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Immobilization of Cholesterol Oxidase: An Overview

Ghosh, Shubhrima, Ahmad, Razi, Khare, Sunil Kumar·2018·The Open Biotechnology Journal

Abstract

Background: Cholesterol oxidases are bacterial oxidases widely used commercially for their application in the detection of cholesterol in blood serum, clinical or food samples. Additionally, these enzymes find potential applications as an insecticide, synthesis of anti-fungal antibiotics and a biocatalyst to transform a number of sterol and non-sterol compounds. However, the soluble form of cholesterol oxidases are found to be less stable when applied at higher temperatures, broader pH range, and incur higher costs. These disadvantages can be overcome by immobilization on carrier matrices. Methods: This review focuses on the immobilization of cholesterol oxidases on various macro/micro matrices as well as nanoparticles and their potential applications. Selection of appropriate support matrix in enzyme immobilization is of extreme importance. Recently, nanomaterials have been used as a matrix for immobilization of enzyme due to their large surface area and small size. The bio-compatible length scales and surface chemistry of nanoparticles provide reusability, stability and enhanced performance characteristics for the enzyme-nanoconjugates. Conclusion: In this review, immobilization of cholesterol oxidase on nanomaterials and other matrices are discussed. Immobilization on nanomatrices has been observed to increase the stability and activity of enzymes. This enhances the applicability of cholesterol oxidases for various industrial and clinical applications such as in biosensors.

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Cited by 26

Research works printed but not linked: 118

  1. Radzicka A, Wolfenden R. A proficient enzyme. Science 1995; 267 (5194) : 90-3. · DOI · Paper page
  2. Ahmad R, Sardar M. Enzyme immobilization: An overview on nanoparticles as immobilization matrix. Biochem & Anal Biochem 2015; 4 (3) : 1-8. · DOI · Paper page
  3. Ahmad R, Mishra A, Sardar M. Peroxidase-TiO2 nanobioconjugates for the removal of phenols and dyes from aqueous solutions. Adv Sci Eng Med 2013; 5 (10) : 1020-5. · doi:10.1166/asem.2013.1387
  4. Kirk O, Borchert TV, Fuglsang CC. Industrial enzyme applications. Curr Opin Biotechnol 2002; 13 (4) : 345-51. · DOI · Paper page
  5. Koeller KM, Wong CH. Enzymes for chemical synthesis. Nature 2001; 409 (6817) : 232-40. · DOI · Paper page
  6. Palmer T, Bonner PL. Enzymes: Biochemistry, biotechnology, clinical chemistry 2007. · doi:10.1533/9780857099921
  7. Ansari SA, Husain Q. Potential applications of enzymes immobilized on/in nano materials: A review. Biotechnol Adv 2012; 30 (3) : 512-23. · DOI · Paper page
  8. Rodrigues RC, Ortiz C, Berenguer-Murcia Á, Torres R, Fernández-Lafuente R. Modifying enzyme activity and selectivity by immobilization. Chem Soc Rev 2013; 42 (15) : 6290-307. · DOI · Paper page
  9. Talbert JN, Goddard JM. Enzymes on material surfaces. Colloids Surf B Biointerfaces 2012; 93 : 8-19. · DOI · Paper page
  10. Bryjak J, Kolarz BN. Immobilisation of trypsin on acrylic copolymers. Process Biochem 1998; 33 (4) : 409-17. · doi:10.1016/s0032-9592(97)00098-8
  11. Janssen MHA, van Langen LM, Pereira SRM, van Rantwijk F, Sheldon RA. Evaluation of the performance of immobilized penicillin G acylase using active-site titration. Biotechnol Bioeng 2002; 78 (4) : 425-32. · DOI
  12. Fernandez-Lafuente R. Stabilization of multimeric enzymes: Strategies to prevent subunit dissociation. Enzyme Microb Technol 2009; 45 (6) : 405-18. · DOI · Paper page
  13. Albanese A, Tang PS, Chan WCW. The effect of nanoparticle size, shape, and surface chemistry on biological systems. Annu Rev Biomed Eng 2012; 14 : 1-16. · DOI · Paper page
  14. Hwang ET, Gu MB. Enzyme stabilization by nano/microsized hybrid materials. Eng Life Sci 2013; 13 (1) : 49-61. · DOI · Paper page
  15. Sotiropoulou S, Chaniotakis NA. Carbon nanotube array-based biosensor. Anal Bioanal Chem 2003; 375 (1) : 103-5. · doi:10.1007/s00216-002-1617-z
  16. Mishra A, Ahmad R, Perwez M, Sardar M. Reusable green synthesized biomimetic magnetic nanoparticles for glucose and H2O2 detection. Bionanoscience 2016; 6 (2) : 93-102. · DOI
  17. Mishra A, Ahmad R, Sardar M. Biosynthesized Iron Oxide nanoparticles mimicking peroxidase activity: Application for biocatalysis and biosensing. J Nanoeng Nanomanuf 2015; 5 (1) : 37-42. · doi:10.1166/jnan.2015.1220
  18. Bellino MG, Soler-Illia GJAA. Nano-designed enzyme-functionalized hierarchical metal-oxide mesoporous thin films: En route to versatile biofuel cells. Small 2014; 10 (14) : 2834-9. · doi:10.1002/smll.201302616
  19. Dizge N, Keskinler Bl. Enzymatic production of biodiesel from canola oil using immobilized lipase. Biomass Bioenergy 2008; 32 (12) : 1274-8. · DOI
  20. Tao Y, Ning M, Dou H. A novel therapeutic system for malignant glioma: Nanoformulation, pharmacokinetic, and anticancer properties of cell-nano-drug delivery. Nanomedicine (Lond) 2013; 9 (2) : 222-32. · DOI
  21. Ahmad R, Khatoon N, Sardar M. Antibacterial effect of green synthesized TiO2 nanoparticles. Adv Sci Lett 2014; 20 (7-9) : 1616-20. · doi:10.1166/asl.2014.5563
  22. Ahmad R, Mohsin M, Ahmad T, Sardar M. Alpha amylase assisted synthesis of TiO2 nanoparticles: Structural characterization and application as antibacterial agents. J Hazard Mater 2015; 283 : 171-7. · doi:10.1016/j.jhazmat.2014.08.073
  23. Khatoon N, Ahmad R, Sardar M. Robust and fluorescent silver nanoparticles using Artemisia annua: Biosynthesis, characterization and antibacterial activity. Biochem Eng J 2015; 102 : 91-7. · DOI
  24. Liu J, Lu C-Y, Zhou H, Xu J-J, Chen H-Y. Flexible gold electrode array for multiplexed immunoelectrochemical measurement of three protein biomarkers for prostate cancer. ACS Appl Mater Interfaces 2014; 6 (22) : 20137-43. · doi:10.1021/am505726b
  25. Johnson BJ, Algar WR, Malanoski AP, Ancona MG, Medintz IL. Understanding enzymatic acceleration at nanoparticle interfaces: Approaches and challenges. Nano Today 2014; 9 (1) : 102-31. · DOI · Paper page
  26. Sinha R, Khare SK. Immobilization of halophilic Bacillus sp. EMB9 protease on functionalized silica nanoparticles and application in whey protein hydrolysis. Bioprocess Biosyst Eng 2015; 38 (4) : 739-48. · doi:10.1007/s00449-014-1314-2
  27. Ahmad R, Khatoon N, Sardar M. Biosynthesis, characterization and application of TiO2 nanoparticles in biocatalysis and protein folding. J Proteins & Proteomics 2013; 4 (2) : 115-21.
  28. Ahmad R, Mishra A, Sardar M. Simultaneous immobilization and refolding of heat treated enzymes on TiO2 nanoparticles. Adv Sci Eng Med 2014; 6 (12) : 1264-8. · doi:10.1166/asem.2014.1644
  29. Ahmad R, Sardar M. Immobilization of cellulase on TiO2 nanoparticles by physical and covalent methods: A comparative study. Indian J Biochem Biophys 2014; 51 (4) : 314-20.
  30. Grewal J, Ahmad R, Khare SK. Development of cellulase-nanoconjugates with enhanced ionic liquid and thermal stability for in situ lignocellulose saccharification. Bioresour Technol 2017; 242 : 236-43. · DOI
  31. Perwez M, Ahmad R, Sardar M. A reusable multipurpose magnetic nanobiocatalyst for industrial applications. Int J Biol Macromol 2017; 103 : 16-24. · DOI
  32. Jia H, Zhu G, Wang P. Catalytic behaviors of enzymes attached to nanoparticles: The effect of particle mobility. Biotechnol Bioeng 2003; 84 (4) : 406-14. · doi:10.1002/bit.10781
  33. Khoshnevisan K, Bordbar A-K, Zare D, et al. Immobilization of cellulase enzyme on superparamagnetic nanoparticles and determination of its activity and stability. Chem Eng J 2011; 171 (2) : 669-73. · doi:10.1016/j.cej.2011.04.039
  34. Wang L, Wei L, Chen Y, Jiang R. Specific and reversible immobilization of NADH oxidase on functionalized carbon nanotubes. J Biotechnol 2010; 150 (1) : 57-63. · doi:10.1016/j.jbiotec.2010.07.005
  35. Zhang B, Xing Y, Li Z, Zhou H, Mu Q, Yan B. Functionalized carbon nanotubes specifically bind to α-chymotrypsin’s catalytic site and regulate its enzymatic function. Nano Lett 2009; 9 (6) : 2280-4. · DOI
  36. Doukyu N. Characteristics and biotechnological applications of microbial cholesterol oxidases. Appl Microbiol Biotechnol 2009; 83 (5) : 825-37. · doi:10.1007/s00253-009-2059-8
  37. Turfitt GE. The microbiological degradation of steroids: 4. Fission of the steroid molecule. Biochem J 1948; 42 (3) : 376-83. · doi:10.1042/bj0420376
  38. Ghosh S, Khare SK. Biodegradation of 7-ketocholesterol by Rhodococcus erythropolis MTCC 3951: Process optimization and enzymatic insights. Chem Phys Lipids 2017; 207 (Pt B) : 253-9. · doi:10.1016/j.chemphyslip.2017.05.008
  39. Doukyu N, Aono R. Purification of extracellular cholesterol oxidase with high activity in the presence of organic solvents from Pseudomonas sp. strain ST-200. Appl Environ Microbiol 1998; 64 (5) : 1929-32. · doi:10.1128/aem.64.5.1929-1932.1998
  40. Ghosh S, Khare SK. Biodegradation of cytotoxic 7-Ketocholesterol by Pseudomonas aeruginosa PseA. Bioresour Technol 2016; 213 : 44-9. · DOI
  41. Doukyu N, Aono R. Cloning, sequence analysis and expression of a gene encoding an organic solvent- and detergent-tolerant cholesterol oxidase of Burkholderia cepacia strain ST-200. Appl Microbiol Biotechnol 2001; 57 (1-2) : 146-52. · doi:10.1007/s002530100753
  42. Brzostek A, Dziadek B, Rumijowska-Galewicz A, Pawelczyk J, Dziadek J. Cholesterol oxidase is required for virulence of Mycobacterium tuberculosis. FEMS Microbiol Lett 2007; 275 (1) : 106-12. · DOI
  43. Doukyu N, Shibata K, Ogino H, Sagermann M. Purification and characterization of Chromobacterium sp. DS-1 cholesterol oxidase with thermal, organic solvent, and detergent tolerance. Appl Microbiol Biotechnol 2008; 80 (1) : 59-70. · doi:10.1007/s00253-008-1526-y
  44. Gadda G, Wels G, Pollegioni L, et al. Characterization of cholesterol oxidase from Streptomyces hygroscopicus and Brevibacterium sterolicum. Eur J Biochem 1997; 250 (2) : 369-76. · DOI
  45. Yazdi MT, Zahraei M, Aghaepour K, Kamranpour N. Purification and partial characterization of a cholesterol oxidase from Streptomyces fradiae. Enzyme Microb Technol 2001; 28 (4-5) : 410-4. · doi:10.1016/s0141-0229(00)00337-9
  46. Lim L, Molla G, Guinn N, Ghisla S, Pollegioni L, Vrielink A. Structural and kinetic analyses of the H121A mutant of cholesterol oxidase. Biochem J 2006; 400 (1) : 13-22. · doi:10.1042/bj20060664
  47. Vrielink A, Ghisla S. Cholesterol oxidase: Biochemistry and structural features. FEBS J 2009; 276 (23) : 6826-43. · doi:10.1111/j.1742-4658.2009.07377.x
  48. Coulombe R, Yue KQ, Ghisla S, Vrielink A. Oxygen access to the active site of cholesterol oxidase through a narrow channel is gated by an Arg-Glu pair. J Biol Chem 2001; 276 (32) : 30435-41. · doi:10.1074/jbc.m104103200
  49. Eventoff W, Rossmann MG. The evolution of dehydrogenases and kinases. CRC Crit Rev Biochem 1975; 3 (2) : 111-40. · DOI
  50. García JL, Uhía I, Galán B. Catabolism and biotechnological applications of cholesterol degrading bacteria. Microb Biotechnol 2012; 5 (6) : 679-99. · DOI · Paper page
  51. Drzyzga O, Fernández de las Heras L, Morales V, Navarro Llorens JM, Perera J. Cholesterol degradation by Gordonia cholesterolivorans. Appl Environ Microbiol 2011; 77 (14) : 4802-10. · DOI
  52. Navas J, González-Zorn B, Ladrón N, Garrido P, Vázquez-Boland JA. Identification and mutagenesis by allelic exchange of choE, encoding a cholesterol oxidase from the intracellular pathogen Rhodococcus equi. J Bacteriol 2001; 183 (16) : 4796-805. · doi:10.1128/jb.183.16.4796-4805.2001
  53. Mendes MV, Recio E, Antón N, et al. Cholesterol oxidases act as signaling proteins for the biosynthesis of the polyene macrolide pimaricin. Chem Biol 2007; 14 (3) : 279-90. · doi:10.1016/j.chembiol.2007.01.010
  54. Singh S, Solanki PR, Pandey MK, Malhotra BD. Cholesterol biosensor based on cholesterol esterase, cholesterol oxidase and peroxidase immobilized onto conducting polyaniline films. Sens Actuators B Chem 2006; 115 (1) : 534-41. · DOI · Paper page
  55. Assmann G, Jabs HU, Kohnert U, Nolte W, Schriewer H. LDL-cholesterol determination in blood serum following precipitation of LDL with polyvinylsulfate. Clin Chim Acta 1984; 140 (1) : 77-83. · DOI · Paper page
  56. Ott P, Binggeli Y, Brodbeck U. A rapid and sensitive assay for determination of cholesterol in membrane lipid extracts. Biochim Biophys Acta 1982; 685 (2) : 211-3. · DOI
  57. Roda A, Festi D, Sama C, et al. Enzymatic determination of cholesterol in bile. Clin Chim Acta 1975; 64 (3) : 337-41. · DOI · Paper page
  58. Ahmad S, Roy PK, Khan AW, Basu SK, Johri BN. Microbial transformation of sterols to C19-steroids by Rhodococcus equi. World J Microbiol Biotechnol 1991; 7 (5) : 557-61. · doi:10.1007/bf00368360
  59. Alexander DL, Fisher JF. A convenient synthesis of 7 α-hydroxycholest-4-en-3-one by the hydroxypropyl-β-cyclodextrin-facilitated cholesterol oxidase oxidation of 3 β,7 α-cholest-5-ene-3,7-diol. Steroids 1995; 60 (3) : 290-4. · DOI
  60. Biellmann JF. Resolution of alcohols by cholesterol oxidase from Rhodococcus erythropolis: Lack of enantiospecificity for the steroids. Chirality 2001; 13 (1) : 34-9. · doi:10.1002/1520-636x(2001)13:1<34::aid-chir7>3.0.co;2-o
  61. Purcell JP, Greenplate JT, Jennings MG, et al. Cholesterol oxidase: A potent insecticidal protein active against boll weevil larvae. Biochem Biophys Res Commun 1993; 196 (3) : 1406-13. · doi:10.1006/bbrc.1993.2409
  62. Pollegioni L, Piubelli L, Molla G. Cholesterol oxidase: Biotechnological applications. FEBS J 2009; 276 (23) : 6857-70. · doi:10.1111/j.1742-4658.2009.07379.x
  63. Kumari L, Kanwar SS. Cholesterol oxidase and its applications. Adv Microbiol 2012; 2 (02) : 49-65. · doi:10.4236/aim.2012.22007
  64. Rodrigues RC, Berenguer-Murcia A, Fernandez-Lafuente R. Coupling chemical modification and immobilization to improve the catalytic performance of enzymes. Adv Synth Catal 2011; 353 (13) : 2216-38. · DOI · Paper page
  65. Garcia-Galan C, Berenguer-Murcia A, Fernandez-Lafuente R, Rodrigues RC. Potential of different enzyme immobilization strategies to improve enzyme performance. Adv Synth Catal 2011; 353 (16) : 2885-904. · DOI · Paper page
  66. Sheldon RA, van Pelt S. Enzyme immobilisation in biocatalysis: Why, what and how. Chem Soc Rev 2013; 42 (15) : 6223-35. · DOI · Paper page
  67. Petry I, Ganesan A, Pitt A, Moore BD, Halling PJ. Proteomic methods applied to the analysis of immobilized biocatalysts. Biotechnol Bioeng 2006; 95 (5) : 984-91. · DOI
  68. Spahn C, Minteer SD. Enzyme immobilization in biotechnology. Recent Pat Eng 2008; 2 (3) : 195-200. · DOI · Paper page
  69. Johnson RD, Wang ZG, Arnold FH. Surface site heterogeneity and lateral interactions in multipoint protein adsorption. J Phys Chem 1996; 100 (12) : 5134-9. · doi:10.1021/jp9523682
  70. Rao SV, Anderson KW, Bachas LG. Oriented immobilization of proteins. Mikrochim Acta 1998; 128 (3) : 127-43. · doi:10.1007/bf01243043
  71. Datta S, Christena LR, Rajaram YRS. Enzyme immobilization: An overview on techniques and support materials. 3 Biotech 2013; 3 (1) : 1-9. · DOI · Paper page
  72. Grosová Z, Rosenberg M, Rebros M, Sipocz M, Sedlácková B. Entrapment of beta-galactosidase in polyvinylalcohol hydrogel. Biotechnol Lett 2008; 30 (4) : 763-7. · DOI
  73. Deshpande A, D’Souza SF, Nadkarni GB. Coimmobilization of D-amino acid oxidase and catalase by entrapment of Trigonopsis variabilis in radiation polymerised polyacrylamide beads. J Biosci 1987; 11 (1) : 137-44. · doi:10.1007/bf02704664
  74. Singh S, Singhal R, Malhotra BD. Immobilization of cholesterol esterase and cholesterol oxidase onto sol-gel films for application to cholesterol biosensor. Anal Chim Acta 2007; 582 (2) : 335-43. · doi:10.1016/j.aca.2006.09.010
  75. Murai K, Kato K. Development of cholesterol biosensor with high sensitivity using dual-enzyme immobilization into the mesoporous silica materials. Appl Surf Sci 2013; 258 (5) : 1725-32. · doi:10.1016/j.apsusc.2011.10.023
  76. Jegan Roy J, Emilia Abraham T. Strategies in making cross-linked enzyme crystals. Chem Rev 2004; 104 (9) : 3705-22. · DOI
  77. Velasco-Lozano S, Lopez-Gallego F, Mateos-Diaz JC, Favela-Torres E. Cross-Linked Enzyme Aggregates (CLEA) in enzyme improvement-a review. Biocatalysis 2014; 1 (1) : 166-77.
  78. Brena BM, Batista-Viera F. Immobilization of enzymes: A literature survey. Immobilization of enzymes and cells 2006; 15-31. · DOI · Paper page
  79. Yong Y, Bai Y, Li Y, Lin L, Cui Y, Xia C. Preparation and application of polymer-grafted magnetic nanoparticles for lipase immobilization. J Magn Magn Mater 2008; 320 (19) : 2350-5. · DOI
  80. Bryjak J, Trochimczuk AW. Immobilization of lipase and penicillin acylase on hydrophobic acrylic carriers. Enzyme Microb Technol 2006; 39 (4) : 573-8. · doi:10.1016/j.enzmictec.2005.11.013
  81. Hartmann M, Kostrov X. Immobilization of enzymes on porous silicas-benefits and challenges. Chem Soc Rev 2013; 42 (15) : 6277-89. · DOI · Paper page
  82. Hudson S, Cooney J, Magner E. Proteins in mesoporous silicates. Angew Chem Int Ed Engl 2008; 47 (45) : 8582-94. · DOI · Paper page
  83. Betancor L, Luckarift HR. Bioinspired enzyme encapsulation for biocatalysis. Trends Biotechnol 2008; 26 (10) : 566-72. · DOI · Paper page
  84. Sardar M, Mishra A, Ahmad R. Biosynthesis of metal nanoparticles and their applications 2014; 239-66. · doi:10.1002/9781118773826.ch8
  85. Ahmad S, Goswami P. Application of chitosan beads immobilized Rhodococcus sp. NCIM 2891 cholesterol oxidase for cholestenone production. Process Biochem 2014; 49 (12) : 2149-57. · doi:10.1016/j.procbio.2014.10.004
  86. Kumar A, Malhotra R, Malhotra BD, Grover SK. Co-immobilization of cholesterol oxidase and horseradish peroxidase in a sol-gel film. Anal Chim Acta 2000; 414 (1) : 43-50. · doi:10.1016/s0003-2670(00)00792-3
  87. Pundir CS. Co-immobilization of cholesterol esterase, cholesterol oxidase and peroxidase onto alkylamine glass beads for measurement of total cholesterol in serum. Curr Appl Phys 2003; 3 (2) : 129-33. · doi:10.1016/s1567-1739(02)00178-5
  88. Chauhan N, Pundir CS. Co-immobilization of cholesterol esterase, cholesterol oxidase and peroxidase on PVC strip for serum cholesterol determination. Anal Methods 2011; 3 (6) : 1360-5. · doi:10.1039/c1ay05082f
  89. Chen Y, Xin Y, Yang H, et al. Immobilization and stabilization of cholesterol oxidase on modified sepharose particles. Int J Biol Macromol 2013; 56 : 6-13. · doi:10.1016/j.ijbiomac.2013.01.026
  90. Dervisevic M, Çevik E, Şenel M, Nergiz C, Abasiyanik MF. Amperometric cholesterol biosensor based on reconstituted cholesterol oxidase on boronic acid functional conducting polymers. J Electroanal Chem 2016; 776 : 18-24. · DOI
  91. Khan R, Kaushik A, Mishra AP. Immobilization of cholesterol oxidase onto electrochemically polymerized film of biocompatible polyaniline-Triton X-100. Mater Sci Eng C 2009; 29 (4) : 1399-403. · doi:10.1016/j.msec.2008.11.001
  92. Akkaya B, Sahin F, Demirel G, Tumturk H. Functional polymeric supports for immobilization of cholesterol oxidase. Biochem Eng J 2009; 43 (3) : 333-7. · doi:10.1016/j.bej.2008.11.003
  93. Le Huy N, Thuy NTM, Binh NH, et al. Covalent immobilization of cholesterol oxidase and poly (styrene-co-acrylic acid) magnetic microspheres on polyaniline films for amperometric cholesterol biosensing. Anal Methods 2013; 5 (6) : 1392-8. · doi:10.1039/c2ay26179k
  94. Huang J, Liu H, Zhang P, Zhang P, Li M, Ding L. Immobilization of cholesterol oxidase on magnetic fluorescent core-shell-structured nanoparticles. Mater Sci Eng C 2015; 57 : 31-7. · doi:10.1016/j.msec.2015.07.038
  95. Ghosh S, Ahmad R, Gautam VK, Khare SK. Cholesterol-oxidase-magnetic nanobioconjugates for the production of 4-cholesten-3-one and 4-cholesten-3, 7-dione. Bioresour Technol 2018; 254 : 91-6. · doi:10.1016/j.biortech.2018.01.030
  96. Kouassi GK, Irudayaraj J, McCarty G. Examination of Cholesterol oxidase attachment to magnetic nanoparticles. J Nanobiotechnology 2005; 3 (1) : 1. · DOI · Paper page
  97. Šulek F, Drofenik M, Habulin M, Knez Ž. Surface functionalization of silica-coated magnetic nanoparticles for covalent attachment of cholesterol oxidase. J Magn Magn Mater 2010; 322 (2) : 179-85. · DOI
  98. Šulek F, Knez Ž, Habulin M. Immobilization of cholesterol oxidase to finely dispersed silica-coated maghemite nanoparticles based magnetic fluid. Appl Surf Sci 2010; 256 (14) : 4596-600. · doi:10.1016/j.apsusc.2010.02.055
  99. Umar A, Ahmad R, Hwang SW, Kim SH, Al-Hajry A, Hahn YB. Development of highly sensitive and selective cholesterol biosensor based on cholesterol oxidase co-immobilized with α-Fe2O3 micro-pine shaped hierarchical structures. Electrochim Acta 2014; 135 : 396-403. · doi:10.1016/j.electacta.2014.04.173
  100. Saxena U, Chakraborty M, Goswami P. Covalent immobilization of cholesterol oxidase on self-assembled gold nanoparticles for highly sensitive amperometric detection of cholesterol in real samples. Biosens Bioelectron 2011; 26 (6) : 3037-43. · doi:10.1016/j.bios.2010.12.009
  101. Lin X, Ni Y, Kokot S. Electrochemical cholesterol sensor based on cholesterol oxidase and MoS2-AuNPs modified glassy carbon electrode. Sens Actuators B Chem 2016; 233 : 100-6. · DOI
  102. Aggarwal V, Malik J, Prashant A, Jaiwal PK, Pundir CS. Amperometric determination of serum total cholesterol with nanoparticles of cholesterol esterase and cholesterol oxidase. Anal Biochem 2016; 500 : 6-11. · doi:10.1016/j.ab.2016.01.019
  103. Temani M, Baccar ZrM, Mansour HB. Activity of cholesterol oxidase immobilized on layered double hydroxide nanomaterials for biosensor application: Acacia salicina scavenging power of hypercholesterolemia therapy. Microelectron Eng 2014; 126 : 165-8. · doi:10.1016/j.mee.2014.07.009
  104. Silva RA, Carmona-Ribeiro AM, Petri DFS. Enzymatic activity of cholesterol oxidase immobilized onto polymer nanoparticles mediated by Congo red. Colloids Surf B Biointerfaces 2013; 110 : 347-55. · DOI
  105. Li M, Huang J, Zhang P, Zhang P, Ding L, Eds. Immobilization of cholesterol oxidase on SiO2 nanoparticles and its application in fiber optic cholesterol sensor. Asia-Pacific Optical Sensors Conference 2016. · doi:10.1364/apos.2016.w4a.33
  106. Ahmad R, Khare SK. Immobilization of Aspergillus niger cellulase on multiwall carbon nanotubes for cellulose hydrolysis. Bioresour Technol 2018; 252 : 72-5. · DOI · Paper page
  107. Konwarh R, Karak N, Rai SK, Mukherjee AK. Polymer-assisted iron oxide magnetic nanoparticle immobilized keratinase. Nanotechnol 2009; 20 (22) : 225107. · doi:10.1088/0957-4484/20/22/225107
  108. Kim J-D. Immobilization of keratinase from Aspergillus flavus K-03 for degradation of feather keratin. Mycobiology 2005; 33 (2) : 121-3. · doi:10.4489/myco.2005.33.2.121
  109. Huang SH, Liao MH, Chen DH. Direct binding and characterization of lipase onto magnetic nanoparticles. Biotechnol Prog 2003; 19 (3) : 1095-100. · doi:10.1021/bp025587v
  110. Chiou S-H, Wu W-T. Immobilization of Candida rugosa lipase on chitosan with activation of the hydroxyl groups. Biomater 2004; 25 (2) : 197-204. · doi:10.1016/s0142-9612(03)00482-4
  111. Das A, Singh J, Yogalakshmi KN. Laccase immobilized magnetic iron nanoparticles: Fabrication and its performance evaluation in chlorpyrifos degradation. Int Biodeterior Biodegradation 2017; 117 : 183-9. · DOI
  112. Kunamneni A, Ghazi I, Camarero S, Ballesteros A, Plou FJ, Alcalde M. Decolorization of synthetic dyes by laccase immobilized on epoxy-activated carriers. Process Biochem 2008; 43 (2) : 169-78. · DOI · Paper page
  113. Namdeo M, Bajpai SK. Immobilization of α-amylase onto Cellulose-Coated Magnetite (CCM) nanoparticles and preliminary starch degradation study. J Mol Catal B Enzym 2009; 59 (1) : 134-9. · doi:10.1016/j.molcatb.2009.02.005
  114. Dey G, Bhupinder S, Banerjee R. Immobilization of alpha-amylase produced by Bacillus circulans GRS 313. Braz Arch Biol Technol 2003; 46 (2) : 167-76. · doi:10.1590/s1516-89132003000200005
  115. Kim D-M, Kim MY, Reddy SS, et al. Electron-transfer mediator for a NAD-glucose dehydrogenase-based glucose sensor. Anal Chem 2013; 85 (23) : 11643-9. · DOI
  116. Wang H-S, Pan Q-X, Wang G-X. A biosensor based on immobilization of horseradish peroxidase in chitosan matrix cross-linked with glyoxal for amperometric determination of hydrogen peroxide. Sensors (Basel) 2005; 5 (4) : 266-76. · doi:10.3390/s5040266
  117. Li G, Xu H, Huang W, Wang Y, Wu Y, Parajuli R. A pyrrole quinoline quinone glucose dehydrogenase biosensor based on screen-printed carbon paste electrodes modified by carbon nanotubes. Meas Sci Technol 2008; 19 (6) : 065203. · DOI
  118. Chaubey A, Gerard M, Singhal R, Singh VS, Malhotra BD. Immobilization of lactate dehydrogenase on electrochemically prepared polypyrrole-polyvinylsulphonate composite films for application to lactate biosensors. Electrochim Acta 2001; 46 (5) : 723-9. · DOI

Metadata

Authors
Ghosh, S., Ahmad, R., & Khare, S. K.
Venue
The Open Biotechnology Journal
Published
2018-08-30
Volume
12
Issue
1
Pages
176-188
ISSN
1874-0707
Cited by
26
Language
en

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

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How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: Immobilization of Cholesterol Oxidase: An Overview. https://app.cochat.ai/papers/10.2174/1874070701812010176
The paper
Ghosh, S., Ahmad, R., & Khare, S. K. (2018). Immobilization of Cholesterol Oxidase: An Overview. The Open Biotechnology Journal. https://doi.org/10.2174/1874070701812010176

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.