736-2_7 (2018).
doi: 10.1007/978-3-319-66736-2_7
Shraddha, R., Shekher, S., Sehgal, M., Kamthania & Kumar, A. Laccase: Microbial sources, production, purification, and potential biotechnological applications. Enzyme Res. 1–11. https://doi.org/10.4061/2011/217861 (2011).
Baldrian, P. Fungal laccases - occurrence and properties. FEMS Microbiol. Rev. 30(2), 215–242. https://doi.org/10.1111/j.1574-4976.2005.00010.x (2006).
doi: 10.1016/j.biortech.2020.122964
pubmed: 16472305
Sousa, A. C., Oliveira, M. C., Martins, L. O. & Robalo, M. P. Towards the rational biosynthesis of substituted phenazines and phenoxazinones by laccases. Green Chem. 16(9). https://doi.org/10.1039/C4GC00901K (2014).
Wang, S., et al. Enzyme Stability and activity in non-aqueous reaction systems: A mini review. Catalysts. 6, 32. https://doi.org/10.3390/catal6020032 (2016).
doi: 10.3390/catal6020032
Villeret, V., et al. The crystal structure of Pyrococcus furiosus ornithine carbamoyltransferase reveals a key role for oligomerization in enzyme stability at extremely high temperatures. Proceedings National Academy Sciences USA 95(6), 2801–2806. https://doi.org/10.1073/pnas.95.6.2801 (1998)
Gao, S., Rojas-Vega, F., Rocha-Martin, J. & Guisán, J. M. Oriented immobilization of antibodies through different surface regions containing amino groups: Selective immobilization through the bottom of the fc region. Int. J. Biol. Macromol. 177, 19–28. https://doi.org/10.1016/j.ijbiomac.2021.02.103 (2021).
doi: 10.1016/j.ijbiomac.2021.02.103
pubmed: 33607135
Teufl, M. & Zajc, C. U. Traxlmayr. Engineering Strategies to Overcome the Stability-function trade-off in proteins. ACS Synth. Biol. 11(3), 1030–1039. https://doi.org/10.1021/acssynbio.1c00512 (2022). Mar 8. PMID: 35258287; PMCID: PMC8938945.
doi: 10.1021/acssynbio.1c00512
pubmed: 35258287
pmcid: 8938945
Rodrigues Rafael, C., Berenguer-Murcia, A., Carballares, D., Morellon-Sterling, R. & Fernandez-Lafuente, R. Stabilization of enzymes via immobilization: Multipoint covalent attachment and other stabilization strategies. Biotechnol. Adv. 52. https://doi.org/10.1016/j.biotechadv.2021.107821 (2021).
Wang, L. et al. Enzyme immobilization as a sustainable approach toward ecological remediation of organic-contaminated soils: Advances, issues, and future perspectives. Crit. Reviews Environ. Sci. Technol. 53(18), 1684–1708. https://doi.org/10.1080/10643389.2023.2180285 (2023).
doi: 10.1080/10643389.2023.2180285
Ramírez-Montoya, L. A., Hernandez-Montoya, V., Montes-Moran, M. A. & Cervantes, F. J. Correlation between mesopore volume of carbon supports and the immobilization of laccase from Trametes Versicolor for the decolorization of acid Orange 7. J. Environ. Manage. 162, 206–214. https://doi.org/10.1016/j.jenvman.2015.07.035 (2015).
doi: 10.1016/j.jenvman.2015.07.035
pubmed: 26241936
Latif, A., Maqbool, A., Sun, K. & Si, Y. Immobilization of trametes versicolor laccase on Cu-alginate beads for biocatalytic degradation of bisphenol A in water: Optimized immobilization, degradation, and toxicity assessment. J. Environ. Chem. Eng. 10, 1, 2213–3437. https://doi.org/10.1016/j.jece.2021.107089 (2022).
doi: 10.1016/j.jece.2021.107089
Girelli, A. M., Pambianco, E. & Scuto, F. R. Sustainable recycling of spent grain for laccase immobilization as a dye removal tool. J. Environ. Chem. Eng. 9, 6. https://doi.org/10.1016/j.jece.2021.106653 (2021).
doi: 10.1016/j.jece.2021.106653
Mogharabi, M. et al. Immobilization of laccase in alginate-gelatin mixed gel and decolorization of synthetic dyes. Bioinorg. Chem. Appl. https://doi.org/10.1155/2012/823830 (2012).
doi: 10.1155/2012/823830
pubmed: 22899898
pmcid: 3415199
Aricov, L. et al. The immobilization of laccase on mixed polymeric microspheres for methyl red decomposition. Coatings 12, 1965 (2022). https://doi.org/10.3390/coatings12121965
Shanmugam, S. et al. Optimal immobilization of Trichoderma Asperellum laccase on polymer-coated Fe3O4@SiO2 nanoparticles for enhanced biohydrogen production from delignified lignocellulosic biomass. Fuel. 273. https://doi.org/10.1016/j.fuel.2020.117777 (2020).
Ibarra, D. et al. Effect of laccase detoxification on bioethanol production from the liquid fraction of steam-pretreated olive tree pruning. Fermentation. 9, 214. https://doi.org/10.3390/fermentation9030214 (2023).
doi: 10.3390/fermentation9030214
Kieffer Curran, L. M. C. L., Mai Pham, L. T., Sale, K. L. & Simmons, B. A. Review of advances in the development of laccases for the valorization of lignin to enable the production of lignocellulosic biofuels and bioproducts. Biotechnol. Adv. 54. https://doi.org/10.1016/j.biotechadv.2021.107809 (2022).
Gujjala, L. K. S., Bandyopadhyay, T. K. & Banerjee, R. Production of biodiesel utilizing laccase pretreated lignocellulosic waste liquor: An attempt towards cleaner production process. Energy Convers. Manage. 196, 979–987. https://doi.org/10.1016/j.enconman.2019.06.036 (2019).
doi: 10.1016/j.enconman.2019.06.036
Kumar, V. P., Sridhar, M. & Rao, R. G. Biological depolymerization of lignin using laccase harvested from the autochthonous fungus Schizophyllum commune employing various production methods and its efficacy in augmenting in vitro digestibility in ruminants. Sci. Rep. 12. https://doi.org/10.1038/s41598-022-15211-9 (2022).
Zhang, K. et al. Laccase immobilized on chitosan-coated Fe3O4 nanoparticles as reusable biocatalyst for degradation of chlorophenol. J. Mol. Struct. 1220. https://doi.org/10.1016/j.molstruc.2020.128769 (2020).
Kumar, V. P., Naik, C. & Sridhar, M. Production, purification, and characterization of novel laccase produced by Schizophyllum commune NI-07 with potential for delignification of crop residues. Appl. Biochem. Microbiol. 51, 432–441. https://doi.org/10.1134/S0003683815040080 (2015).
doi: 10.1134/S0003683815040080
Deng, Z. et al. Laccase pretreatment of wheat straw: Effects of the physicochemical characteristics and the kinetics of enzymatic hydrolysis. Biotechnol. Biofuels. 12, 159. https://doi.org/10.1186/s13068-019-1499-3 (2019).
doi: 10.1186/s13068-019-1499-3
pubmed: 31249622
pmcid: 6589886
Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 242–254 (1976).
doi: 10.1016/0003-2697(76)90527-3
Origin Pro, V. Origin Lab Corporation, Northampton, MA, USA 285–292, ISSN 1002 – 0160 (2023). https://doi.org/10.1016/S1002-0160(17)60391-6
Bourbonnais, R., Leech, D. & Paice, M. G. Electrochemical analysis of the interactions of laccase mediators with lignin model compounds. Biochim. Biophys. Acta. 1379(3), 381–390 (1998).
doi: 10.1016/S0304-4165(97)00117-7
pubmed: 9545600
Phillips, C. J. C., Chiy, P. C., Arney, D. R. & Kärt, O. Effects of sodium fertilizers and supplements on milk production and mammary gland health. J. Dairy. Res. 67, 1–12 (2000).
doi: 10.1017/S0022029999003970
pubmed: 10717838
Zucca, P., Fernandez-Lafuente, R. & Sanjust, E. Agarose and its derivatives as supports for enzyme immobilization. Molecules. 21(11), 1577. https://doi.org/10.3390/molecules21111577 (2016).
doi: 10.3390/molecules21111577
pubmed: 27869778
pmcid: 6273708
Salgotra, R. K. & Chauhan, B. S. Genetic diversity, conservation, and utilization of plant genetic resources. Genes. 14, 174. https://doi.org/10.3390/genes14010174 (2023).
doi: 10.3390/genes14010174
pubmed: 36672915
pmcid: 9859222
Jolivalt, C., Brenon, S., Caminade, E., Mougin, C. & Pontie, M. Immobilization of laccase from Trametes Versicolor on a modified PVDF microfiltration membrane: Characterization of the grafted support and application in removing a phenyl-urea pesticide in wastewater. J. Membrane Sci. 180, 103–113 (2000).
doi: 10.1016/S0376-7388(00)00522-6
Singh, J. & Kumar Kapoor, R. Immobilization and reusability efficiency of Laccase onto different matrices using different approaches. Pharma Innov. J. 8(4), 373–378 (2019).
Shirley, B. A., Stanssens, P., Hahn, U. & Pace, C. N. Contribution of hydrogen bonding to the conformational stability of ribonuclease T1. Biochemistry 31(3), 725–732 (1992).
Morellon-Sterling, R. et al. Effect of amine length in the interference of the multipoint covalent immobilization of enzymes on glyoxyl agarose beads. J. Biotechnol. 329, 128–142. https://doi.org/10.1016/j.jbiotec.2021.02.005 (2021).
doi: 10.1016/j.jbiotec.2021.02.005
pubmed: 33600890
Pezzella, C., Russo, M. E., Marzocchella, A., Salatino, P. & Sannia, G. Immobilization of a Pleurotus ostreatus laccase mixture on perlite and its application to dye decolorization. Biomed. Res. Int. https://doi.org/10.1155/2014/308613 (2014).
doi: 10.1155/2014/308613
pubmed: 24895564
pmcid: 4034487
Betancor, L. et al. Guisan. Different mechanisms of protein immobilization on glutaraldehyde activated supports: Effect of support activation and immobilization conditions. Enzyme Microb. Technol. 39(4), 877–882 (2006).
doi: 10.1016/j.enzmictec.2006.01.014
Blanco, R. M. & Guisan, J. M. Stabilization of enzymes by multipoint covalent attachment to agarose-aldehyde gels. Borohydride reduction of trypsin-agarose derivatives. Enzyme Microb. Technol. 11(6), 360–366 (1989).
doi: 10.1016/0141-0229(89)90020-3
Dai, C. A., Chen, Y. F. & Liu, M. W. Thermal properties measurements of renatured gelatin using conventional and temperature-modulated differential scanning calorimetry. J. Appl. Polym. Sci. 99, 1795–1801. https://doi.org/10.1002/app.22711 (2006).
doi: 10.1002/app.22711
Bayramoglu, G., Altintas, B., Yilmaz, M. & Arica, M. Y. Immobilization of chloroperoxidase onto highly hydrophilic polyethylene chains via bio-conjugation: Catalytic properties and stabilities. Bioresour. Technol. 102(2), 475–482. https://doi.org/10.1016/j.biortech.2010.08.056 (2011).
doi: 10.1016/j.biortech.2010.08.056
pubmed: 20829037
Pedroche, J. et al. Effect of the support and experimental conditions in the intensity of the multipoint covalent attachment of proteins on glyoxylic-agarose supports-correlation between enzyme-support linkages and thermal stability. Enzyme Microb. Technol. 40, 1160–1166. https://doi.org/10.1016/j.enzmictec.2006.08.023 (2007).
doi: 10.1016/j.enzmictec.2006.08.023
Milstein, O. et al. Transformation of lignin-related compounds with laccase in organic solvents. J. Biotechnol. 30, 37–48 (1993).
doi: 10.1016/0168-1656(93)90025-I
Kashefi, S., Borghei, S. M. & Mahmoodi, N. M. Covalently immobilized laccase onto graphene oxide nanosheets: Preparation, characterization, and biodegradation of azo dyes in colored wastewater. J. Mol. Liquids. 276, 153–162 (2019).
doi: 10.1016/j.molliq.2018.11.156
Ruzicka, J., Carroll, A. D. & Lähdesmäki, I. Immobilization of proteins on agarose beads, monitored in real-time by bead injection spectroscopy. Analyst. 131(7), 799–808. https://doi.org/10.1039/b603768b (2006).
doi: 10.1039/b603768b
pubmed: 16802025
pmcid: 1585966
Boparai, H. K., Joseph, M. & O’Carroll, D. M. Kinetics and thermodynamics of cadmium ion removal by adsorption onto nano zerovalent iron particles. J. Hazard. Mater. 186(1), 458–465 (2011).
doi: 10.1016/j.jhazmat.2010.11.029
pubmed: 21130566
Gilani, S. L., Najafpour, G. D., Moghadamnia, A. & Kamaruddin, A. H. Kinetics and Isotherm studies of the immobilized lipase on Chitosan Support. Int. J. Eng. 29, 10, 1319–1331 (2016).
Simón-Herrero, C. et al. Sánchez-Silva. Immobilized laccase on polyimide aerogels for removal of carbamazepine. J. Hazard. Mater. 376, 83–90. https://doi.org/10.1016/j.jhazmat.2019.05.032 (2019).
doi: 10.1016/j.jhazmat.2019.05.032
pubmed: 31125942
Zdarta, J. et al. Robust biodegradation of naproxen and diclofenac by laccase immobilized using electrospun nanofibers with enhanced stability and reusability. Mater. Sci. Eng. C. 103. https://doi.org/10.1016/j.msec.2019.109789 (2019).
De Oliveira, S. M. et al. Immobilization and stabilization of commercial β-1,4-endoxylanase Depol™ 333MDP by multipoint covalent attachment for xylan hydrolysis: Production of prebiotics (xylo-oligosaccharides). Biocatal. Biotransform. 36(2), 141–150. https://doi.org/10.1080/10242422.2017.1308497 (2018).
doi: 10.1080/10242422.2017.1308497
Kyomuhimbo, H. D. & Brink, H. G. Applications and immobilization strategies of the copper-centered laccase enzyme: A review. Heliyon. 9. https://doi.org/10.1016/j.heliyon.2023.e13156 (2023).
Yusdy, S. R., Patel, M. G. S., Yap & Wang, D. I. C. Immobilization of l-lactate dehydrogenase on magnetic nanoclusters for chiral synthesis of pharmaceutical compounds. Biochem. Eng. J. 48(1), 13–21 (2009).
doi: 10.1016/j.bej.2009.07.017
Thiyagarajan, P., Selvam, K., Sudhakar, C. & Thangaswamy, S. Enhancement of adsorption of magenta dye by immobilized laccase on functionalized biosynthesized activated carbon nanotubes. Water Air Soil. Pollution. 231. https://doi.org/10.1007/s11270-020-04737-1 (2020).
Jafari, Y., Amiri, H. & Karimi, K. Acetone pretreatment for improvement of acetone, butanol, and ethanol production from sweet sorghum bagasse. Appl. Energy. 168, 216–225 (2016).
doi: 10.1016/j.apenergy.2016.01.090
Rafferty, K., Davies, K. M. & Heaney, R. P. Potassium intake and the calcium economy. J. Am. Coll. Nutr. 24(2), 99–106. https://doi.org/10.1080/07315724.2005.10719450 (2005).
doi: 10.1080/07315724.2005.10719450
pubmed: 15798076
McNeill, D. M., Roche, J. R. & Stockdale, C. R. McLachlan. Nutritional strategies for the prevention of hypocalcemia at calving for dairy cows in pasture-based systems. Australian J. Agric. Res. 53, 755–770 (2002).
doi: 10.1071/AR01100
Handojo, L. A. et al. Calcium Soap from Palm Fatty Acid Distillate for Ruminant Feed: The Influence of Initial Mixing Temperature. IOP Conf. Series: Materi. Sci. Eng. 543. https://doi.org/10.1088/1757-899X/543/1/012017 (2019).
Kai, D., Tan, M. J., Chee, P. L. Chua, Y. K. Yap, & X. J. Loh. Towards lignin-based functional materials in a sustainable world. Green Chem. 18(5), 1175–1200 (2016).
doi: 10.1039/C5GC02616D
Olivieri, G., Wijffels, R., Marzocchella, A., Russo, & M. E. Bioreactor and bioprocess design issues in enzymatic hydrolysis of lignocellulosic biomass. Catalysts 11, 680. https://doi.org/10.3390/catal11060680 (2021).
Spörndly, E. & Åsberg, T. Eating rate and preference of different concentrate components for cattle. J. Dairy. Sci. 89(6), 2188–2199. https://doi.org/10.3168/jds.S0022-0302(06)72289-5 (2006).
doi: 10.3168/jds.S0022-0302(06)72289-5
pubmed: 16702285
Banfi, L., Narisano, E., Riva, R., Stiasni, N. & Hiersemann, M. Sodium Borohydride. Encyclopedia of Reagents for Organic Synthesis (J. Wiley & Sons, 2004). https://doi.org/10.1002/047084289X.rs052
Toxicological Profile for Glutaraldehyde. Atlanta (GA). Agency for Toxic Substances and Disease Registry (US); 2017 Jul. 1, Public health statement for glutaraldehyde. https://www.ncbi.nlm.nih.gov/books/NBK591682/
Lopes, M. M. et al. Immobilization of phytase on zeolite modified with iron(II) for use in the animal feed and food industry sectors. Process Biochem. 100, 260–271. https://doi.org/10.1016/j.procbio.2020.10.017 (2021).
doi: 10.1016/j.procbio.2020.10.017