Preparation and characterization of nanomagnetic cross-linked cellulase aggregates for cellulose bioconversion

Journal of Chemical Technology and Biotechnology

Volumn 91, Issue 2, 2016, Pages 539-546

  Jafari Khorshidi, Kaveh ^a   Lenjannezhadian, Hengameh ^b   Jamalan, Mostafa ^c   Zeinali, Majid ^d  

^a ISLAMIC AZAD UNIVERSITY   (Iran)

^b UNIVERSITY OF TEHRAN   (Iran)

^c AHVAZ JUNDISHAPUR UNIVERSITY OF MEDICAL SCIENCES   (Iran)

^d RESEARCH INSTITUTE OF PETROLEUM INDUSTRY RIPI   (Iran)

Author keywords

Bioconversion; Cellulase; Cellulose; Cross linked enzyme aggregates; Magnetic core shell nanoparticles

Indexed keywords

AGGREGATES; BIOCONVERSION; BIOLOGICAL MATERIALS; ENZYMES; HYDROLYSIS; NANOMAGNETICS; NANOPARTICLES;

CELLULASE; CORE-SHELL NANOPARTICLES; CROSS-LINKED ENZYME AGGREGATES; HYDROLYZING ENZYMES; LIGNOCELLULOSIC MATERIAL; OPERATIONAL STABILITY; OPTIMUM TEMPERATURE; TEMPERATURE VALUES;

CELLULOSE;

AMINE; CELLULASE; CELLULOSE; CROSS LINKED CELLULASE AGGREGATE; MAGNETIC NANOPARTICLE; PROTEIN AGGREGATE; SILICA NANOPARTICLE; UNCLASSIFIED DRUG;

ACIDITY; ARTICLE; BIOTRANSFORMATION; ENZYMATIC ASSAY; ENZYME ACTIVITY; ENZYME IMMOBILIZATION; ENZYME STABILITY; HYDROLYSIS; INFRARED SPECTROSCOPY; MATERIAL COATING; PH; RECYCLING; SCANNING ELECTRON MICROSCOPY; TEMPERATURE; X RAY DIFFRACTION;

EID: 84953838053     PISSN: 02682575     EISSN: 10974660     Source Type: Journal    
DOI: 10.1002/jctb.4615     Document Type: Article

References (57)

1. Sheehan J and Himmel M, Enzymes, energy, and the environment: a strategic perspective on the US Department of Energy's research and development activities for bioethanol. Biotechnol Prog 15:817-827 (1999).
2. Dashtban M, Schraft H and Qin W, Fungal bioconversion of lignocellulosic residues; opportunities and perspectives. Int J Biol Sci 5:578-595 (2009).
3. Kim S and Dale BE, Global potential bioethanol production from wasted crops and crop residues. Biomass Bioenergy 26:361-375 (2004).
4. Kumar R, Singh S and Singh OV, Bioconversion of lignocellulosic biomass: biochemical and molecular perspectives. J Ind Microbiol Biotechnol 35:377-391 (2008).
5. Champagne P, Feasibility of producing bio-ethanol from waste residues: a Canadian perspective: feasibility of producing bio-ethanol from waste residues in Canada. Resources Conservation Recycl 50:211-230 (2007).
6. Sánchez C, Lignocellulosic residues: biodegradation and bioconversion by fungi. Biotechnol Adv 27:185-194 (2009).
7. Mosier N, Wyman C, Dale B, Elander R, Lee Y, Holtzapple M et al., Features of promising technologies for pretreatment of lignocellulosic biomass. Bioresource Technol 96:673-686 (2005).
8. Nigam PS, Gupta N and Anthwal A, Pre-treatment of agro-industrial residues, in Biotechnology for Agro-Industrial Residues Utilisation, ed. by Nigam PS and Pandey A. Springer, New York City, pp. 13-33 (2009).
9. Streamer M, Eriksson KE and Pettersson B, Extracellular enzyme system utilized by the fungus Sporotrichum pulverulentum (Chrysosporium lignorum) for the breakdown of cellulose. Eur J Biochem 59:607-613(1975).
10. Akiba S, Kimura Y, Yamamoto K and Kumagai H, Purification and characterization of a protease-resistant cellulase from Aspergillus niger. J Ferment Bioeng 79:125-130 (1995).
11. Bayer EA, Chanzy H, Lamed R and Shoham Y, Cellulose, cellulases and cellulosomes. Curr Opin Structural Biol 8:548-457 (1998).
12. Lynd LR, Van Zyl WH, McBride JE and Laser M, Consolidated bioprocessing of cellulosic biomass: an update. Curr Opin Biotechnol 16:577-583 (2005).
13. Taherzadeh MJ and Karimi K, Enzymatic-based hydrolysis processes for ethanol. Bio Resources 2:707-738 (2007).
14. Martinek K, Klibanov A, Goldmacher V and Berezin I, The principles of enzyme stabilization I. Increase in thermostability of enzymes covalently bound to a complementary surface of a polymer support in a multipoint fashion. Biochim Biophys Acta 485:1-12 (1977).
15. Rembaum A and Dreyer W, Immunomicrospheres: reagents for cell labeling and separation. Science 208:364-368 (1980).
16. Simionescu CI, Popa VI, Popa M and Maxim S, On the possibilities of immobilization and utilization of some cellulase enzymes. J Appl Polym Sci 39:1837-1846 (1990).
17. Katchalski-Katzir E, Immobilized enzymes-learning from past successes and failures. Trends Biotechnol 11:471-478 (1993).
18. Scouten WH, Luong JH and Stephen Brown R, Enzyme or protein immobilization techniques for applications in biosensor design. Trends Biotechnol 13:178-185 (1995).
19. Wang P, Sergeeva MV, Lim L and Dordick JS, Biocatalytic plastics as active and stable materials for biotransformations. Nat Biotechnol 15:789-793 (1997).
20. Collings A and Caruso F, Biosensors: recent advances. Rep Prog Phys 60:1397 (1997).
21. Caruso F, Nanoengineering of particle surfaces. Adv Mater 13:11-22 (2001).
22. 4 and characterization. Biotechnol Bioeng 33:321-326 (1989).
23. Mao X, Guo G, Huang J, Du Z, Huang Z, Ma L et al., A novel method to prepare chitosan powder and its application in cellulase immobilization. J Chem Technol Biotechnol 81:189-195 (2006).
24. Cao L, van Rantwijk F and Sheldon RA, Cross-linked enzyme aggregates: a simple and effective method for the immobilization of penicillin acylase. Org Lett 2:1361-1364 (2000).
25. Shah S, Sharma A and Gupta MN, Preparation of cross-linked enzyme aggregates by using bovine serum albumin as a proteic feeder. Anal Biochem 351:207-213 (2006).
26. Aytar BS and Bakir U, Preparation of cross-linked tyrosinase aggregates. Process Biochem 43:125-131(2008).
27. Van Langen LM, Selassa RP, Van Rantwijk F and Sheldon RA, Cross-linked aggregates of (R)-oxynitrilase: a stable, recyclable biocatalyst for enantioselective hydrocyanation. Org Lett 7:327-329 (2005).
28. Gupta P, Dutt K, Misra S, Raghuwanshi S and Saxena RK, Characterization of cross-linked immobilized lipase from thermophilic mould Thermomyces lanuginosa using glutaraldehyde. Bioresource Technol 100:4074-4076 (2009).
29. Roberge C, Amos D, Pollard D and Devine P, Preparation and application of cross-linked aggregates of chloroperoxidase with enhanced hydrogen peroxide tolerance. J Mol Catal B: Enzyme 56:41-45 (2009).
30. Vaidya BK, Kuwar SS, Golegaonkar SB and Nene SN, Preparation of cross-linked enzyme aggregates of l-aminoacylase via co-aggregation with polyethyleneimine. J Mol Catal B: Enzyme 74:184-191 (2012).
31. Lopez-Serrano P, Cao L, Van Rantwijk F and Sheldon R, Cross-linked enzyme aggregates with enhanced activity: application to lipases. Biotechnol Lett 24:1379-1383 (2002).
32. Sheldon R, Cross-linked enzyme aggregates (CLEAs): stable and recyclable biocatalysts. Biochem Soc Trans 35:1583-1587 (2007).
33. Dalal S, Kapoor M and Gupta MN, Preparation and characterization of combi-CLEAs catalyzing multiple non-cascade reactions. J Mol Catal B: Enzyme 44:128-132 (2007).
34. Sheldon RA, Characteristic features and biotechnological applications of cross-linked enzyme aggregates (CLEAs). Appl Microbiol Biotechnol 92:467-477 (2011).
35. Kim M, Park JM, Um HJ, Lee DH, Lee KH, Kobayashi F et al., Immobilization of cross-linked lipase aggregates onto magnetic beads for enzymatic degradation of polycaprolactone. J Basic Microbiol 50:218-226 (2010).
36. Matijošyte I, Arends IW, de Vries S and Sheldon RA, Preparation and use of cross-linked enzyme aggregates (CLEAs) of laccases. J Mol Catal B: Enzyme 62:142-148 (2010).
37. Talekar S, Ghodake V, Ghotage T, Rathod P, Deshmukh P, Nadar S et al., Novel magnetic cross-linked enzyme aggregates (magnetic CLEAs) of alpha amylase. Bioresour Technol 123:542-547 (2012).
38. Ju H, Jang E, Ryu BH and Kim TD, Characterization and preparation of highly stable aggregates of a novel type of hydrolase (BL28) from Bacillus licheniformis. Bioresource Technol 128:81-86 (2013).
39. Lu AH, Salabas EL and Schuth F, Magnetic nanoparticles: synthesis, protection, functionalization, and application. Angew Chem Int Ed Engl 46:1222-1244 (2007).
40. Laurent S, Forge D, Port M, Roch A, Robic C, Vander Elst L et al., Magnetic iron oxide nanoparticles: synthesis, stabilization, vectorization, physicochemical characterizations, and biological applications. Chem Rev 108:2064-2110 (2008).
41. Yang D, Hu J and Fu S, Controlled synthesis of magnetite-silica nanocomposites via a seeded sol-gel approach. J Phys Chem C 113:7646-7651 (2009).
42. Wu W, He Q and Jiang C, Magnetic iron oxide nanoparticles: synthesis and surface functionalization strategies. Nanoscale Res Lett 3:397-415 (2009).
43. Bumb A, Brechbiel M, Choyke P, Fugger L, Eggeman A, Prabhakaran D et al., Synthesis and characterization of ultra-small superparamagnetic iron oxide nanoparticles thinly coated with silica. Nanotechnology 19:335601 (2008).
44. Chim-anage P, Kashiwagi Y, Magae Y, Ohta T and Sasaki T, Properties of cellulase immobilized on agarose gel with spacer. Biotechnol Bioeng 28:1876-1878 (1986).
45. Tu M, Zhang X, Kurabi A, Gilkes N, Mabee W and Saddler J, Immobilization of β-glucosidase on Eupergit C for lignocellulose hydrolysis. Biotechnol Lett 28:151-156 (2006).
46. Hirsh S, Bilek M, Nosworthy N, Kondyurin A, Dos Remedios C and McKenzie D, A comparison of covalent immobilization and physical adsorption of a cellulase enzyme mixture. Langmuir 26:14380-14388 (2010).
47. Zhou J, Immobilization of cellulase on a reversibly soluble-insoluble support: properties and application. J Agric Food Chem 58:6741-6746 (2010).
48. Daoud FB-O, Kaddour S and Sadoun T, Adsorption of cellulase Aspergillus niger on a commercial activated carbon: kinetics and equilibrium studies. Colloids Surf B Biointerfaces 75:93-99 (2010).
49. Xu Z, Miao Y, Chen JY, Jiang X, Lin L and Ouyang P, Co-immobilization mechanism of cellulase and xylanase on a reversibly soluble polymer. Appl Biochem Biotechnol 163:153-161 (2011).
50. Gokhale AA, Lu J and Lee I, Immobilization of cellulase on magnetoresponsive graphene nano-supports. J Mol Catal B: Enzyme 90:76-86 (2013).
51. Stöber W, Fink A and Bohn E, Controlled growth of monodisperse silica spheres in the micron size range. J Colloid Interface Sci 26:62-69 (1968).
52. Lever M, A new reaction for colorimetric determination of carbohydrates. Anal Biochem 47:273-279 (1972).
53. Sangeetha K and Emilia Abraham T, Preparation and characterization of cross-linked enzyme aggregates (CLEA) of subtilisin for controlled release applications. Int J Biol Macromol 43:314-319 (2008).
54. Wang M, Qi W, Jia C, Ren Y, Su R and He Z, Enhancement of activity of cross-linked enzyme aggregates by a sugar-assisted precipitation strategy: technical development and molecular mechanism. J Biotechnol 156:30-38 (2011).
55. Sun WQ, Davidson P and Chan HS, Protein stability in the amorphous carbohydrate matrix: relevance to anhydrobiosis. Biochim Biophys Acta 1425:245-254 (1998).
56. Iyer PV and Ananthanarayan L, Enzyme stability and stabilization-aqueous and non-aqueous environment. Process Biochem 43:1019-1032 (2008).
57. Bilen J and Bakir U, The effect of crosslinking on thermal inactivation of cellulases. Prog Biotechnol 15:151-156 (1998).