REFERENCES
1. Asthana M, Syiemlieh I, Kumar A, Lal RA. Direct oxidation of alcohols catalysed by heterometallic complex [CuNi(bz)3(bpy)2] ClO4 to aldehydes and ketones mediated by hydrogen peroxide as a terminal oxidant. Inorganica Chimica Acta 2020;502:119286.
2. Shaabani A, Shaabani S, Afaridoun H. Highly selective aerobic oxidation of alkyl arenes and alcohols: cobalt supported on natural hydroxyapatite nanocrystals. RSC Adv 2016;6:48396-404.
3. Mallat T, Baiker A. Oxidation of alcohols with molecular oxygen on solid catalysts. Chem Rev 2004;104:3037-58.
4. Nakagawa K, Konaka R, Nakata T. Oxidation with Nickel Peroxide. I. oxidation of alcohols. J Org Chem 1962;27:1597-601.
5. Lou JD, Xu ZN. Selective oxidation of primary alcohols with chromium trioxide under solvent free conditions. Tetrahedron Lett 2002;43:6095-7.
7. Taylor RJ, Reid M, Foot J, Raw SA. Tandem oxidation processes using manganese dioxide: discovery, applications, and current studies. Acc Chem Res 2005;38:851-69.
8. Hasanpour B, Jafarpour M, Feizpour F, Rezaeifard A. Copper(II)-ethanolamine triazine complex on chitosan-functionalized nanomaghemite for catalytic aerobic oxidation of benzylic alcohols. Catal Lett 2021;151:45-55.
9. Martı́n SE, Suárez DF. Catalytic aerobic oxidation of alcohols by Fe(NO3)3-FeBr3. Tetrahedron Lett 2002;43:4475-9.
10. Qiu S, Li Y, Xu H, et al. Efficient catalytic oxidation of benzyl alcohol by tetrasubstituted cobalt phthalocyanine-MWCNTs composites. Solid State Sci 2022;129:106905.
11. Schultz MJ, Hamilton SS, Jensen DR, Sigman MS. Development and comparison of the substrate scope of Pd-catalysts for the aerobic oxidation of alcohols. J Org Chem 2005;70:3343-52.
12. Personick ML, Zugic B, Biener MM, Biener J, Madix RJ, Friend CM. Ozone-activated nanoporous gold: a stable and storable material for catalytic oxidation. ACS Catal 2015;5:4237-41.
13. Parmeggiani C, Cardona F. Transition metal based catalysts in the aerobic oxidation of alcohols. Green Chem 2012;14:547-64.
15. Shibuya M, Tomizawa M, Suzuki I, Iwabuchi Y. 2-azaadamantane N-oxyl (AZADO) and 1-Me-AZADO: highly efficient organocatalysts for oxidation of alcohols. J Am Chem Soc 2006;128:8412-3.
16. Punniyamurthy T, Velusamy S, Iqbal J. Recent advances in transition metal catalyzed oxidation of organic substrates with molecular oxygen. Chem Rev 2005;105:2329-63.
17. Liu J, Wu S, Li Z. Recent advances in enzymatic oxidation of alcohols. Curr Opin Chem Biol 2018;43:77-86.
18. Moa S, Himo F. Quantum chemical study of mechanism and stereoselectivity of secondary alcohol dehydrogenase. J Inorg Biochem 2017;175:259-66.
19. Kroutil W, Mang H, Edegger K, Faber K. Biocatalytic oxidation of primary and secondary alcohols. Adv Synth Catal 2004;346:125-42.
20. Tian K, Li Z. A simple biosystem for the high-yielding cascade conversion of racemic alcohols to enantiopure amines. Angew Chem Int Ed Engl 2020;59:21745-51.
21. Albarrán-velo J, Gotor-fernández V, Lavandera I. One-pot two-step chemoenzymatic deracemization of allylic alcohols using laccases and alcohol dehydrogenases. Mol Catal 2020;493:111087.
22. González-granda S, Méndez-sánchez D, Lavandera I, Gotor-fernández V. Laccase-mediated oxidations of propargylic alcohols. Application in the deracemization of 1-arylprop-2-yn-1-ols in combination with alcohol dehydrogenases. ChemCatChem 2020;12:520-7.
23. Martínez-montero L, Gotor V, Gotor-fernández V, Lavandera I. Stereoselective amination of racemic sec-alcohols through sequential application of laccases and transaminases. Green Chem 2017;19:474-80.
24. Méndez-sánchez D, Mangas-sánchez J, Lavandera I, Gotor V, Gotor-fernández V. Chemoenzymatic deracemization of secondary alcohols by using a TEMPO-Iodine-alcohol dehydrogenase system. ChemCatChem 2015;7:4016-20.
25. de Gonzalo G, Paul CE. Recent trends in synthetic enzymatic cascades promoted by alcohol dehydrogenases. Curr Opin Green Sust 2021;32:100548.
26. Schoemaker HE, Mink D, Wubbolts MG. Dispelling the myths--biocatalysis in industrial synthesis. Science 2003;299:1694-7.
27. Hartmann M, Kostrov X. Immobilization of enzymes on porous silicas--benefits and challenges. Chem Soc Rev 2013;42:6277-89.
28. Gao J, Kong W, Zhou L, et al. Monodisperse core-shell magnetic organosilica nanoflowers with radial wrinkle for lipase immobilization. Chem Eng J 2017;309:70-9.
29. Deng J, Wang H, Zhan H, et al. Catalyzed degradation of polycyclic aromatic hydrocarbons by recoverable magnetic chitosan immobilized laccase from Trametes versicolor. Chemosphere 2022;301:134753.
30. 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;10:69-78.
31. Gao J, Wang Y, Du Y, et al. Construction of biocatalytic colloidosome using lipase-containing dendritic mesoporous silica nanospheres for enhanced enzyme catalysis. Chem Eng J 2017;317:175-86.
32. Videira-quintela D, Martin O, Montalvo G. Emerging opportunities of silica-based materials within the food industry. Microchem J 2021;167:106318.
33. Costantini A, Califano V. Lipase immobilization in mesoporous silica nanoparticles for biofuel production. Catalysts 2021;11:629.
34. Kalantari M, Yu M, Yang Y, et al. Tailoring mesoporous-silica nanoparticles for robust immobilization of lipase and biocatalysis. Nano Res 2017;10:605-17.
35. Cao G, Gao J, Zhou L, et al. Fabrication of Ni2+-nitrilotriacetic acid functionalized magnetic mesoporous silica nanoflowers for one pot purification and immobilization of His-tagged ω-transaminase. BioChem Eng J 2017;128:116-25.
36. Zhou L, Ouyang Y, Kong W, et al. One pot purification and co-immobilization of His-tagged old yellow enzyme and glucose dehydrogenase for asymmetric hydrogenation. Enzyme Microb Technol 2022;156:110001.
37. Li Y, Luan P, Dong L, et al. Asymmetric reduction of conjugated C=C bonds by immobilized fusion of old yellow enzyme and glucose dehydrogenase. Green Synth Catal 2022:online ahead of print.
38. Gao L, Wang Z, Liu Y, et al. Co-immobilization of metal and enzyme into hydrophobic nanopores for highly improved chemoenzymatic asymmetric synthesis. Chem Commun 2020;56:13547-50.
39. Kong W, Liu Y, Huang C, et al. Direct asymmetric reductive amination of alkyl (hetero)aryl ketones by an engineered amine dehydrogenase. Angewandte Chemie 2022;134:e202202264.
40. Demir A, Şeşenoglu Ö, Eren E, et al. Enantioselective synthesis of α-Hydroxy ketones via benzaldehyde lyase-catalyzed C−C bond formation reaction. Adv Synth Catal 2002;344:96-103.
41. Peng B, Ma CL, Zhang PQ, et al. An effective hybrid strategy for converting rice straw to furoic acid by tandem catalysis via Sn-sepiolite combined with recombinant E. coli whole cells harboring horse liver alcohol dehydrogenase. Green Chem 2019;21:5914-23.
42. Ghannadi S, Abdizadeh H, Miroliaei M, Saboury AA. Immobilization of alcohol dehydrogenase on titania nanoparticles to enhance enzyme stability and remove substrate inhibition in the reaction of formaldehyde to methanol. Ind Eng Chem Res 2019;58:9844-54.
43. Esmaeilnejad-ahranjani P, Kazemeini M, Singh G, Arpanaei A. Amine-functionalized magnetic nanocomposite particles for efficient immobilization of lipase: effects of functional molecule size on properties of the immobilized lipase. RSC Adv 2015;5:33313-27.
44. Zang L, Qiu J, Wu X, Zhang W, Sakai E, Wei Y. Preparation of magnetic chitosan nanoparticles as support for cellulase immobilization. Ind Eng Chem Res 2014;53:3448-54.
45. Barbosa O, Ortiz C, Berenguer-murcia Á, Torres R, Rodrigues RC, Fernandez-lafuente R. Glutaraldehyde in bio-catalysts design: a useful crosslinker and a versatile tool in enzyme immobilization. RSC Adv 2014;4:1583-600.
46. Songulashvili G, Jimenéz-Tobón GA, Jaspers C, Penninckx MJ. Immobilized laccase of Cerrena unicolor for elimination of endocrine disruptor micropollutants. Fungal Biol 2012;116:883-9.
47. Zhang J, Xu Z, Chen H, Zong Y. Removal of 2,4-dichlorophenol by chitosan-immobilized laccase from Coriolus versicolor. BioChem Eng J 2009;45:54-9.
48. Sathishkumar P, Kamala-kannan S, Cho M, et al. 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.
49. Kašpar O, Tokárová V, Nyanhongo GS, Gübitz G, Štěpánek F. Effect of cross-linking method on the activity of spray-dried chitosan microparticles with immobilized laccase. Food Bioprod Process 2013;91:525-33.
50. Li X, Zhu H, Feng J, et al. One-pot polylol synthesis of graphene decorated with size- and density-tunable Fe3O4 nanoparticles for porcine pancreatic lipase immobilization. Carbon 2013;60:488-97.
51. Ida J, Matsuyama T, Yamamoto H. Immobilization of glucoamylase on ceramic membrane surfaces modified with a new method of treatment utilizing SPCP-CVD. Biochem Eng J 2000;5:179-84.
52. Grahame DAS, Bryksa BC, Yada RY. Improving and tailoring enzymes for food quality and functionality. Woodhead Publishing; 2015.pp.11-55.
53. Frankenberger W, Johanson J. Effect of pH on enzyme stability in soils. Soil Biol Biochem 1982;14:433-7.
54. Puetz H, Puchľová E, Vranková K, Hollmann F. Biocatalytic oxidation of alcohols. Catalysts 2020;10:952.
55. Lalonde J. Highly engineered biocatalysts for efficient small molecule pharmaceutical synthesis. Curr Opin Biotechnol 2016;42:152-8.
56. Paul CE, Lavandera I, Gotor‐Fernández V, Kroutil W, Gotor V. Escherichia coli /ADH-A: an all-inclusive catalyst for the selective biooxidation and deracemisation of secondary alcohols. ChemCatChem 2013;5:3875-81.
57. Musa MM, Hollmann F, Mutti FG. Synthesis of enantiomerically pure alcohols and amines via biocatalytic deracemisation methods. Catal Sci Technol 2019;9:5487-503.
58. Mutti FG, Knaus T, Scrutton NS, Breuer M, Turner NJ. Conversion of alcohols to enantiopure amines through dual-enzyme hydrogen-borrowing cascades. Science 2015;349:1525-9.
