메뉴 건너뛰기




Volumn 4, Issue 3, 2016, Pages 828-834

A Novel Approach to Enzymatic Unhairing and Fiber Opening of Skin Using Enzymes Immobilized on Magnetite Nanoparticles

Author keywords

Dehairing; Fiber opening; Fibrozyme; Immobilization; Iron oxide nanoparticles; Nanozyme

Indexed keywords

ENZYME IMMOBILIZATION; ENZYMES; FIBERS; INDICATORS (CHEMICAL); IRON OXIDES; LEATHER; MAGNETITE NANOPARTICLES; METAL NANOPARTICLES; METALS; NANOPARTICLES; PROTEINS; RADIOACTIVE WASTE VITRIFICATION; SCANNING ELECTRON MICROSCOPY; STAINLESS STEEL; TISSUE;

EID: 84960154825     PISSN: None     EISSN: 21680485     Source Type: Journal    
DOI: 10.1021/acssuschemeng.5b00869     Document Type: Article
Times cited : (29)

References (36)
  • 1
    • 36448983569 scopus 로고    scopus 로고
    • Ecofriendly lime and sulfide free enzymatic dehairing of skins and hides using a bacterial alkaline protease
    • Sivasubramanian, S.; Manohar, B. M.; Rajaram, A.; Puvanakrishnan, R. Ecofriendly lime and sulfide free enzymatic dehairing of skins and hides using a bacterial alkaline protease Chemosphere 2008, 70, 1015-1024 10.1016/j.chemosphere.2007.09.036
    • (2008) Chemosphere , vol.70 , pp. 1015-1024
    • Sivasubramanian, S.1    Manohar, B.M.2    Rajaram, A.3    Puvanakrishnan, R.4
  • 2
    • 1642323710 scopus 로고    scopus 로고
    • Progress and recent trendsin biotechnological methods for leather processing
    • Thanikaivelan, P.; Rao, J. R.; Nair, B. U.; Ramasami, T. Progress and recent trendsin biotechnological methods for leather processing Trends Biotechnol. 2004, 22, 181-188 10.1016/j.tibtech.2004.02.008
    • (2004) Trends Biotechnol. , vol.22 , pp. 181-188
    • Thanikaivelan, P.1    Rao, J.R.2    Nair, B.U.3    Ramasami, T.4
  • 3
    • 84879843532 scopus 로고    scopus 로고
    • Enzyme mediated beam house operations of leather industry: A needed step towards greener technology
    • Saran, S.; Mahajan, R. V.; Kaushik, R.; Isar, J.; Saxena, R. K. Enzyme mediated beam house operations of leather industry: A needed step towards greener technology J. Cleaner Prod. 2013, 54, 315-322 10.1016/j.jclepro.2013.04.017
    • (2013) J. Cleaner Prod. , vol.54 , pp. 315-322
    • Saran, S.1    Mahajan, R.V.2    Kaushik, R.3    Isar, J.4    Saxena, R.K.5
  • 4
    • 0345829152 scopus 로고    scopus 로고
    • Green solution for tannery pollution: Effect of enzyme based lime free unhairing and fiber opening in combination with pickle-free chrome tanning
    • Saravanabhavan, S.; Aravindhan, R.; Thanikaivelan, P.; Rao, J. R.; Nair, B. U. Green solution for tannery pollution: effect of enzyme based lime free unhairing and fiber opening in combination with pickle-free chrome tanning Green Chem. 2003, 5, 707-714 10.1039/b305285k
    • (2003) Green Chem. , vol.5 , pp. 707-714
    • Saravanabhavan, S.1    Aravindhan, R.2    Thanikaivelan, P.3    Rao, J.R.4    Nair, B.U.5
  • 5
    • 84878937789 scopus 로고    scopus 로고
    • Environmentally friendly hide unhairing: Enzymatic hide processing for the replacement of sodium sulfide and deliming
    • Dettmer, A.; Cavalli, E.; Ayub, M. A. Z.; Gutterres, M. Environmentally friendly hide unhairing: enzymatic hide processing for the replacement of sodium sulfide and deliming J. Cleaner Prod. 2013, 47 (1) 11-18 10.1016/j.jclepro.2012.04.024
    • (2013) J. Cleaner Prod. , vol.47 , Issue.1 , pp. 11-18
    • Dettmer, A.1    Cavalli, E.2    Ayub, M.A.Z.3    Gutterres, M.4
  • 6
    • 12144286869 scopus 로고    scopus 로고
    • Effects of pH, light and temperature on (1 -> 3,1 -> 4)-beta-glucanase stability in wheat leaves
    • Walti, M.; Roulin, S.; Feller, U. Effects of pH, light and temperature on (1 -> 3,1 -> 4)-beta-glucanase stability in wheat leaves Plant Physiol. Biochem. 2002, 40, 363-371 10.1016/S0981-9428(02)01373-6
    • (2002) Plant Physiol. Biochem. , vol.40 , pp. 363-371
    • Walti, M.1    Roulin, S.2    Feller, U.3
  • 7
    • 79958043773 scopus 로고    scopus 로고
    • Facile, high efficiency immobilization of lipase enzyme on magnetic iron oxide nanoparticles via a biomimetic coating
    • Ren, Y.; Rivera, J. G.; He, L.; Kulkarni, H.; Lee, D. K.; Messersmith, P. B. Facile, high efficiency immobilization of lipase enzyme on magnetic iron oxide nanoparticles via a biomimetic coating BMC Biotechnol. 2011, 11, 63 10.1186/1472-6750-11-63
    • (2011) BMC Biotechnol. , vol.11 , pp. 63
    • Ren, Y.1    Rivera, J.G.2    He, L.3    Kulkarni, H.4    Lee, D.K.5    Messersmith, P.B.6
  • 9
    • 79959788687 scopus 로고    scopus 로고
    • 2nanorod composites: Towards high-activity photocatalytic materials
    • 2nanorod composites: Towards high-activity photocatalytic materials Appl. Catal., B 2011, 106 (1-2) 76-82 10.1016/j.apcatb.2011.05.007
    • (2011) Appl. Catal., B , vol.106 , Issue.12 , pp. 76-82
    • Liu, J.1    Liu, L.2    Bai, H.3    Wang, Y.4    Sun, D.D.5
  • 10
    • 33751413501 scopus 로고    scopus 로고
    • Facile synthesis of superparamagnetic magnetite nanoparticles in liquid polyols
    • Cai, W.; Wan, J. Facile synthesis of superparamagnetic magnetite nanoparticles in liquid polyols J. Colloid Interface Sci. 2007, 305, 366-370 10.1016/j.jcis.2006.10.023
    • (2007) J. Colloid Interface Sci. , vol.305 , pp. 366-370
    • Cai, W.1    Wan, J.2
  • 11
    • 84879814814 scopus 로고    scopus 로고
    • Immobilization of amylase on gum acacia stabilized magnetitenanoparticles, an easily recoverable and reusable support
    • Swarnalatha, V.; Rani, A. E.; Dhamodharan, R. Immobilization of amylase on gum acacia stabilized magnetitenanoparticles, an easily recoverable and reusable support J. Mol. Catal.B: Enzym. 2013, 96, 6-13
    • (2013) J. Mol. Catal.B: Enzym. , vol.96 , pp. 6-13
    • Swarnalatha, V.1    Rani, A.E.2    Dhamodharan, R.3
  • 12
    • 84939535249 scopus 로고    scopus 로고
    • Immobilization of Thermomyceslanuginosus lipase on ZnO nanoparticles: Mimicking the interfacial environment
    • Shah, E.; Mahapatra, P.; Bedekar, A. V.; Soni, H. P. Immobilization of Thermomyceslanuginosus lipase on ZnO nanoparticles: mimicking the interfacial environment RSC Adv. 2015, 5, 26291-26300 10.1039/C5RA02249E
    • (2015) RSC Adv. , vol.5 , pp. 26291-26300
    • Shah, E.1    Mahapatra, P.2    Bedekar, A.V.3    Soni, H.P.4
  • 13
    • 84902976306 scopus 로고    scopus 로고
    • Penicilliumexpansum lipase-coated magnetic Fe3O4-polymer hybrid hollow nanoparticles: A highly recoverable and magnetically separable catalyst for the synthesis of 1,3-dibutylurea
    • Liu, W.; Wang, W.; Liu, H.; Zhou, Y.; Zhang, H.; Zhou, X. Penicilliumexpansum lipase-coated magnetic Fe3O4-polymer hybrid hollow nanoparticles: A highly recoverable and magnetically separable catalyst for the synthesis of 1,3-dibutylurea RSC Adv. 2014, 4, 25983-25992 10.1039/c4ra04156a
    • (2014) RSC Adv. , vol.4 , pp. 25983-25992
    • Liu, W.1    Wang, W.2    Liu, H.3    Zhou, Y.4    Zhang, H.5    Zhou, X.6
  • 14
    • 9944253349 scopus 로고    scopus 로고
    • Glucose oxidase-magnetite nanoparticle bioconjugate for glucose sensing
    • Rossi, L. M.; Quach, A. D.; Rosenzweig, Z. Glucose oxidase-magnetite nanoparticle bioconjugate for glucose sensing Anal. Bioanal. Chem. 2004, 380, 606-613 10.1007/s00216-004-2770-3
    • (2004) Anal. Bioanal. Chem. , vol.380 , pp. 606-613
    • Rossi, L.M.1    Quach, A.D.2    Rosenzweig, Z.3
  • 15
    • 84872101098 scopus 로고    scopus 로고
    • Synthesis of Stable Magnetic Nanofluids of Different Particle Sizes
    • Muthukumaran, T.; Gnanaprakash, G.; Philip, J. Synthesis of Stable Magnetic Nanofluids of Different Particle Sizes J. Nanofluids 2012, 1, 85-92 10.1166/jon.2012.1006
    • (2012) J. Nanofluids , vol.1 , pp. 85-92
    • Muthukumaran, T.1    Gnanaprakash, G.2    Philip, J.3
  • 16
    • 84856245416 scopus 로고    scopus 로고
    • Facile Synthesis of PEG-Coated Magnetite (Fe3O4) Nanoparticles and Their Prevention of the Reduction of Cytochrome C
    • Mukhopadhyay, A.; Joshi, N.; Chattopadhyay, K.; De, G. Facile Synthesis of PEG-Coated Magnetite (Fe3O4) Nanoparticles and Their Prevention of the Reduction of Cytochrome C ACS Appl. Mater. Interfaces 2012, 4, 142-149 10.1021/am201166m
    • (2012) ACS Appl. Mater. Interfaces , vol.4 , pp. 142-149
    • Mukhopadhyay, A.1    Joshi, N.2    Chattopadhyay, K.3    De, G.4
  • 18
    • 85012738381 scopus 로고
    • The estimation of pepsin, trypsin, papain, and cathepsin with hemoglobin
    • Anson, M. L. The estimation of pepsin, trypsin, papain, and cathepsin with hemoglobin J. Gen. Physiol. 1938, 22 (1) 79-89 10.1085/jgp.22.1.79
    • (1938) J. Gen. Physiol. , vol.22 , Issue.1 , pp. 79-89
    • Anson, M.L.1
  • 19
    • 0001247393 scopus 로고
    • On tyrosine and tryptophane determinations in proteins
    • Folin, O.; Ciocalteu, V. On tyrosine and tryptophane determinations in proteins J. Biol. Chem. 1927, 73, 627-650
    • (1927) J. Biol. Chem. , vol.73 , pp. 627-650
    • Folin, O.1    Ciocalteu, V.2
  • 20
    • 33748037939 scopus 로고
    • Amylases, α and β
    • Bernfeld, P. Amylases, α and β Methods Enzymol. 1955, 1, 149-158 10.1016/0076-6879(55)01021-5
    • (1955) Methods Enzymol. , vol.1 , pp. 149-158
    • Bernfeld, P.1
  • 21
    • 84908260965 scopus 로고    scopus 로고
    • Cohesive system for enzymatic unhairing and fibre opening: An architecture towards eco-benign pretanning operation
    • Jayakumar, G. C.; Ganesh, S.; Palanivel, S.; Palanivel, M.; Jonnalagadda, R. R. Cohesive system for enzymatic unhairing and fibre opening: An architecture towards eco-benign pretanning operation J. Cleaner Prod. 2014, 83, 428-436 10.1016/j.jclepro.2014.07.039
    • (2014) J. Cleaner Prod. , vol.83 , pp. 428-436
    • Jayakumar, G.C.1    Ganesh, S.2    Palanivel, S.3    Palanivel, M.4    Jonnalagadda, R.R.5
  • 22
    • 84927558480 scopus 로고    scopus 로고
    • Ionic liquids: New age materials for eco-friendly leather processing
    • Jayakumar, G. C.; Mehta, A.; Rao, J. R.; Fathima, N. N. Ionic liquids: new age materials for eco-friendly leather processing RSC Adv. 2015, 5, 31998-32005 10.1039/C5RA02167G
    • (2015) RSC Adv. , vol.5 , pp. 31998-32005
    • Jayakumar, G.C.1    Mehta, A.2    Rao, J.R.3    Fathima, N.N.4
  • 23
    • 29744443793 scopus 로고    scopus 로고
    • Expression of glutamine synthetase and cell proliferation in human idiopathic epiretinal Membrane
    • Kase, S.; Saito, W.; Ohgami, K.; Yoshida, K.; Furudate, N.; Yokoi, M.; Saito, A.; Kase, M.; Ohno, S. Expression of glutamine synthetase and cell proliferation in human idiopathic epiretinal Membrane Br. J. Ophthalmol. 2006, 90 (1) 96-98 10.1136/bjo.2007.119404
    • (2006) Br. J. Ophthalmol. , vol.90 , Issue.1 , pp. 96-98
    • Kase, S.1    Saito, W.2    Ohgami, K.3    Yoshida, K.4    Furudate, N.5    Yokoi, M.6    Saito, A.7    Kase, M.8    Ohno, S.9
  • 24
    • 58349105162 scopus 로고    scopus 로고
    • Cleaner tanning practices for tannery pollution abatement: Role of enzymes in ecofriendly vegetable tanning
    • Kanth, S. V.; Venba, R.; Madhan, B.; Chandrababu, N. K.; Sadulla, S. Cleaner tanning practices for tannery pollution abatement: role of enzymes in ecofriendly vegetable tanning J. Cleaner Prod. 2009, 17, 507-515 10.1016/j.jclepro.2008.08.021
    • (2009) J. Cleaner Prod. , vol.17 , pp. 507-515
    • Kanth, S.V.1    Venba, R.2    Madhan, B.3    Chandrababu, N.K.4    Sadulla, S.5
  • 26
    • 0010064805 scopus 로고    scopus 로고
    • IUP 6, Measurement of tensile strength and percentage elongation
    • IUP 6, Measurement of tensile strength and percentage elongation. J. Soc. Leather Technol. Chem. 2000, 84, 317.
    • (2000) J. Soc. Leather Technol. Chem. , vol.84 , pp. 317
  • 27
    • 0010026549 scopus 로고    scopus 로고
    • IUP 8, Measurement of tear load-double edge tears
    • IUP 8, Measurement of tear load-double edge tears. J. Soc. Leather Technol. Chem. 2000, 84, 327.
    • (2000) J. Soc. Leather Technol. Chem. , vol.84 , pp. 327
  • 28
    • 0037075438 scopus 로고    scopus 로고
    • Poly(Vinyl Pyridine) as a Universal Surface Modifier for Immobilization of Nanoparticles
    • Malynych, S.; Luzinov, I.; Chumanov, G. Poly(Vinyl Pyridine) as a Universal Surface Modifier for Immobilization of Nanoparticles J. Phys. Chem. B 2002, 106, 1280-1285 10.1021/jp013236d
    • (2002) J. Phys. Chem. B , vol.106 , pp. 1280-1285
    • Malynych, S.1    Luzinov, I.2    Chumanov, G.3
  • 29
    • 15944400027 scopus 로고    scopus 로고
    • PVA stabilized gold nanoparticles by use of unexplored albeit conventional reducing agent. Mater
    • Khanna, P. K.; Gokhale, R.; Subbarao, V. V. V; Vishwanath, A. K.; Das, B. K.; Satyanarayana, C. V. V PVA stabilized gold nanoparticles by use of unexplored albeit conventional reducing agent. Mater Mater. Chem. Phys. 2005, 92, 229-233 10.1016/j.matchemphys.2005.01.016
    • (2005) Mater. Chem. Phys. , vol.92 , pp. 229-233
    • Khanna, P.K.1    Gokhale, R.2    Subbarao, V.V.V.3    Vishwanath, A.K.4    Das, B.K.5    Satyanarayana, C.V.V.6
  • 30
    • 35748934180 scopus 로고    scopus 로고
    • Controlled PEGylation of Monodisperse Fe3O4 Nanoparticles for Reduced Non-Specific Uptake by Macrophage Cells
    • Xie, J.; Xu, C.; Kohler, N.; Hou, Y.; Sun, S. Controlled PEGylation of Monodisperse Fe3O4 Nanoparticles For Reduced Non-Specific Uptake by Macrophage Cells Adv. Mater. 2007, 19, 3163-3166 10.1002/adma.200701975
    • (2007) Adv. Mater. , vol.19 , pp. 3163-3166
    • Xie, J.1    Xu, C.2    Kohler, N.3    Hou, Y.4    Sun, S.5
  • 31
    • 47249102447 scopus 로고    scopus 로고
    • Zeta potential measurement as a diagnostic tool in enzyme immobilisation
    • Schultz, N.; Metreveli, G.; Franzreb, M.; Frimmel, F. H.; Syldatk, C. Zeta potential measurement as a diagnostic tool in enzyme immobilisation Colloids Surf., B 2008, 66, 39-44 10.1016/j.colsurfb.2008.05.004
    • (2008) Colloids Surf., B , vol.66 , pp. 39-44
    • Schultz, N.1    Metreveli, G.2    Franzreb, M.3    Frimmel, F.H.4    Syldatk, C.5
  • 33
    • 58649089588 scopus 로고    scopus 로고
    • Ethyl isovalerate synthesis using Candida rugosa lipase immobilized on silica nanoparticles prepared in nonionic reverse micelles
    • Dandavate, V.; Keharia, H.; Madamwar, D. Ethyl isovalerate synthesis using Candida rugosa lipase immobilized on silica nanoparticles prepared in nonionic reverse micelles Process Biochem. 2009, 44, 349-352 10.1016/j.procbio.2008.11.001
    • (2009) Process Biochem. , vol.44 , pp. 349-352
    • Dandavate, V.1    Keharia, H.2    Madamwar, D.3
  • 34
    • 84872432741 scopus 로고    scopus 로고
    • Ferrofluid based on polyethylene glycol-coated iron oxide nanoparticles: Characterization and properties
    • García-Jimeno, S.; Estelrich, J. Ferrofluid based on polyethylene glycol-coated iron oxide nanoparticles: Characterization and properties Colloids Surf., A 2013, 420, 74-81 10.1016/j.colsurfa.2012.12.022
    • (2013) Colloids Surf., A , vol.420 , pp. 74-81
    • García-Jimeno, S.1    Estelrich, J.2
  • 35
    • 84905116471 scopus 로고    scopus 로고
    • Understanding the chemical free enzyme based cleaner unhairing process in leather manufacturing
    • Saravanan, P.; Renitha, T. S.; Gowthaman, M. K.; Kamini, N. R. Understanding the chemical free enzyme based cleaner unhairing process in leather manufacturing J. Cleaner Prod. 2014, 79, 258-264 10.1016/j.jclepro.2014.05.022
    • (2014) J. Cleaner Prod. , vol.79 , pp. 258-264
    • Saravanan, P.1    Renitha, T.S.2    Gowthaman, M.K.3    Kamini, N.R.4
  • 36
    • 0142073274 scopus 로고    scopus 로고
    • Catalytic Behaviors of Enzymes Attached to Nanoparticles: The Effect of Particle Mobility
    • Jia, H.; Zhu, G.; Wang, P. Catalytic Behaviors of Enzymes Attached to Nanoparticles: The Effect of Particle Mobility Biotechnol. Bioeng. 2003, 84, 406-414 10.1002/bit.10781
    • (2003) Biotechnol. Bioeng. , vol.84 , pp. 406-414
    • Jia, H.1    Zhu, G.2    Wang, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.