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Volumn 109, Issue , 2016, Pages 51-58

Enzymatic clarification of fruit juices using xylanase immobilized on 1,3,5-triazine-functionalized silica-encapsulated magnetic nanoparticles

Author keywords

Biocatalysis; Enzyme technology; Food engineering; Immobilized enzyme; Magnetic nanoparticles; Xylanase

Indexed keywords

CLARIFIERS; ELECTRON MICROSCOPY; ENZYMES; FOURIER TRANSFORM INFRARED SPECTROSCOPY; FRUIT JUICES; FRUITS; HIGH RESOLUTION TRANSMISSION ELECTRON MICROSCOPY; MAGNETISM; METAL IONS; METALS; NANOMAGNETICS; NANOPARTICLES; ORGANIC SOLVENTS; PH EFFECTS; SCANNING ELECTRON MICROSCOPY; SILICA; SOLVENTS; SYNTHESIS (CHEMICAL); TRANSMISSION ELECTRON MICROSCOPY; X RAY POWDER DIFFRACTION;

EID: 84954557938     PISSN: 1369703X     EISSN: 1873295X     Source Type: Journal    
DOI: 10.1016/j.bej.2015.12.013     Document Type: Article
Times cited : (117)

References (42)
  • 1
    • 80052967874 scopus 로고    scopus 로고
    • Characterization of statistically produced xylanase for enrichment of fruit juice clarification process
    • Dhiman S.S., Garg G., Sharma J., Mahajan R. Characterization of statistically produced xylanase for enrichment of fruit juice clarification process. New Biotechnol. 2011, 28:746-755.
    • (2011) New Biotechnol. , vol.28 , pp. 746-755
    • Dhiman, S.S.1    Garg, G.2    Sharma, J.3    Mahajan, R.4
  • 2
    • 26444616577 scopus 로고    scopus 로고
    • Optimizing conditions for enzymatic clarification of banana juice using response surface methodology (RSM)
    • Lee W., Yusof S., Hamid N.S.A., Baharin B.S. Optimizing conditions for enzymatic clarification of banana juice using response surface methodology (RSM). J. Food Eng. 2006, 73:55-63.
    • (2006) J. Food Eng. , vol.73 , pp. 55-63
    • Lee, W.1    Yusof, S.2    Hamid, N.S.A.3    Baharin, B.S.4
  • 3
    • 40849126876 scopus 로고    scopus 로고
    • A study of retention of sugars in the process of clarification of pineapple juice (Ananas comosus, L. Merril) by micro-and ultra-filtration
    • De Carvalho L.M.J., De Castro I.M., Da Silva C.A.B. A study of retention of sugars in the process of clarification of pineapple juice (Ananas comosus, L. Merril) by micro-and ultra-filtration. J. Food Eng. 2008, 87:447-454.
    • (2008) J. Food Eng. , vol.87 , pp. 447-454
    • De Carvalho, L.M.J.1    De Castro, I.M.2    Da Silva, C.A.B.3
  • 4
    • 84870885611 scopus 로고    scopus 로고
    • Iron oxide filled magnetic carbon nanotube-enzyme conjugates for recycling of amyloglucosidase: toward useful applications in biofuel production process
    • Goh W.J., Makam V.S., Hu J., Kang L., Zheng M., Yoong S.L., Udalagama C.N., Pastorin G. Iron oxide filled magnetic carbon nanotube-enzyme conjugates for recycling of amyloglucosidase: toward useful applications in biofuel production process. Langmuir 2012, 28:16864-16873.
    • (2012) Langmuir , vol.28 , pp. 16864-16873
    • Goh, W.J.1    Makam, V.S.2    Hu, J.3    Kang, L.4    Zheng, M.5    Yoong, S.L.6    Udalagama, C.N.7    Pastorin, G.8
  • 5
    • 80054938906 scopus 로고    scopus 로고
    • Efficacy of xylanase purified from Aspergillus niger DFR-5 alone and in combination with pectinase and cellulase to improve yield and clarity of pineapple juice
    • Pal A., Khanum F. Efficacy of xylanase purified from Aspergillus niger DFR-5 alone and in combination with pectinase and cellulase to improve yield and clarity of pineapple juice. J. Food Sci. Technol. 2011, 48:560-568.
    • (2011) J. Food Sci. Technol. , vol.48 , pp. 560-568
    • Pal, A.1    Khanum, F.2
  • 6
    • 58149154817 scopus 로고    scopus 로고
    • Hyper production of cellulase-free xylanase by Thermomyces lanuginosus SSBP on bagasse pulp and its application in biobleaching
    • Manimaran A., Kumar K.S., Permaul K., Singh S. Hyper production of cellulase-free xylanase by Thermomyces lanuginosus SSBP on bagasse pulp and its application in biobleaching. Appl. Microbiol. Biotechnol. 2009, 81:887-893.
    • (2009) Appl. Microbiol. Biotechnol. , vol.81 , pp. 887-893
    • Manimaran, A.1    Kumar, K.S.2    Permaul, K.3    Singh, S.4
  • 7
    • 21344435552 scopus 로고    scopus 로고
    • Characterization of a xylanase from the newly isolated thermophilic Thermomyces lanuginosus CAU44 and its application in bread making
    • Jiang Z., Yang S., Tan S., Li L., Li X. Characterization of a xylanase from the newly isolated thermophilic Thermomyces lanuginosus CAU44 and its application in bread making. Lett. Appl. Microbiol. 2005, 41:69-76.
    • (2005) Lett. Appl. Microbiol. , vol.41 , pp. 69-76
    • Jiang, Z.1    Yang, S.2    Tan, S.3    Li, L.4    Li, X.5
  • 9
    • 4444277888 scopus 로고    scopus 로고
    • Effect of supplementation of xylanase and phospholipase to a wheat-based diet for weanling pigs on nutrient digestibility and concentrations of microbial metabolites in ileal digesta and feces
    • Diebold G., Mosenthin R., Piepho H.-P., Sauer W. Effect of supplementation of xylanase and phospholipase to a wheat-based diet for weanling pigs on nutrient digestibility and concentrations of microbial metabolites in ileal digesta and feces. J. Anim. Sci. 2004, 82:2647-2656.
    • (2004) J. Anim. Sci. , vol.82 , pp. 2647-2656
    • Diebold, G.1    Mosenthin, R.2    Piepho, H.-P.3    Sauer, W.4
  • 11
    • 3142763845 scopus 로고    scopus 로고
    • Application of chitin-and chitosan-based materials for enzyme immobilizations: a review
    • Krajewska B. Application of chitin-and chitosan-based materials for enzyme immobilizations: a review. Enzyme Microb. Technol. 2004, 35:126-139.
    • (2004) Enzyme Microb. Technol. , vol.35 , pp. 126-139
    • Krajewska, B.1
  • 13
    • 80051793850 scopus 로고    scopus 로고
    • Enhancing the functional properties of thermophilic enzymes by chemical modification and immobilization
    • Cowan D.A., Fernandez-Lafuente R. Enhancing the functional properties of thermophilic enzymes by chemical modification and immobilization. Enzyme Microb. Technol. 2011, 49:326-346.
    • (2011) Enzyme Microb. Technol. , vol.49 , pp. 326-346
    • Cowan, D.A.1    Fernandez-Lafuente, R.2
  • 14
    • 84951759187 scopus 로고    scopus 로고
    • Functionalized superparamagnetic graphene oxide nanosheet in enzyme engineering: a highly dispersive, stable and robust biocatalyst
    • Royvaran M., Taheri-Kafrani A., Landarani-Isfahani A., Mohammadi S. Functionalized superparamagnetic graphene oxide nanosheet in enzyme engineering: a highly dispersive, stable and robust biocatalyst. Chem. Eng. J. 2016, 288:414-422.
    • (2016) Chem. Eng. J. , vol.288 , pp. 414-422
    • Royvaran, M.1    Taheri-Kafrani, A.2    Landarani-Isfahani, A.3    Mohammadi, S.4
  • 15
    • 84861898733 scopus 로고    scopus 로고
    • Xylanase immobilized nanoporous gold as a highly active and stable biocatalyst
    • Yan X., Wang X., Zhao P., Xu P., Ding Y. Xylanase immobilized nanoporous gold as a highly active and stable biocatalyst. Microporous Mesoporous Mater. 2012, 161:1-6.
    • (2012) Microporous Mesoporous Mater. , vol.161 , pp. 1-6
    • Yan, X.1    Wang, X.2    Zhao, P.3    Xu, P.4    Ding, Y.5
  • 16
    • 38549130729 scopus 로고    scopus 로고
    • Simultaneous refolding, purification and immobilization of xylanase with multi-walled carbon nanotubes
    • Shah S., Gupta M.N. Simultaneous refolding, purification and immobilization of xylanase with multi-walled carbon nanotubes. Biochim. Biophys. Acta 2008, 1784:363-367.
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 363-367
    • Shah, S.1    Gupta, M.N.2
  • 17
    • 84923667125 scopus 로고    scopus 로고
    • Covalent attachment of xylanase on functionalized magnetic nanoparticles and determination of its activity and stability
    • Soozanipour A., Taheri-Kafrani A., Landarani Isfahani A. Covalent attachment of xylanase on functionalized magnetic nanoparticles and determination of its activity and stability. Chem. Eng. J. 2015, 270:235-243.
    • (2015) Chem. Eng. J. , vol.270 , pp. 235-243
    • Soozanipour, A.1    Taheri-Kafrani, A.2    Landarani Isfahani, A.3
  • 18
    • 84939838740 scopus 로고    scopus 로고
    • Xylanase immobilized on novel multifunctional hyperbranched polyglycerol-grafted magnetic nanoparticles: an efficient and robust biocatalyst
    • Landarani Isfahani A., Taheri-Kafrani A., Amini M., Mirkhani V., Moghadam M., Soozanipour A., Razmjou A. Xylanase immobilized on novel multifunctional hyperbranched polyglycerol-grafted magnetic nanoparticles: an efficient and robust biocatalyst. Langmuir 2015, 31:9219-9227.
    • (2015) Langmuir , vol.31 , pp. 9219-9227
    • Landarani Isfahani, A.1    Taheri-Kafrani, A.2    Amini, M.3    Mirkhani, V.4    Moghadam, M.5    Soozanipour, A.6    Razmjou, A.7
  • 19
    • 0034669586 scopus 로고    scopus 로고
    • Simultaneous purification and immobilization of Aspergillus niger xylanase on the reversibly soluble polymer Eudragit TM L-100
    • Sardar M., Roy I., Gupta M.N. Simultaneous purification and immobilization of Aspergillus niger xylanase on the reversibly soluble polymer Eudragit TM L-100. Enzyme Microb. Technol. 2000, 27:672-679.
    • (2000) Enzyme Microb. Technol. , vol.27 , pp. 672-679
    • Sardar, M.1    Roy, I.2    Gupta, M.N.3
  • 20
    • 84873606993 scopus 로고    scopus 로고
    • Xylanase immobilization on functionalized polyaniline support by covalent attachment
    • Madakbaş S., Daniş Ö., Demir S., Kahraman M.V. Xylanase immobilization on functionalized polyaniline support by covalent attachment. Starch-Starke 2013, 65:146-150.
    • (2013) Starch-Starke , vol.65 , pp. 146-150
    • Madakbaş, S.1    Daniş, Ö.2    Demir, S.3    Kahraman, M.V.4
  • 21
    • 64649106692 scopus 로고    scopus 로고
    • Direct electrochemistry of glucose oxidase and biosensing for glucose based on graphene
    • Shan C., Yang H., Song J., Han D., Ivaska A., Niu L. Direct electrochemistry of glucose oxidase and biosensing for glucose based on graphene. Anal. Chem. 2009, 81:2378-2382.
    • (2009) Anal. Chem. , vol.81 , pp. 2378-2382
    • Shan, C.1    Yang, H.2    Song, J.3    Han, D.4    Ivaska, A.5    Niu, L.6
  • 22
    • 84882945349 scopus 로고    scopus 로고
    • Progress in enzyme immobilization in ordered mesoporous materials and related applications
    • Zhou Z., Hartmann M. Progress in enzyme immobilization in ordered mesoporous materials and related applications. Chem. Soc. Rev. 2013, 42:3894-3912.
    • (2013) Chem. Soc. Rev. , vol.42 , pp. 3894-3912
    • Zhou, Z.1    Hartmann, M.2
  • 23
    • 84871271401 scopus 로고    scopus 로고
    • Enhanced catalytic activity of self-assembled-monolayer-capped gold nanoparticles
    • Taguchi T., Isozaki K., Miki K. Enhanced catalytic activity of self-assembled-monolayer-capped gold nanoparticles. Adv. Mater. 2012, 24:6462-6467.
    • (2012) Adv. Mater. , vol.24 , pp. 6462-6467
    • Taguchi, T.1    Isozaki, K.2    Miki, K.3
  • 25
    • 84876950303 scopus 로고    scopus 로고
    • 4) as a support for recyclable catalysts in the development of sustainable methodologies
    • 4) as a support for recyclable catalysts in the development of sustainable methodologies. Chem. Soc. Rev. 2013, 42:3371-3393.
    • (2013) Chem. Soc. Rev. , vol.42 , pp. 3371-3393
    • Gawande, M.B.1    Branco, P.S.2    Varma, R.S.3
  • 26
    • 84896897096 scopus 로고    scopus 로고
    • Covalent immobilization of porcine pancreatic lipase on carboxyl-activated magnetic nanoparticles: characterization and application for enzymatic inhibition assays
    • Zhu Y.-T., Ren X.-Y., Liu Y.-M., Wei Y., Qing L.-S., Liao X. Covalent immobilization of porcine pancreatic lipase on carboxyl-activated magnetic nanoparticles: characterization and application for enzymatic inhibition assays. Mater. Sci. Eng. C 2014, 38:278-285.
    • (2014) Mater. Sci. Eng. C , vol.38 , pp. 278-285
    • Zhu, Y.-T.1    Ren, X.-Y.2    Liu, Y.-M.3    Wei, Y.4    Qing, L.-S.5    Liao, X.6
  • 27
    • 84908611407 scopus 로고    scopus 로고
    • Well-defined bioarchitecture for immobilization of chloroperoxidase on magnetic nanoparticles and its application in dye decolorization
    • Cui R., Bai C., Jiang Y., Hu M., Li S., Zhai Q. Well-defined bioarchitecture for immobilization of chloroperoxidase on magnetic nanoparticles and its application in dye decolorization. Chem. Eng. J. 2015, 259:640-646.
    • (2015) Chem. Eng. J. , vol.259 , pp. 640-646
    • Cui, R.1    Bai, C.2    Jiang, Y.3    Hu, M.4    Li, S.5    Zhai, Q.6
  • 28
    • 47249140441 scopus 로고    scopus 로고
    • Magnetic iron oxide nanoparticles: synthesis, stabilization, vectorization, physicochemical characterizations, and biological applications
    • Laurent S., Forge D., Port M., Roch A., Robic C., Vander Elst L., Muller R.N. Magnetic iron oxide nanoparticles: synthesis, stabilization, vectorization, physicochemical characterizations, and biological applications. Chem. Rev. 2008, 108:2064-2110.
    • (2008) Chem. Rev. , vol.108 , pp. 2064-2110
    • Laurent, S.1    Forge, D.2    Port, M.3    Roch, A.4    Robic, C.5    Vander Elst, L.6    Muller, R.N.7
  • 30
  • 31
    • 67650492686 scopus 로고    scopus 로고
    • Cu(II)-azabis(oxazoline)-complexes immobilized on superparamagnetic magnetite@silica-nanoparticles: a highly selective and recyclable catalyst for the kinetic resolution of 1,2-diols
    • Schätz A., Hager M., Reiser O. Cu(II)-azabis(oxazoline)-complexes immobilized on superparamagnetic magnetite@silica-nanoparticles: a highly selective and recyclable catalyst for the kinetic resolution of 1,2-diols. Adv. Funct. Mater. 2009, 19:2109-2115.
    • (2009) Adv. Funct. Mater. , vol.19 , pp. 2109-2115
    • Schätz, A.1    Hager, M.2    Reiser, O.3
  • 32
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 33
    • 0026537453 scopus 로고
    • Interlaboratory testing of methods for assay of xylanase activity
    • Bailey M.J., Biely P., Poutanen K. Interlaboratory testing of methods for assay of xylanase activity. J. Biotechnol. 1992, 23:257-270.
    • (1992) J. Biotechnol. , vol.23 , pp. 257-270
    • Bailey, M.J.1    Biely, P.2    Poutanen, K.3
  • 34
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller G.L. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 1959, 31:426-428.
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 36
    • 0037295457 scopus 로고    scopus 로고
    • Differential scanning calorimetric, circular dichroism, and Fourier transform infrared spectroscopic characterization of the thermal unfolding of xylanase A from Streptomyces lividans
    • Roberge M., Lewis R.N., Shareck F., Morosoli R., Kluepfel D., Dupont C., McElhaney R.N. Differential scanning calorimetric, circular dichroism, and Fourier transform infrared spectroscopic characterization of the thermal unfolding of xylanase A from Streptomyces lividans. Proteins 2003, 50:341-354.
    • (2003) Proteins , vol.50 , pp. 341-354
    • Roberge, M.1    Lewis, R.N.2    Shareck, F.3    Morosoli, R.4    Kluepfel, D.5    Dupont, C.6    McElhaney, R.N.7
  • 38
    • 0025813478 scopus 로고
    • Urease immobilized on chitosan membrane. Inactivation by heavy metal ions
    • Krajewska B. Urease immobilized on chitosan membrane. Inactivation by heavy metal ions. J. Chem. Technol. Biotechnol. 1991, 52:157-162.
    • (1991) J. Chem. Technol. Biotechnol. , vol.52 , pp. 157-162
    • Krajewska, B.1
  • 39
    • 0032985544 scopus 로고    scopus 로고
    • Immobilization of Paenibacillusmacerans NRRL B-3186 cyclodextrin glucosyltransferase and properties of the immobilized enzyme
    • Abdel-Naby M.A. Immobilization of Paenibacillusmacerans NRRL B-3186 cyclodextrin glucosyltransferase and properties of the immobilized enzyme. Process Biochem. 1999, 34:399-405.
    • (1999) Process Biochem. , vol.34 , pp. 399-405
    • Abdel-Naby, M.A.1
  • 40
    • 0036452522 scopus 로고    scopus 로고
    • Catalytic properties of the immobilized Aspergillus tamarii xylanase
    • Gouda M.K., Abdel-Naby M.A. Catalytic properties of the immobilized Aspergillus tamarii xylanase. Microbiol. Res. 2002, 157:275-281.
    • (2002) Microbiol. Res. , vol.157 , pp. 275-281
    • Gouda, M.K.1    Abdel-Naby, M.A.2
  • 41
    • 0141670504 scopus 로고    scopus 로고
    • Modeling the effect of free water on enzyme activity in immobilized lipase-catalyzed reactions in organic solvents
    • Páez B.C., Medina A.R., Rubio F.C., Moreno P.G., Grima E.M. Modeling the effect of free water on enzyme activity in immobilized lipase-catalyzed reactions in organic solvents. Enzyme Microb. Technol. 2003, 33:845-853.
    • (2003) Enzyme Microb. Technol. , vol.33 , pp. 845-853
    • Páez, B.C.1    Medina, A.R.2    Rubio, F.C.3    Moreno, P.G.4    Grima, E.M.5
  • 42
    • 84879992738 scopus 로고    scopus 로고
    • Enzymatic clarification of fruit juices (apple, pineapple, and tomato) using purified Bacillus pumilus SV-85S xylanase
    • Nagar S., Mittal A., Gupta V.K. Enzymatic clarification of fruit juices (apple, pineapple, and tomato) using purified Bacillus pumilus SV-85S xylanase. Biotechnol. Bioprocess Eng. 2012, 17:1165-1175.
    • (2012) Biotechnol. Bioprocess Eng. , vol.17 , pp. 1165-1175
    • Nagar, S.1    Mittal, A.2    Gupta, V.K.3


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