Abstract
Since from the recent past, the attention of industrial wastes has grabbed the focus of the researchers toward designing and development of certain methods or processes in order to lessen the usage and the production of pollutants. With the knowledge of green chemistry, the catalysis using enzymes is the potential method for the production of industrial polymers at a high level without using hazardous reagents and thus curbing the pollution. Enzyme cofactors play a significant role in bio-catalysis since enzymes need them in order to catalyze significantly important reactions in organic synthesis. With the introduction and implementation of stringent processes to discharge waste into the environment, there is a need of the hour to develop alternative methods or processes to treat wastes. There exist large numbers of reported enzymes, which are mentioned in this chapter, from numerous microbes which are playing a major role in treating industrial wastes. Enzymes being specific in nature act and remove pollutants of recalcitrant nature via a certain process like precipitation and then transforming to some other products with certain changes in their characteristics. This results in increasing the susceptibility toward treatment in order to transform the waste into a value-added product. There are numerous unique applications of the catalytic activities, highlighted in the chapter for the proper understanding of the enzymes with the significance of their functions. Nowadays, it has become extensively important to use enzymes rather than hazardous chemicals so as to touch the demands of healthy, clean, and green technologies to protect our earth. This chapter highlights the importance of bio-catalytic reactions to treat various industrial wastes like the tobacco industry, pharmaceutical industry, textile industry, and dye industry with minimum invasiveness.
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Abbreviations
- AOPs:
-
Advanced oxidation processes
- CLEA:
-
Cross-linked enzyme aggregates
- CaLB:
-
Candida antarctica lipase B
- COD:
-
Chemical oxygen demand
- DMF:
-
Dimethylformamide
- DEP:
-
Deep eutectic solvents
- DCW:
-
Dry cell weight
- FAE:
-
Fatty acid esters
- FT-IR:
-
Fourier transform infrared spectroscopy
- HiC:
-
Humicola insolens cutinase
- HSP:
-
6-Hydroxy-3-succinoyl-pyridine
- HPLC:
-
High-pressure liquid chromatography
- ISM:
-
Iterative saturation mutagenesis
- IPR:
-
Intellectual property rights
- PCR:
-
Polymerase chain reaction
- MDH:
-
Mannitol 1-dehydrogenase
- MNCs:
-
Multinational companies
- NAD:
-
Nicotinamide adenine dinucleotide
- PET:
-
Poly(ethylene terephthalate)
- scCO2:
-
Supercritical carbon dioxide
- SF:
-
Submerged fermentation
- SEN:
-
Single enzyme nanoparticle
- SO3H:
-
Sulfonic acid
- SP:
-
3-Succinoyl-pyridine
- TAGs:
-
Triacylglycerols
- WRF:
-
White rot fungi
References
Abbott AP, Harris RC, Ryder KS, D’Agostino C, Gladden LF, Mantle MD. Glycerol eutectics as sustainable solvent systems. Green Chem. 2011;13:82–90. https://doi.org/10.1039/C0GC00395F.
Adrio JL, Demain AL. Microbial cells and enzymes – a century of progress. In: Barredo JL, editor. Methods in biotechnology. Microbial enzymes and biotransformations, vol. 17. Totowa: Humana Press; 2005. p. 1–27.
Adrio JL, Demain AL. Microbial enzymes: tools for biotechnological processes. Biomolecules. 2014;4:117–39. https://doi.org/10.3390/biom4010117.
Ahmad R, Sardar M. Enzyme immobilization: an overview on nanoparticles as immobilization matrix. Biochem Anal Biochem. 2015;4:178. https://doi.org/10.4172/2161-1009.1000178.
Aitken MD. Waste treatment applications of enzymes: opportunities and obstacles. Chem Eng J. 1993;52:49–58. https://doi.org/10.1016/0300-9467(93)80057-U.
Alonso D, Baeza A, Chinchilla R, Guillena G, Pastor IM, Ramon DJ. Deep eutectic solvents: the organic reaction medium of the century. Eur J Org Chem. 2016:612–32. https://doi.org/10.1002/ejoc.201501197.
Anastas P, Eghbali N. Green chemistry: principles and practice. Chem Soc Rev. 2010;39:301–12. https://doi.org/10.1039/b918763b.
Arca-Ramos A, Ammann EM, Gasser CA, Nastold P, Eibes G, Feijoo G, Lema JM, Moreira MT, Corvini PFX. Assessing the use of nanoimmobilized laccases to remove micropollutants from wastewater. Environ Sci Pollut Res. 2016;23:3217–28. https://doi.org/10.1007/s11356-015-5564-6.
Arora DS, Sharma RK. Ligninolytic fungal laccases and their biotechnological applications. Appl Biochem Biotechnol. 2010;160:1760–88.
Arslan S, Eyvaz M, Gürbulak E, Yüksel E. A review of state-of-the-art technologies in dye-containing wastewater treatment-The textile industry case. Textile Wastewater Treatment; Emriye Akcakoca Kumbasar, InTech; 2016. Available online: http://www.intechopen.com/books/textile-wastewater-treatment/a-reviewof-state-of-the-art-technologies-in-dye-containing-wastewater-treatment-the-textile-industr. Accessed 10 Nov 2016.
Asano Y, Dadashipour M, Yamazaki M, Doi N, Komeda H. Functional expression of a plant hydroxynitrile lyase in Escherichia coli by directed evolution: creation and characterization of highly in vivo soluble mutants. Protein Eng Des Sel. 2011;24:607–16. https://doi.org/10.1093/protein/gzr030.
Asgher M, Bhatti HN, Ashraf M, Legge RL. Recent developments in biodegradation of industrial pollutants by white rot fungi and their enzyme system. Biodegradation. 2008;19:771–83. https://doi.org/10.1007/s10532-008-9185-3.
Asgher M, Noreen S, Bilal M. Enhancing catalytic functionality of Trametes versicolor IBL-04 laccase by immobilization on chitosan microspheres. Chem Eng Res Des. 2017;119:1–11. https://doi.org/10.1016/j.cherd.2016.12.011.
Asif MB, Hai FI, Singh L, Price WE, Nghiem LD. Degradation of pharmaceuticals and personal care products by white-rot fungi – a critical review. Curr Pollut Rep. 2017:1–16.
Ballardo C, Abraham J, Barrena R, Artola A, Gea T, Sanchez A. Valorization of soy waste through SSF for the production of compost enriched with Bacillus thuringiensis with biopesticide properties. J Environ Manag. 2016;169:126–31. https://doi.org/10.1016/j.jenvman.2015.12.029.
Balzarini J, Stevens M, De Clercq E, Schols D, Pannecouque C. Pyridine N-oxide derivatives: unusual anti-HIV compounds with multiple mechanisms of antiviral action. J Antimicrob Chemother. 2005;55:135–8. https://doi.org/10.1093/jac/dkh530.
Bartsch S, Kourist R, Bornscheuer UT. Complete inversion of enantioselectivity towards acetylated tertiary alcohols by a double mutant of a Bacillus subtilis esterase. Angew Chem Int Ed Engl. 2008;47:1508–11. https://doi.org/10.1002/anie.200704606.
Bathen D. Physical waves in adsorption technology – an overview. Sep Purif Technol. 2003;33:163–77. https://doi.org/10.1016/S1383-5866(03)00004-2.
Bokma E, Koronakis E, Lobedanz S, Hughes C, Koronakis V. Directed evolution of a bacterial efflux pump: adaptation of the E-coli TolC exit duct to the Pseudomonas MexAB translocase. FEBS Lett. 2006;580:5339–43. https://doi.org/10.1016/j.febslet.2006.09.005.
Bozell JJ, Petersen GR. Technology development for the production of biobased products from biorefinery carbohydrates-The US Department of Energy’s “Top 10” revisited. Green Chem. 2010;12:539–54. https://doi.org/10.1039/B922014C.
Brown LD, Cologgi KF, Ulrich AC. Chapter 12: Bioremediation of oil spills on land. In: Oil spill science and technology. Boston: Elsevier; 2016. p. 699–729. Available in: https://books.google.com.br/books?hl=pt-BR&lr=&id=err2CwAAQBAJ&oi=fnd&pg=PP1&dq=Chapter+12:+Bioremediation+of+oil+spills+on+land.+&ots=raQk3UhWq9&sig=6EOjtQ8twFWYiSIPWfxArXkagHw#v=onepage&q=Chapter%2012%3A%20Bioremediation%20of%20oil%20spills%20on%20land.&f=false.
Bruzzone S, Chiappe C, Focardi SE, Pretti C, Renzi M. Theoretical descriptor for the correlation of aquatic toxicity of ionic liquids by quantitative structure−toxicity relationships. Chem Eng J. 2011;175:17–23. https://doi.org/10.1021/ci010011r.
Budisa N, Schulze-Makuch D. Supercritical carbon dioxide and its potential as a life-sustaining solvent in a planetary environment. Life. 2014;4:331–40. https://doi.org/10.3390/life4030331.
Burkhardt-Holm P. Linking water quality to human health and environment: the fate of micropollutants. Inst Water Policy Nat Univ Singap. 2011:1–62.
Carrea G, Riva S. Organic synthesis with enzymes in non-aqueous media. Weinheim: Wiley-VCH; 2008. ISBN:978-3-527-31846-9
Carrea G, Ottolina G, Riva S. Role of solvents in the control of enzyme selectivity in organic media. Trends Biotechnol. 1995;13:63–70. https://doi.org/10.1016/S0167-7799(00)88907-6.
Castro AM, de Andréa TV, Castilho LR, Freire DMG. Use of mesophilic fungal amylases produced by solid-state fermentation in the cold hydrolysis of raw babassu cake starch. Appl Biochem Biotechnol. 2010;162:1612–25. https://doi.org/10.1007/s12010-010-8942-z.
Castro AM, Andréa TV, Carvalho DF, Teixeira MMP, Castilho LR, Freire DMG. Valorization of residual agroindustrial cakes by fungal production of multienzyme complexes and their use in cold hydrolysis of raw starch. Waste Biomass Valoriz. 2011;2:291–302. https://doi.org/10.1007/s12649-011-9075-5.
Castro AM, Castilho LR, Freire DMG. Characterization of babassu, canola, castor seed and sunflower residual cakes for use as raw materials for fermentation processes. Ind Crops Prod. 2016;83:140–8. https://doi.org/10.1016/j.indcrop.2015.12.050.
Chagas PMB, Torresa JA, Silva MC, Corrêa AD. Immobilized soybean hull peroxidase for the oxidation of phenolic compounds in coffee processing wastewater. Int J Biol Macromol. 2015;81:568–75. https://doi.org/10.1016/j.ijbiomac.2015.08.061.
Chapman J, Ismail AE, Dinou CZ. Industrial of enzymes: recent advances, techniques, and outlooks. Catal. 2018;8:1–26. https://doi.org/10.3390/catal8060238.
Chatzifragkou A, Papanikolaou S, Kopsahelis N, Kachrimanidou V, Dorado MP, Koutinas AA. Biorefinery development through utilization of biodiesel industry by-products as sole fermentation feedstock for 1,3-propanediol production. Bioresour Technol. 2014;159:167–75. https://doi.org/10.1016/j.biortech.2014.02.021.
Chemical Business. Green chemical principles; 2013. Available online: http://search.ebscohost.com/login.aspx?authtype=uid&user=ns240517main&,password=main&profile=ehost&defaultdb=bth. Accessed 20 July 2014.
Chemistry & Industry. Building a greener future; 2009. Available online: http://search.ebscohost.com/login.aspx?authtype=uid&user=ns240517main&password=main&profile=ehost&defaultdb=bth. Accessed 20 July 2014.
Chen S, Engel PC. Efficient screening for new amino acid dehydrogenase activity: directed evolution of Bacillus sphaericus phenylalanine dehydrogenase towards activity with an unsaturated non-natural amino acid. J Biotechnol. 2009;142:127–34. https://doi.org/10.1016/j.jbiotec.2009.03.005.
Chhabra M, Mishra S, Sreekrishnan TR. Immobilized laccasemediated dye decolorization and transformation pathway of azo dye acid red 27. J Environ Health Sci Eng. 2015;13:1–9. https://doi.org/10.1186/s40201-015-0192-0.
Chiappe C, Marra A, Mele A. Synthesis and applications of ionic liquids derived from natural sugars. Top Curr Chem. 2010;295:177–95.
Choi YH, Van Spronsen J, Dai Y, Verberne M, Hollmann F, Arends IWCE, Witkamp GJ, Verpoorte R. Are natural deep eutectic solvents the missing link in understanding cellular metabolism and physiology? Plant Physiol. 2011;156:1701–5. https://doi.org/10.1104/pp.111.178426.
Christ TN, Deweese KA, Woodyer RD. Directed evolution toward improved production of L-ribose from ribitol. Comb Chem High Throughput Screen. 2010;13:302–8. https://doi.org/10.2174/138620710791054277.
Christian V, Shrivastava R, Shukla D, Modi H, Vyas BRM. Mediator role of veratryl alcohol in the lignin peroxidase-catalyzed oxidative decolorization of Remazol Brilliant Blue R. Enzyme Microb Technol. 2005;36:327–32. https://doi.org/10.1016/j.enzmictec.2004.09.006.
Cinelli BA, López JA, Castilho LR, Freire DMG, Castro AM. Granular starch hydrolysis of babassu agroindustrial residue: a bioprocess within the context of biorefinery. Fuel. 2014;124:41–8. https://doi.org/10.1016/j.fuel.2014.01.076.
Clark JH, Farmer TJ, Herrero-Davila L, Sherwood J. Circular economy design considerations for research and process development in the chemical sciences. Green Chem. 2016;14:3914–34. https://doi.org/10.1039/C6GC00501B.
Coleman D, Gathergood N. Biodegradation studies of ionic liquids. Chem Soc Rev. 2010;39:600–37. https://doi.org/10.1039/B817717C.
Cruz-Morato C, Ferrando-Climent L, Rodriguez-Mozaz S, Barcelo D, Marco-Urrea E, Vicent T, Sarra M. Degradation of pharmaceuticals in non-sterile urban wastewater by Trametes versicolor in a fluidized bed bioreactor. Water Res. 2013;47:5200–10. https://doi.org/10.1016/j.watres.2013.06.007.
Cruz-Morato C, Lucas D, Llorca M, Rodriguez-Mozaz S, Gorga M, Petrovic M, Barcelo D, Vicent T, Sarra M, Marco-Urrea E. Hospital wastewater treatment by fungal bioreactor: removal efficiency for pharmaceuticals and endocrine disruptor compounds. Sci Total Environ. 2014;493:365–76. https://doi.org/10.1016/j.scitotenv.2014.05.117.
Daassi D, Rodriguez-Couto S, Nasri M, Mechichi T. Biodegradation of textile dyes by immobilized laccase from Coriolopsis gallica into Ca-alginate beads. Int Biodeterior Biodegrad. 2014;90:71–8. https://doi.org/10.1016/j.ibiod.2014.02.006.
Davis RM, Wakefield M, Amos A, Gupta PC. The hitchhiker’s guide to tobacco control: a global assessment of harms, remedies, and controversies. Annu Rev Public Health. 2007;28:171–94. https://doi.org/10.1146/annurev.publhealth.28.021406.144033.
de Carvalho CC. Enzymatic and whole cell catalysis: finding new strategies for old processes. Biotechnol Adv. 2011;29:75–83. https://doi.org/10.1016/j.biotechadv.2010.09.001.
De Groeve MR, De Baere M, Hoflack L, Desmet T, Vandamme EJ, Soetaert W. Creating lactose phosphorylase enzymes by directed evolution of cellobiose phosphorylase. Protein Eng Des Sel. 2009;22:393–9. https://doi.org/10.1093/protein/gzp017.
De Groeve MR, Tran GH, Van Hoorebeke A, Stout J, Desmet T, Savvides SN, Soetaert W. Development and application of a screening assay for glycoside phosphorylases. Anal Biochem. 2010;401:162–7. https://doi.org/10.1016/j.ab.2010.02.028.
de Regil R, Sandoval G. Biocatalysis for biobased chemicals. Biomolecules. 2013;3:812–47. https://doi.org/10.3390/biom3040812.
Deetlefs M, Seddon KR. Assessing the greenness of some typical laboratory ionic liquid preparations. Green Chem. 2010;12:17–30. https://doi.org/10.1039/B915049H.
Demarche P, Junghanns C, Nair RR, Agathos SN. Harnessing the power of enzymes for environmental stewardship. Research review paper. Biotechnol Adv. 2012;30:933–53. https://doi.org/10.1016/j.biotechadv.2011.05.013.
Deska M, Konczak B. Immobilized fungal laccase as “green catalyst”for the decolourization process–state of the art. Process Biochem. 2019; https://doi.org/10.1016/j.procbio.2019.05.024.
Dhillon GS, Brar SK, Vera M, Tyagi RD. Utilization of different agro-industrial wastes for sustainable bioproduction of citric acid by Aspergillus niger. Biochem Eng J. 2011;54:83–92. https://doi.org/10.1016/j.bej.2011.02.002.
Diaz JCM, Rodríguez JA, Roussos S, Cordova J, Abousalham A, Carriere F, Baratti J. Lipase from the thermotolerant fungus Rhizopus homothallicus is more thermostable when produced using solid state fermentation than liquid fermentation procedures. Enzyme Microb Technol. 2006;39:1042–105. https://doi.org/10.1016/j.enzmictec.2006.02.005.
Dominguez de Maria P, Hollmann F. On the (Un) greenness of biocatalysis: some challenging figures and some promising options. Front Microbiol. 2015;6:01257. https://doi.org/10.3389/fmicb.2015.01257.
Du C, Lin SKC, Koutinas A, Wang R, Dorado P, Webb C. A wheat biorefining strategy based on solid-state fermentation for fermentative production of succinic acid. Bioresour Technol. 2008;99:8310–5. https://doi.org/10.1016/j.biortech.2008.03.019.
Du J, Shao Z, Zhao HM. Engineering microbial factories for synthesis of value-added products. J Ind Microbiol Biotechnol. 2011;38:873–90. https://doi.org/10.1007/s10295-011-0970-3.
Dunlop MJ, Dossani ZY, Szmidt HL, Chu HC, Lee TS, Keasling JD, Hadi MZ, Mukhopadhyay A. Engineering microbial biofuel tolerance and export using efflux pumps. Mol Syst Biol. 2011;7:487. https://doi.org/10.1038/msb.2011.21.
Duran N, Esposito E. Potential applications of oxidative enzymes and phenoloxidase-like compounds in wastewater and soil treatment: a review. Appl Catal B Environ. 2000;28:83–99. https://doi.org/10.1016/S0926-3373(00)00168-5.
Durand E, Lecomte J, Barea B, Piombo G, Dubreucq E, Villeneuve P. Evaluation of deep eutectic solvents as new media for Candida Antarctica lipase B catalyzed reactions. Process Biochem. 2012;47:2081–9. https://doi.org/10.1039/C3GC40899J.
Efremenko E, Senko O, Zubaerova D, Podorozhko E, Lozinsky V. New biocatalyst with multiple enzymatic activities for treatment of complex food wastewaters. Food Technol Biotechnol. 2008;46:208–12.
Elgue S, Prat L, Cabassud M, Cezerac J. Optimisation of solvent replacement procedures according to economic and environmental criteria. Chem Eng J. 2006;117:169–77. https://doi.org/10.1016/j.cej.2005.11.017.
Fadel HHM, Mahmoud MG, Asker MMS, Lotfy SN. Characterization and evaluation of coconut aroma produced by Trichoderma viride EMCC-107 in solid state fermentation on sugarcane bagasse. Electron J Biotechnol. 2015;18:5–9. https://doi.org/10.1016/j.ejbt.2014.10.006.
Fernandez-Arrojo L, Guazzaroni ME, Lopez-Cortes N, Beloqui A, Ferrer M. Metagenomic era for biocatalyst identification. Curr Opin Biotechnol. 2010;21:725–33. https://doi.org/10.1016/j.copbio.2010.09.006.
Fernández-Fernández M, Sanromán MÁ, Moldes D. Recent developments and applications of immobilized laccase. Biotechnol Adv. 2013;31:1808–25. https://doi.org/10.1016/j.biotechadv.2012.02.013.
Ferreira-Leitão VS, Gottschalk LMF, Ferrara MA, Nepomuceno AL, Molinari HBC, Bon EPS. Biomass residues in Brazil: availability and potential uses. Waste Biomass Valoriz. 2010;1:65–76. https://doi.org/10.1007/s12649-010-9008-8.
Ferreira-Leitão VS, Cammarota MC, Aguieiras ECG, de Sá LRV, Lafuente R, Freire DMG. The protagonism of biocatalysis in green chemistry and its environmental benefits. Catalysts. 2017;7:9. https://doi.org/10.3390/catal7010009.
Forgacs E, Cserháti T, Oros G. Removal of synthetic dyes from wastewaters: a review. Environ Int. 2004;30:953–71. https://doi.org/10.1016/j.envint.2004.02.001.
Forster-Carneiro T, Berni M, Dorileo I, Rostagno M. Biorefinery study of availability of agriculture residues and wastes for integrated biorefineries in Brazil. Resour Conserv Recycl. 2013;77:78–88. https://doi.org/10.1016/j.resconrec.2013.05.007.
Fujii Y, Kabumoto H, Nishimura K, Fujii T, Yanai S, Takeda K, Tamura N, Arisawa A, Tamura T. Purification, characterization, and directed evolution study of a vitamin D3 hydroxylase from Pseudonocardia autotrophica. Biochem Biophys Res Commun. 2009;385:170–5. https://doi.org/10.1016/j.bbrc.2009.05.033.
Fukumoto K, Yoshizawa M, Ohno H. Room temperature ionic liquids from 20 natural amino acids. J Am Chem Soc. 2005;127:2398–9. https://doi.org/10.1021/ja043451i.
Gad SS. Polyciclic aromatic amines. Encyclopedia of toxicology. 3rd ed. Cambridge, MA: Academic Press; 2014. p. 1038–9.
Gaind S, Singh S. Production, purification and characterization of neutral phytase from thermotolerant Aspergillus flavus ITCC 6720. Int Biodeterior Biodegrad. 2015;99:15–22. https://doi.org/10.1016/j.ibiod.2014.12.013.
Gao X, Xie X, Pashkov I, Sawaya MR, Laidman J, Zhang W, Cacho R, Yeates TO, Tang Y. Directed evolution and structural characterization of a simvastatin synthase. Chem Biol. 2009;16:1064–74. https://doi.org/10.1016/j.chembiol.2009.09.017.
Garcia-Ruiz E, Mate D, Ballesteros A, Martinez AT, Alcalde M. Evolving thermostability in mutant libraries of ligninolytic oxidoreductases expressed in yeast. Microb Cell Factories. 2010;9:17. https://doi.org/10.1186/1475-2859-9-17.
Goetz AE, Garg NK. Regioselective reactions of 3,4-pyridynes enabled by the aryne distortion model. Nat Chem. 2013;5:54–60.
Gorke JT, Srienc F, Kazlauskas RJ. Hydrolase-catalyzed biotransformations in deep eutectic solvents. Chem Commun. 2008:1235–7. https://doi.org/10.1039/B716317G.
Gornall AG, Bardawill CJ, David MM. Determination of serum proteins by means of biuret reaction. J Biol Chem. 1949;177:51–66. Available in: https://s3.amazonaws.com/academia.edu.documents/7522360/gornall_etal.pdf?AWSAccessKeyId=AKIAIWOWYYGZ2Y53UL3A&Expires=1504211294&Signature=G%2BsPS%2FmddQ9n7jd1FjsEHydjTMw%3D&response-content-disposition=inline%3B%20filename%3DDetermination_of_serum_proteins_by_means.pdf.
Guajardo N, Müller CR, Schrebler R, Carlesi C, Dominguez de Maria P. Deep Eutectic solvents for organocatalysis, biotransformations, and multistep organocatalyst/enzyme combinations. ChemCatChem. 2016;8:1020–7. https://doi.org/10.3390/catal8050217.
Gumba RE, Saallah S, Misson M, Ongkudon CM, Anton A. Green biodiesel production: a review on feedstock, catalyst, monolithic reactor and supercritical fluid technology. Biofuel Res J. 2016;3:431–47. https://doi.org/10.18331/BRJ2016.3.3.3.
Gupta N, Farinas ET. Directed evolution of CotA laccase for increased substrate specificity using Bacillus subtilis spores. Protein Eng Des Sel. 2010;23:679–82. https://doi.org/10.1093/protein/gzq036.
Gurusamy R, Natarajan S. Current status on biochemistry and molecular biology of microbial degradation of nicotine. Sci World J. 2013:e125385. https://doi.org/10.1155/2013/125385.
Gutarra MLE, Godoy MG, Castilho LR, Freire DMG. Ioculum strategies for Penicillium simplicissimum lipase production by solid-state fermentation using a residue from the babassu oil industry. J Chem Technol Biotechnol. 2007;82:313–8. https://doi.org/10.1002/jctb.1674.
Gutarra MLE, Godoy MG, Maugeri F, Rodrigues MI, Freire DMG, Castilho LR. Production of an acidic and thermostable lipase of the mesophilic fungus Penicillium simplicissimum by solid-state fermentation. Bioresour Technol. 2009;100:5249–54. https://doi.org/10.1016/j.biortech.2008.08.050.
Hammond OS, Bowron DT, Edler KJ. Liquid structure of the choline chloride-urea deep eutectic solvent (reline) from neutron diffraction and atomistic modelling. Green Chem. 2016;18:2736–44. https://doi.org/10.1039/C5GC02914G.
Hancock SM, Rich JR, Caines ME, Strynadka NC, Withers SG. Designer enzymes for glycosphingolipid synthesis by directed evolution. Nat Chem Biol. 2009;5:508–14. https://doi.org/10.1038/nchembio.191.
Hao Yu, Hongzhi Tang & Ping Xu. Green strategy from waste to value-added-chemical production: efficient biosynthesis of 6-hydroxy-3-succinoyl-pyridine by an engineered biocatalyst, SCIENTIFIC REPORTS. 2014;4:5397, https://doi.org/10.1038/srep05397
Hata T, Kawai S, Okamura H, Nishida T. Removal of diclofenac and mefenamic acid by the white rot fungus Phanerochaete sordida YK-624 and identification of their metabolites after fungal transformation. Biodegradation. 2010a;21:681–9. https://doi.org/10.1007/s10532-010-9334-3.
Hata T, Shintate H, Kawai S, Okamura H, Nishida T. Elimination of carbamazepine by repeated treatment with laccase in the presence of 1-hydroxybenzotriazole. J Hazard Mater. 2010b;181:1175–8. https://doi.org/10.1016/j.jhazmat.2010.05.103.
Henze M, Harremoës P, La Cour JJ, Arvin E. Wastewater treatment: biological and chemical processes. Berlin/Heidelberg: Springer; 2001. p. 36–7.
Hermann BG, Patel M. Today’s and tomorrow’s bio-based bulk chemicals from white biotechnology. Appl Biochem Biotechnol. 2007;136:361–88. https://doi.org/10.1007/s12010-007-9031-9.
Hill MD. Recent strategies for the synthesis of pyridine derivatives. Chemistry (Weinheim Bergstr Ger). 2010;16:12052–62. https://doi.org/10.1002/chem.201001100.
Hobbs HR, Kondor B, Stephenson P, Sheldon RA, Thomas NR, Poliakoff M. Continuous kinetic resolution catalysed by cross-linked enzyme aggregates, ‘CLEAs’, in supercritical CO2. Green Chem. 2006;8:816–21. https://doi.org/10.1039/B604738F.
Hocevar L, Soares VRB, Oliveira FS, Korn MGA, Teixeira LSG. Application of multivariate analysis in mid-infrared spectroscopy as a tool for the evaluation of waste frying oil blends. J Am Oil Chem Soc. 2012;89:781–6. https://doi.org/10.1007/s11746-011-1968-8.
Holkar CR, Jadhav AJ, Pinjari DV, Mahamuni NM, Pandit AB. A critical review on textile wastewater treatments: possible approaches. J Envriron Manag. 2016;182:351–66. https://doi.org/10.1016/j.jenvman.2016.07.090.
Holker U, Hofer M, Lenz J. Biotechnological advantages of laboratory-scale solid state fermentation with fungi. Appl Microbiol Biotechnol. 2004;64:175–86. https://doi.org/10.1007/s00253-003-1504-3.
Hou XD, Liu QP, Smith TJ, Li N, Zong MH. Evaluation of toxicity and biodegradability of cholinium amino acids ionic liquids. PLoS One. 2013;8:e59145. https://doi.org/10.1371/journal.pone.0059145.
Hsieh D, Marchut AJ, Wei C, Zheng B, Wang SSY, Kiang S. Model-based solvent selection during conceptual process design of a new drug manufacturing process. Org Process Res Dev. 2009;13:690–7. https://doi.org/10.1021/op900058e.
Hudlicky T, Reed JW. Applications of biotransformations and biocatalysis to complexity generation in organic synthesis. Chem Soc Rev. 2009;38:3117–32. https://doi.org/10.1039/b901172m.
Husain M, Husain Q. Applications of redox mediators in the treatment of organic pollutants by using oxidoreductive enzymes: a review. Crit Rev Environ Sci Technol. 2007;38:1–42. https://doi.org/10.1080/10643380701501213.
Imamura C, Shigemori Y. Enhancement of thermal stabilization of formaldehyde dehydrogenase from Pseudomonas putida by directed evolution. Biosci Biotechnol Biochem. 2010;74:1462–5. https://doi.org/10.1271/bbb.100026.
Imran M, Crowley DE, Khalid A, Hussain S, Mumtaz MW, Arshad M. Microbial biotechnology for decolorization of textile wastewaters. Rev Environ Sci Biotechnol. 2014;14:73–92.
Irshad M, Bahadur BA, Anwar Z, Yaqoob M, Ijaz A, Iqbal HMN. Decolorization applicability of sol-gel matrix-immobilized laccase produced from Ganoderma leucidum using agro-industrial waste. Bioresources. 2012;7:4249–61.
Jaiswal N, Pandey VP, Dwivedi UN. Immobilization of papaya laccase in chitosan led to improved multipronged stability and dye discoloration. Int J Biol Macromol. 2016;86:288–95. https://doi.org/10.1016/j.ijbiomac.2016.01.079.
Jeganathan J, Bassi A, Nakhla G. Pre-treatment of high oil and grease pet food industrial wastewaters using immobilized lipase hydrolyzation. J Hazard Mater. 2006;137:121–8. https://doi.org/10.1016/j.jhazmat.2005.11.106.
Jochens H, Aerts D, Bornscheuer UT. Thermostabilization of an esterase by alignment-guided focussed directed evolution. Protein Eng Des Sel. 2010;23:903–9. https://doi.org/10.1093/protein/gzq071.
Johannes TW, Zhao H. Directed evolution of enzymes and biosynthetic pathways. Curr Opin Microbiol. 2006;9:261–7. https://doi.org/10.1016/j.mib.2006.03.003.
Jorgensen, A., Le Bocq, A., Nazarkina, L., et al. (2008) Methodologies for social life cycle assessment. Int J LCA 13: 96–103
Kabumoto H, Miyazaki K, Arisawa A. Directed evolution of the actinomycete cytochrome P450moxA (CYP105) for enhanced activity. Biosci Biotechnol Biochem. 2009;73:1922–7. https://doi.org/10.1271/bbb.90013.
Kaiser JP, Feng YC, Bollag JM. Microbial metabolism of pyridine, quinoline, acridine, and their derivatives under aerobic and anaerobic conditions. Microbiol Rev. 1995;60:483–98.
Karam J, Nicell JA. Potential applications of enzymes in waste treatment. J Chem Technol Biotechnol. 1997;69:141–53. https://doi.org/10.1002/(SICI)1097-4660(199706)69:2<141::AID-JCTB694>3.0.CO;2-U.
Kashefi S, Borghei SM, Mahmoodi NM. Covalently immobilized laccase onto graphene oxide nanosheets: preparation, characterization, and biodegradation of azo dyes in colored wastewater. J Mol Liq. 2019;276:153–62. https://doi.org/10.1016/j.molliq.2018.11.156.
Khan AA, Husain Q. Decolorization and removal of textile and non-textile dyes from polluted wastewater and dyeing effluent by using potato (Solanum tuberosum) soluble and immobilized polyphenol oxidase. Bioresour Technol. 2007;98:1012–9. https://doi.org/10.1016/j.biortech.2006.04.008.
Khersonsky O, Rothlisberger D, Wollacott AM, Murphy P, Dym O, Albeck S, Kiss G, Houk KN, Baker D, Tawfik DS. Optimization of the in-silico-designed kemp eliminase KE70 by computational design and directed evolution. J Mol Biol. 2011;407:391–412. https://doi.org/10.1016/j.jmb.2011.01.041.
Khlifi R, Belbahri L, Woodward S, Ellouz M, Dhouib A, Sayadi S, Mechichi T. Decolourization and detoxification of textile industry wastewater by the laccase-mediator system. J Hazard Mater. 2010;175:802–8. https://doi.org/10.1016/j.jhazmat.2009.10.079.
Khmelnitsky YL, Welch SH, Clark DS, Dordick JS. Salts dramatically enhance activity of enzymes suspended in organic solvents. J Am Chem Soc. 1994;116:2647–8. https://doi.org/10.1021/ja00085a066.
Kim HJ, Uhm TG, Kim SB, Kim P. Escherichia coli arabinose isomerase and Staphylococcus aureus tagatose-6-phosphate isomerase: which is a better template for directed evolution of nonnatural substrate isomerization? J Microbiol Biotechnol. 2010;20:1018–21.
Kittl R, Withers SG. New approaches to enzymatic glycoside synthesis through directed evolution. Carbohydr Res. 2010;345:1272–9. https://doi.org/10.1016/j.carres.2010.04.002.
Klibanov AM. Asymmetric transformations catalyzed by enzymes in organic solvents. Acc Chem Res. 1990;23:114–20. https://doi.org/10.1021/ar00172a004.
Klibanov AM. Why are enzymes less active in organic solvents than in water. Trends Biotechnol. 1997;15:97–101. https://doi.org/10.1016/S0167-7799(97)01013-5.
Koch DJ, Chen MM, van Beilen JB, Arnold FH. In vivo evolution of butane oxidation by terminal alkane hydroxylases AlkB and CYP153A6. Appl Environ Microbiol. 2009;75:337–44. https://doi.org/10.1128/AEM.01758-08.
Kosjek T, Andersen HR, Kompare B, Ledin A, Heath E. Fate of carbamazepine during water treatment. Environ. Sci. Technol. 2009;43:6256e6261.
Kourist R, Bornscheuer UT. Biocatalytic synthesis of optically active tertiary alcohols. Appl Biochem Biotechnol. 2011;91:505–17. https://doi.org/10.1007/s00253-011-3418-9.
Kumar A, Singh S. Directed evolution: tailoring biocatalysis for industrial application. Crit Rev Biotechnol. 2013;33:365–78. https://doi.org/10.3109/07388551.2012.716810.
Kumar S, Mathur A, Singh V, Nandy S, Kumar K, Negi S. Bioremediation of waste cooking oil using a novel lipase produced by Penicillium chrysogenum SNP5 grown in solid medium containing waste grease. Bioresour Technol. 2012;120:300–4. https://doi.org/10.1016/j.biortech.2012.06.018.
Kurnik K, Treder K, Skorupa-Kłaput M, Tretyn A, Tyburski J. Removal of phenol from synthetic and industrial wastewater by potato pulp peroxidases. Water Air Soil Pollut. 2015;226:254–71. https://doi.org/10.1007/s11270-015-2517-0.
Lagesson A, Fahlman J, Brodin T, Fick J, Jonsson M, Bystrom P, Klaminder J. Bioaccumulation of five pharmaceuticals at multiple trophic levels in an aquatic food web – insights from a field experiment. Sci Total Environ. 2016;568:208–15. https://doi.org/10.1016/j.scitotenv.2016.05.206.
Le TT, Murugesan K, Lee CS, Vu CH, Chang YS, Jeon JR. Degradation of synthetic pollutants in real wastewater using laccase encapsulated in core-shell magnetic copper alginate beads. Bioresour Technol. 2016;216:203–10. https://doi.org/10.1016/j.biortech.2016.05.077.
Li N, Ma D, Zong MH. Enhancing the activity and regioselectivity of lipases for 3′-benzoylation of floxuridine and its analogs by using ionic liquid-containing systems. J Biotechnol. 2008;133:103–9. https://doi.org/10.1016/j.jbiotec.2007.09.003.
Li Y, Peng X, Chen H. Comparative characterization of proteins secreted by Neurospora sitophila in solid-state and submerged fermentation. J Biosci Bioeng. 2010;116:493–8. https://doi.org/10.1016/j.jbiosc.2013.04.001.
Lienert J, Güdel K, Escher BI. Screening method for ecotoxicological hazard assessment of 42 pharmaceuticals considering human metabolism and excretory routes. Environ Sci Technol. 2007;41:4471–8. https://doi.org/10.1021/es0627693.
Lima-Ramos J, Tufvesson P, Woodley JM. Application of environmental and techno-economic metrics to biocatalytic process development. Green Process Synth. 2014;3:195–213. https://doi.org/10.1515/gps-2013-0094.
Littlechild JA. Archaeal enzymes and applications in industrial biocatalysts. Archaea. 2015. 10 pages. https://doi.org/10.1155/2015/147671
Liu QB, Janssen MHA, van Rantwijk F, Sheldon RA. Room-temperature ionic liquids that dissolve carbohydrates in high concentrations. Green Chem. 2005;7:39–42. https://doi.org/10.1039/B412848F.
Liu L, Schmid RD, Urlacher VB. Engineering cytochrome P450 monooxygenase CYP 116B3 for high dealkylation activity. Biotechnol. Lett. 2010a; 32(6):841–845.
Liu YH, Ye M, Lu Y, Zhang X, Li G. Improving the decolorization for textile dyes of a metagenome-derived alkaline laccase by directed evolution. Appl Biochem Biotechnol. 2011;91:667–75. https://doi.org/10.1007/s00253-011-3292-5.
Liu C, Luo J, Xu L, Huo Z. Synthesis of 2-substituted pyridines from pyridine N-oxides. Arkivoc. 2013;1:154–74. https://doi.org/10.3998/ark.5550190.0014.105.
López E, Deive FJ, Longo M, Sanromán A. Strategies for utilisation of food- processing wastes to produce lipases in solid-state cultures of Rhizopus oryzae. Bioprocess Biosyst Eng. 2010;33:929–35. https://doi.org/10.1007/s00449-010-0416-8.
López JA, Lázaro CC, Castilho LR, Freire DMG, Castro AM. Characterization of multienzyme solutions produced by solid-state fermentation of babassu cake, for use in cold hydrolysis of raw biomass. Biochem Eng J. 2013;77:231–9. https://doi.org/10.1016/j.bej.2013.06.006.
Ma Y, Wei Y, Qiu J, Wen R, Hong J, Liu W. Isolation, transposon mutagenesis, and characterization of the novel nicotine-degrading strain Shinella sp. HZN7. Appl Microbiol Biotechnol. 2014;98:2625–36. https://doi.org/10.1007/s00253-013-5207-0.
Macedo GA, Pastore GM, Park YK. Partial purification and characterization of an extracellular lipase from a newly isolated strain of Geotrichum sp. Rev Bras Microbiol. 1997;28:90. Available in: http://repositorio.unicamp.br/handle/REPOSIP/59086
MacPherson IS, Rosell FI, Scofield M, Mauk AG, Murphy ME. Directed evolution of copper nitrite reductase to a chromogenic reductant. Protein Eng Des Sel. 2010;23:137–45. https://doi.org/10.1093/protein/gzp084.
Madeira JV Jr, Ferreira LR, Macedo J, Macedo GA. Efficient tannase production using brazilian citrus residues and potential application for orange juice valorization. Biocatal Agric Biotechnol. 2015;4:91–7. https://doi.org/10.1016/j.bcab.2014.11.005.
Mahadik ND, Puntambekar US, Bastawde KB, Khire JM, Gokhale DV. Production of acidic lipase by Aspergillus niger in solid state fermentation. Process Biochem. 2002;38:715–21. https://doi.org/10.1016/S0032-9592(02)00194-2.
Marco-Urrea E, Perez-Trujillo M, Vicent T, Caminal G. Ability of white-rot fungi to remove selected pharmaceuticals and identification of degradation products of ibuprofen by Trametes versicolor. Chemosphere. 2009;74:765–72. https://doi.org/10.1016/j.chemosphere.2008.10.040.
Market and Market, Industrial enzymes market by type, application, brands and by region-global trends and forecasts to 2020. 2018. https://www.prnewswire.com/news-releases/industrialenzymes-market-by-type-application-brands%2D%2Dby-region%2D%2D-global-trends-and-forecasts-to-2020-300240612.html/. Accessed 15 Dec 2018.
Masse L, Kennedy KJ, Chou S. Testing of alkaline enzymatic hydrolysis pretreatment for fat particles in slaughterhouse wastewater. Bioresour Technol. 2001;77:145–55. https://doi.org/10.1016/S0960-8524(00)00146-2.
Masse L, Massé DI, Kennedy KJ. Effect of hydrolysis pretreatment on fat degradation during anaerobic digestion of slaughterhouse wastewater. Process Biochem. 2003;38:1365–72. https://doi.org/10.1016/s0032-9592(03)00020-7.
Matsuda T. Recent progress in biocatalysis using supercritical carbon dioxide. J Biosci Bioeng. 2013;115:233–41. https://doi.org/10.1016/j.jbiosc.2012.10.002.
Matsuda T, Kanamaru R, Watanabe K, Kamitanaka T, Harada T, Nakamura K. Asymmetric synthesis using hydrolytic enzymes in supercritical carbon dioxide. Tetrahedron: Asymmetry. 2005;16:905–15. https://doi.org/10.1016/j.tetasy.2005.01.004.
Matto M, Husain Q. Decolorization of textile effluent by bitter gourd peroxidase immobilized on concanavalin A layered calcium alginate-starch beads. J Hazard Mater. 2009;164:1540–6. https://doi.org/10.1016/j.jhazmat.2008.09.069.
Maugeri Z, Dominguez de Maria P. Novel choline-chloride based deep-eutectic solvents with renewable hydrogen bond donors: levulinic acid and sugar-based polyols. RSC Adv. 2012;2:421–5. https://doi.org/10.1039/C1RA00630D.
Mayer B. How much nicotine kills a human? Tracing back the generally accepted lethal dose to dubious self-experiments in the nineteenth century. Arch Toxicol. 2014;88:5–7. https://doi.org/10.1007/s00204-013-1127-0.
Mazutti MA, Zabot G, Boni G, Skovronski A, de Oliveira D, di Luccio M, Rodrigues MI, Treichel H, Maugeri F. Optimization of inulinase production by solid-state fermentation in a packed bed bioreactor. J Chem Technol Biotechnol. 2010;85:109–14. https://doi.org/10.1002/jctb.2273.
McEvoy FJ, Wright WB, Birnberg GH, Albright JD. Inventors; American Cyanamid Company, assignee. ω –Heteroaroyl (propionyl or butyryl)-L-prolines. 1981; United States patent US 4:299,769.
Miele A, Giardina P, Sannia G, Faraco V. Random mutants of a Pleurotus ostreatus laccase as new biocatalysts for industrial effluents bioremediation. J Appl Microbiol. 2010;108:998–1006. https://doi.org/10.1111/j.1365-2672.2009.04505.x.
Mir-Tutusaus J, Sarra M, Caminal G. Continuous treatment of non-sterile hospital wastewater by Trametes versicolor: how to increase fungal viability by means of operational strategies and pretreatments. J Hazard Mater. 2016;318:561–70. https://doi.org/10.1016/j.jhazmat.2016.07.036.
Monhemi H, Housaindokht MR, Moosavi-Movahedi AA, Bozorgmehr MR. How a protein can remain stable in a solvent with high content of urea: insights from molecular dynamics simulation of Candida antarctica lipase B in urea: choline chloride deep eutectic solvent. Phys Chem Chem Phys. 2014;16:14882–95. https://doi.org/10.1039/c4cp00503a.
Mugdha A, Usha M. Enzymatic treatment of wastewater containing dyestuffs using different delivery systems. Sci Rev Chem Commun. 2012;2:31–40.
Murugesan A, Umarani C, Subramanian R, Nedunchezhian N. Bio-diesel as an alternative fuel for diesel engines-A review. Renew Sust Energy Rev. 2009;13:653–62. https://doi.org/10.1016/j.rser.2007.10.007.
Naghdi M, Taheran M, Brar SK, Kermanshahi-pour A, Verma M, Surampalli R. Immobilized laccase on oxygen functionalized nanobiochars through mineral acids treatment for removal of carbamazepine. Sci Total Environ. 2017;15:584–5. https://doi.org/10.1016/j.scitotenv.2017.01.021.
Naghdi M, Taheran M, Brar SK, Kermanshahi-pour A, Verma M, Surampalli RY. Removal of pharmaceutical compounds in water and wastewater using fungal oxidoreductase enzymes. Environ Poll. 2018;234:190–213.
Nazaret S, Aminov R. Role and prevalence of antibiosis and the related resistance genes in the environment. Front Microbiol. 2014;5:520e520. https://doi.org/10.3389/fmicb.2014.00520.
Neoh CH, Lam CY, Yahya A, Ware I, Ibrahim Z. Utilization of agro-industrial residues from palm oil industry for production of lignocellulolytic enzymes by Curvularia clavata. Waste Biomass Valoriz. 2015;6:385–90. https://doi.org/10.1007/s12649-015-9357-4.
Nguyen LN, Hai FI, Yang S, Kang J, Leusch FD, Roddick F, Price WE, Nghiem LD. Removal of trace organic contaminants by an MBR comprising a mixed culture of bacteria and white-rot fungi. Bioresour Technol. 2013;148:234–41. https://doi.org/10.1016/j.biortech.2013.08.142.
Nguyen LN, van de Merwe JP, Hai FI, Leusch FD, Kang J, Price WE, Roddick F, Magram SF, Nghiem LD. Laccase-syringaldehyde-mediated degradation of trace organic contaminants in an enzymatic membrane reactor: removal efficiency and effluent toxicity. Bioresour Technol. 2016;200:477–84. https://doi.org/10.1016/j.biortech.2015.10.054.
Nigam PS, Gupta N, Anthwal A. In: Nigam PS, Pandey A, editors. Pre-treatment of agro-industrial residues. In biotechnology for agro-industrial residues utilisation. Dordrecht: Springer; 2009. p. 13–33.
Novelli PK, Barros MM, Fleuri LF. Novel inexpensive fungi proteases: production by solid state fermentation and characterization. Food Chem. 2016;198:119–24. https://doi.org/10.1016/j.foodchem.2015.11.089.
Nwobi BE, Ofoegbu O, Adesina OB. Extraction and qualitative assessment of African sweet orange seed oil. Afr J Food Agric Nutr Dev. 2006;6:1–11. https://doi.org/10.4314/ajfand.v6i2.71747.
Okino-Delgado CH, Fleuri LF. Obtaining lipases from byproducts of orange juice processing. Food Chem. 2014;163:103±107. https://doi.org/10.1016/j.foodchem.2014.04.090
Okino-Delgado CH, Fleuri LF. Orange and mango by-products: agro-industrial waste as source of bioactive compounds and botanical versus commercial description – a review. Food Rev Int (Print). 2015;1:15±20. https://doi.org/10.1080/87559129.2015.1041183
Okino-Delgado CH, Fleuri LF. Obtaining concentrated extract of lipases from orange waste. Protocols IO. 2017; https://doi.org/10.17504/protocols.io.j3rcqm6.
Okino-Delgado CH, do Prado DZ, Facanali R, Marque MMO, Nascimento AS, da Costa Fernandes CJ, William Fernando Zambuzzi WF, Fleuri LF. Bioremediation of cooking oil waste using lipases from wastes. PLoS ONE. 2017;12:e0186246. https://doi.org/10.1371/journal.pone.0186246.
Okrasa K, Levy C, Wilding M, Goodall M, Baudendistel N, Hauer B, Leys D, Micklefield J. Structure-guided directed evolution of alkenyl and arylmalonate decarboxylases. Angew Chem Int Ed Engl. 2009;48:7691–4. https://doi.org/10.1002/anie.200904112.
Pandey A. Solid-state fermentation. Biochem Eng J. 2003;13:81–4. https://doi.org/10.1016/S1369-703X(02)00121-3.
Papadakis E, Tula AK, Gani R. Solvent selection methodology for ph pharmaceutical processes: solvent swap. Chem Eng Res Des. 2016;115:443–61. https://doi.org/10.1016/j.cherd.2016.09.004.
Paques FW, Macedo GA. Lipases de laÂtex vegetais: propriedades e aplicacËões industriais. QuõÂmica Nova. 2006;29: 93–99. Available in: http://www.scielo.br/pdf/%0D/qn/v29n1/27863.pdf.
Park S, Kazlauskas RJ. Improved preparation and use of room-temperature ionic liquids in lipase-catalyzed enantio- and regioselective acylations. J Org Chem. 2001;66:8395–401. https://doi.org/10.1021/jo015761e.
Park YS, Kang SW, Lee JS, Hong SI, Kim SW. Xylanase production in solid state fermentation by Aspergillus niger mutant using statistical experimental designs. Appl Microbiol Biotechnol. 2002;58:761–6. https://doi.org/10.1007/s00253-002-0965-0.
Patel RN. Biocatalysis: synthesis of key intermediates for development of pharmaceuticals. ACS Cata. 2011;1:1056–74. https://doi.org/10.1021/cs200219b.
Patil SR, Dayanand A. Optimization of process for the production of fungal pectinases from deseeded sunflower head in submerged and solid-state conditions. Bioresour Technol. 2006;97:2340–4. https://doi.org/10.1016/j.biortech.2005.10.025.
Petkovic M, Ferguson JL, Nimal Gunaratne HQ, Ferreira R, Leitão MC, Seddon KR, Rebelo LPN, Pereira CS. Novel biocompatible cholinium-based ionic liquids−toxicity and biodegradability. Green Chem. 2010;12:643–9. https://doi.org/10.1039/B922247B.
Piotrowska-Cyplik A, Olejnik A, Cyplik P, Dach J, Czarnecki Z. The kinetics of nicotine degradation, enzyme activities and genotoxic potential in the characterization of tobacco waste composting. Bioresour Technol. 2009;100:5037–44. https://doi.org/10.1016/j.biortech.2009.05.053.
Prasad S, Bocola M, Reetz MT. Revisiting the lipase from Pseudomonas aeruginosa: directed evolution of substrate acceptance and enantioselectivity using iterative saturation mutagenesis. Chemphyschem. 2011;12:1550–7. https://doi.org/10.1002/cphc.201100031.
Quartinello F, Vajnhandl S, Valh JV, Farmer TJ, Voncina B, Lobnik A, Acero EH, Pellis A, Guebitz GM. Synergistic chemo-enzymatic hydrolysis of poly (ethylene terephthalate) from textile waste. Microb Biotechnol. 2017;10:1376–83. https://doi.org/10.1111/1751-7915.12734.
Rajagopal R, Saady NMC, Torrijos M, Thanikal JV, Hung YT. Sustainable agro-food industrial wastewater treatment using high rate anaerobic process. Water. 2013;5:292–311. https://doi.org/10.3390/w5010292.
Ramachandran S, Patel AK, Nampoothiri KM, Francis F, Nagy V, Szakacs G, Pandey A. Coconut oil cake—A potential raw material for the production of -amylase. Bioresour. Technol. 2004; 93, 169–174.
Ramachandran S, Singh SK, Larroche C, Soccol CR, Pandey A. Oil cakes and their biotechnological applications-A review. Bioresour Technol. 2007;98:2000–9. https://doi.org/10.1016/j.biortech.2006.08.002.
Reetz MT, Wu S. Laboratory evolution of robust and enantio-selective Baeyer-Villiger monooxygenases for asymmetric catalysis. J Am Chem Soc. 2009;131:15424–32. https://doi.org/10.1021/ja906212k.
Reetz MT, Soni P, Fernandez L, Gumulya Y, Carballeira JD. Increasing the stability of an enzyme toward hostile organic solvents by directed evolution based on iterative saturation mutagenesis using the B-FIT method. Chem Commun (Camb). 2010;46:8657–8. https://doi.org/10.1039/c0cc02657c.
Ribitsch D, Winkler S, Gruber K, Karl W, Wehrschutz-Sigl E, Eiteljorg I, Schratl P, Remler P, Stehr R, Bessler C, Mussmann N, Sauter K, Maurer KH, Schwab H. Engineering of choline oxidase from Arthrobacter nicotianae for potential use as biological bleach in detergents. Appl Biochem Biotechnol. 2010;87:1743–52. https://doi.org/10.1007/s00253-010-2637-9.
Rodarte-Morales A, Feijoo G, Moreira M, Lema J. Operation of stirred tank reactors (STRs) and fixed-bed reactors (FBRs) with free and immobilized Phanerochaete chrysosporium for the continuous removal of pharmaceutical compounds. Biochem Eng J. 2012;66:38–45. https://doi.org/10.1016/j.bej.2012.04.011.
Roduit JP, Wellig A, Kiener A. Renewable functionalized pyridines derived from microbial metabolites of the alkaloid (S)-nicotine. Heterocycles. 1997;45:1687–702.
Ruggaber TP, Talley JW. Enhancing bioremediation with enzymatic processes: a review. Pract Period Hazard Toxic Radioact Waste Manag. 2006;10:73–85. https://doi.org/10.1061/(asce)1090-025x(2006)10:2(73).
Sathishkumar P, Kamala-Kannan S, Cho M, Kim JS, Hadibarata T, Salim MR, Oh BT. Laccase immobilization on cellulose nanofiber: the catalytic efficiency and recyclic application for simulated dye effluent treatment. J Mol Catal B Enzym. 2014;100:111–20. https://doi.org/10.1016/j.molcatb.2013.12.008.
Savile CK, Janey JM, Mundorff EC, Moore JC, Tam S, Jarvis WR, Colbeck JC, Krebber A, Fleitz FJ, Brands J, Devine PN, Huisman GW, Hughes GJ. Biocatalytic asymmetric synthesis of chiral amines from ketones applied to sitagliptin manufacture. Science. 2010;329:305–9. https://doi.org/10.1126/science.1188934.
Schmid A, Dordick JS, Hauer B, Kiener A, Wubbolts M, Witholt B. Industrial biocatalysis today and tomorrow. Nature. 2001;409:258–68. https://doi.org/10.1038/35051736.
Schmidt M, Bottcher D, Bornscheuer UT. Protein engineering of carboxyl esterases by rational design and directed evolution. Protein Pept Lett. 2009;16:1162–71. https://doi.org/10.2174/092986609789071216.
Schwarzbauer J, Heim S, Brinker S, Littke R. Occurrence and alteration of organic contaminants in seepage and leakage water from a waste deposit landfill. Water Res. 2002;36:2275–87. https://doi.org/10.1016/S0043-1354(01)00452-3.
Selwal MK, Yadav A, Selwal KK, Aggarwal NK, Gupta R, Gautam SK. Tannase production by Penicillium atramentosum KM under SSF and its applications in wine clarification and tea cream solubilization. Braz J Microbiol. 2011;42:374–87. https://doi.org/10.1590/S1517-83822011000100047.
Senthivelan T, Kanagaraj J, Panda R. Recent trends in fungal laccase for various industrial applications: an eco-friendly approach-A review. Biotechnol Bioprocess Eng. 2016;21:19–38. https://doi.org/10.1007/s12257-015-0278-7.
Sheldon RA, Woodley JM. Role of biocatalysis in sustainable chemistry. Chem Rev. 2018;118:801–38. https://doi.org/10.1021/acs.chemrev.7b00203.
Shon HK, Tian D, Kwon DY, Jin CS, Lee TJ, Chung WJ. Degradation of fat, oil, and grease (FOGs) by lipase producing bacterium Pseudomonas sp. strain D2D3. J Microb Biotechnol. 2002;12:583–91.
Sivaperumal P, Kamal K, Rajaram R. Chapter 8-Bioremediation of industrial waste through enzyme producing marine microorganisms. In: Advances in food and nutrition research, marine enzymes biotechnology: production and industrial applications, Part III-Application of marine enzymes, vol. 80; 2017. p. 165–79. https://doi.org/10.1016/bs.afnr.2016.10.006.
Slack RJ, Gronow JR, Voulvoulis N. Household hazardous waste in municipal landfills: contaminants in leachate. Sci Total Environ. 2005;337:119–37. https://doi.org/10.1016/j.scitotenv.2004.07.002.
Soares VF, Castilho LR, Bon EPS, Freire DMG. High-yield Bacillus subtilis protease production by solid-state fermentation. Appl Biochem Biotechnol. 2005;121–124:311–9.
Solís M, Solís A, Pérez HI, Manjarrez N, Flores M. Microbial decolouration of azo dyes: a review. Process Biochem. 2012;47:1723–48. https://doi.org/10.1016/j.procbio.2012.08.014.
Stacke J, Graff T, Rempel C, Dal-Bosco SM. Perfil de aÂcidos graxos no oÂleo de soja, apoÂs diferentes tempos de uso, no processo de fritura. Revista de Destaque Acadêmico. 2009;1:71–79. Available in: https://www.researchgate.net/profile/claudete_rempel/publication/263735208_perfil_de_acidos_graxos_no_oleo_de_soja_apos_diferentes_tempos_de_uso_no_processo_de_fritura/links/02e7e53bc9e7854d0e000000.pdf.
Stackelberg PE, Gibs J, Furlong ET, Meyer MT, Zaugg SD, Lippincott RL. Efficiency of conventional drinking-water-treatment processes in removal of pharmaceuticals and other organic compounds. Sci Total Environ. 2007;377:255–72. https://doi.org/10.1016/j.scitotenv.2007.01.095.
Steinrück HP, Wasserscheid P. Ionic liquids in catalysis. Catal Lett. 2015;145:380–97.
Straathof AJJ. Transformation of biomass into commodity chemicals using enzymes or cells. Chem Rev. 2014;114:1871–908. https://doi.org/10.1021/cr400309c.
Suzuki Y, Asada K, Miyazaki J, Tomita T, Kuzuyama T, Nishiyama M. Enhancement of the latent 3-isopropylmalate dehydrogenase activity of promiscuous homoisocitrate dehydrogenase by directed evolution. Biochem. J. 2010; 431:401–410.
Tadkaew N, Hai FI, McDonald JA, Khan SJ, Nghiem LD. Removal of trace organics by MBR treatment: the role of molecular properties. Water Res. 2011;45:2439–51. https://doi.org/10.1016/j.watres.2011.01.023.
Talukder MMR, Tamalampudy S, Li CJ, Le YL, Wu JC, Kondo A. An improved method of lipase preparation incorporating both solvent treatment and immobilization onto matrix. Biochem Eng. 2007;33:60–5. https://doi.org/10.1016/j.bej.2006.10.004.
Tang WL, Li Z, Zhao HM. Inverting the enantioselectivity of P450pyr monooxygenase by directed evolution. Chem Commun (Camb). 2010;46:5461–3. https://doi.org/10.1039/c0cc00735h.
Tang H, Wang L, Wang W, Yu H, Zhang K, Yao Y, Xu P. Systematic unraveling of the unsolved pathway of nicotine degradation in pseudomonas. PLoS Genet. 2013;9:e1003923. https://doi.org/10.1371/journal.pgen.1003923.
Urano N, Fukui S, Kumashiro S, Ishige T, Kita S, Sakamoto K, Kataoka M, Shimizu S. Directed evolution of an aminoalcohol dehydrogenase for efficient production of double chiral aminoalcohols. J Biosci Bioeng. 2011;111:266–71. https://doi.org/10.1016/j.jbiosc.2010.11.005.
Valladão ABG, Cammarota MC, Torres AG, Freire DMG. Profiles of fatty acids and triacylglycerols and their influence on the anaerobic biodegradability of effluents from poultry slaughterhouse. Bioresour Technol. 2011;102:7043–50. https://doi.org/10.1016/j.biortech.2011.04.037.
van Rantwijk F, Sheldon RA. Biocatalysis in ionic liquids. Chem Rev. 2007;107:2757–85. https://doi.org/10.1021/cr050946x.
Velmurugan P, Hur H, Balachandar V, Kamala-Kannan S, Lee K, Lee S, Chae JC, Shea PJ, Oh BT. Monascus pigment production by solid-state fermentation with corn cob substrate. J Biosci Bioeng. 2011;112:590–4. https://doi.org/10.1016/j.jbiosc.2011.08.009.
Villegas LGC, Mashhadi N, Chen M, Mukherjee D, Taylor KE, Biswas N. A short review of techniques for phenol removal from wastewater. Curr Pollut Rep. 2016;2:157–67.
Vishwanatha KS, Rao AGA, Singh SA. Acid protease production by solid-state fermentation using Aspergillus oryzae MTCC 5341: optimization of process parameters. J Ind Microbiol Biotechnol. 2010;37:129–38. https://doi.org/10.1007/s10295-009-0654-4.
Wandrey C, Liese A, Kihumbu D. Industrial biocatalysis: past, present, and future. Org Process Res Dev. 2000;4:286–90. https://doi.org/10.1021/op990101l.
Wang LX, Huang W. Enzymatic transglycosylation for glycoconjugate synthesis. Curr Opin Chem Biol. 2009;13:592–600. https://doi.org/10.1016/j.cbpa.2009.08.014.
Wang J, Wan W. Factors influencing fermentative hydrogen production: A review. Int J Hydrog Energy 2009;34:799–811.
Wang QY, Yang GY, Liu YL, Feng Y. Discrimination of esterase and peptidase activities of acylaminoacyl peptidase from hyperthermophilic Aeropyrum pernix K1 by a single mutation. J Biol Chem. 2006;281:18618–25. https://doi.org/10.1074/jbc.m601015200.
Wang M, Si T, Zhao H. Biocatalyst development by directed evolution. Bioresour Technol. 2012;115C:117–25. https://doi.org/10.1016/j.biortech.2012.01.054.
Wang JH, He HZ, Wang MZ, Wang S, Zhang J, Wei W, Xu HX, Lv ZM, Shen DS. Bioaugmentation of activated sludge with Acinetobacter sp. TW enhances nicotine degradation in a synthetic tobacco wastewater treatment system. Bioresour Technol. 2013;142:445–53. https://doi.org/10.1016/j.biortech.2013.05.067.
Wang W, Xu P, Tang H. Sustainable production of valuable compound 3-succinoyl-pyridine by genetically engineering Pseudomonas putida using the tobacco waste. Scientific Reports. 2015;5:16411. https://doi.org/10.1038/srep16411.
Westerhoff P, Moon H, Minakata D, Crittenden J. Oxidation of organics in retentates from reverse osmosis wastewater reuse facilities. Water Res. 2009;43:3992–8. https://doi.org/10.1016/j.watres.2009.04.010.
Woodyer RD, Christ TN, Deweese KA. Single-step bioconversion for the preparation of L-gulose and L-galactose. Carbohydr Res. 2010;345:363–8. https://doi.org/10.1016/j.carres.2009.11.023.
Wu BP, Wen Q, Xu H, Yang Z. Insights into the impact of deep eutectic solvents on horseradish peroxidase: activity, stability and structure. J Mol Catal B: Enzym. 2014;101:101–7.
Xia L, Cen P. Cellulase production by solid state fermentation on lignocellulosic waste from the xylose industry. Process Biochem. 1999;34:909–12. https://doi.org/10.1016/S0032-9592(99)00015-1.
Yu H, Tang H, Xu P. Green strategy from waste to value-added-chemical production: efficient biosynthesis of 6-hydroxy-3-succinoyl-pyridine by an engineered biocatalyst. Sci Rep. 2014;4:5397. https://doi.org/10.1038/srep05397.
Zaks A, Klibanov AM. Enzymatic catalysis in organic degrees media at 100 degrees C. Science. 1984;224:1249–51. https://doi.org/10.1126/science.6729453.
Zhang YD, Luo CR, Wang HL, Lu GF. Advances in microbial degradation of nicotine and its application. Tob Sci Technol. 2003;197:3–7.
Zhao HM. Highlights of biocatalysis and biomimetic catalysis. ACS Catal. 2011;1:1119–20. https://doi.org/10.1021/cs200425r.
Zhao HM, Giver L, Shao Z, Affholter JA, Arnold FH. Molecular evolution by staggered extension process (StEP) in vitro recombination. Nat Biotechnol. 1998;16:258–61.
Zhao H, Baker GA, Holmes S. Protease activation in glycerol-based deep eutectic solvents. J Mol Catal B: Enzym. 2011;72:163–7. https://doi.org/10.1016/j.molcatb.2011.05.015.
Zheng F, Cui BK, Wu XJ, Meng G, Liu HX, Si J. Immobilization of laccase onto chitosan beads to enhance its capability to degrade synthetic dyes. Int Biodeter Biodegr. 2016:69–78. https://doi.org/10.1016/j.ibiod.2016.03.004.
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Sharma, A., Arya, S.K. (2020). Bio-catalysis as a Green Approach for Industrial Waste Treatment. In: Inamuddin, Asiri, A. (eds) Applications of Nanotechnology for Green Synthesis. Nanotechnology in the Life Sciences. Springer, Cham. https://doi.org/10.1007/978-3-030-44176-0_14
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