Candida rugosa lipase immobilization on various chemically modified Chromium terephthalate MIL-101

The paper seeks to immobilize Candida rugosa lipase (CRL) on Chromium terephthalate MIL-101 (MIL-101(Cr)) and its three chemically modified forms: amino MIL-101(Cr) (NH2-MIL), trichlorotriazine amino MIL-101(Cr) (TCT@NH2-MIL) and glutaraldehyde amino MIL-101(Cr) (Glu@NH2-MIL). The synthesis process...

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Published inJournal of molecular liquids Vol. 254; pp. 137 - 144
Main Authors Zare, Atefeh, Bordbar, Abdol-Khalegh, Jafarian, Faranak, Tangestaninejad, Shahram
Format Journal Article
LanguageEnglish
Published Elsevier B.V 15.03.2018
Subjects
Candida rugosa lipase (CRL)
Immobilization
Metal organic frameworks
MIL-101(Cr)
Stability
Immobilization
Stability
Candida rugosa lipase (CRL)
Metal organic frameworks
MIL-101(Cr)
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Abstract The paper seeks to immobilize Candida rugosa lipase (CRL) on Chromium terephthalate MIL-101 (MIL-101(Cr)) and its three chemically modified forms: amino MIL-101(Cr) (NH2-MIL), trichlorotriazine amino MIL-101(Cr) (TCT@NH2-MIL) and glutaraldehyde amino MIL-101(Cr) (Glu@NH2-MIL). The synthesis process of these metal organic frameworks, CRL immobilization and the morphology of supports were verified using FTIR, PXRD, BET and FE-SEM techniques. The enzyme loading and the specific activity at different initial concentration of lipase for all the supports were measured and the obtained results were compared. The highest specific activity at any given point in the common range of enzyme loading belongs to CRL@Glu@NH2-MIL. While all the immobilized CRLs show no significant drop in residual activity after pH stress, the thermal stability is just substantially improved for CRL@TCT@NH2-MIL and CRL@Glu@NH2-MIL. About 80–90% of the initial enzymatic activity retained after 35 days for all of the supports indicating a significant storage stability of the immobilized CRLs. [Display omitted] •The CRL was successfully immobilized on MIL-101(Cr) and its three chemically modified forms.•The highest specific activity at any given point in the common range of enzyme loading belongs to CRL@Glu@NH2-MIL.•An excellent pH stability was observed for immobilized CRL.•The improvement in thermal stability of immobilized CRLs was observed specially for CRL@Glu@NH2-MIL and CRL@TCT@ NH2-MIL.
AbstractList The paper seeks to immobilize Candida rugosa lipase (CRL) on Chromium terephthalate MIL-101 (MIL-101(Cr)) and its three chemically modified forms: amino MIL-101(Cr) (NH2-MIL), trichlorotriazine amino MIL-101(Cr) (TCT@NH2-MIL) and glutaraldehyde amino MIL-101(Cr) (Glu@NH2-MIL). The synthesis process of these metal organic frameworks, CRL immobilization and the morphology of supports were verified using FTIR, PXRD, BET and FE-SEM techniques. The enzyme loading and the specific activity at different initial concentration of lipase for all the supports were measured and the obtained results were compared. The highest specific activity at any given point in the common range of enzyme loading belongs to CRL@Glu@NH2-MIL. While all the immobilized CRLs show no significant drop in residual activity after pH stress, the thermal stability is just substantially improved for CRL@TCT@NH2-MIL and CRL@Glu@NH2-MIL. About 80–90% of the initial enzymatic activity retained after 35 days for all of the supports indicating a significant storage stability of the immobilized CRLs. [Display omitted] •The CRL was successfully immobilized on MIL-101(Cr) and its three chemically modified forms.•The highest specific activity at any given point in the common range of enzyme loading belongs to CRL@Glu@NH2-MIL.•An excellent pH stability was observed for immobilized CRL.•The improvement in thermal stability of immobilized CRLs was observed specially for CRL@Glu@NH2-MIL and CRL@TCT@ NH2-MIL.
Author Bordbar, Abdol-Khalegh
Jafarian, Faranak
Tangestaninejad, Shahram
Zare, Atefeh
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Cites_doi 10.1016/j.enzmictec.2017.08.008
10.1021/ja2038003
10.1039/C5RA24441B
10.2174/138920309789630534
10.1016/j.molcatb.2013.04.015
10.1016/j.biortech.2011.01.006
10.1039/c3cs35446f
10.1016/j.molcatb.2016.08.009
10.1039/C5CS00307E
10.1039/B711564B
10.1016/j.cej.2008.05.015
10.1002/pro.5560030111
10.1016/j.cej.2013.11.059
10.1016/j.ultsonch.2017.02.028
10.1002/chem.201405252
10.1007/s12010-009-8897-0
10.1023/A:1005668500716
10.1016/j.micromeso.2008.10.013
10.1039/b804680h
10.1039/C6RA10885G
10.1016/j.cej.2011.10.097
10.1039/C3CS60472A
10.1007/s11244-006-0025-6
10.1039/C6RA25396B
10.1021/bm025729+
10.1016/j.procbio.2015.07.014
10.1074/jbc.R800080200
10.1016/0003-2697(76)90527-3
10.1016/S0142-9612(03)00482-4
10.1039/c0cc03288c
10.1126/science.1116275
10.1021/acs.langmuir.5b03614
10.1016/j.fbp.2016.07.016
10.3390/catal6080115
10.1039/C5CY01181G
10.1021/bm400762h
10.1039/c3tb00257h
10.1039/C7CS00058H
10.1021/bm049688o
10.1039/c2ra20641b
10.1039/C6MH00312E
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Keywords Immobilization
Stability
Candida rugosa lipase (CRL)
Metal organic frameworks
MIL-101(Cr)
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References Adlercreutz (bb0020) 2013; 42
Grochulski, Li, Schrag, Cygler (bb0205) 1994; 3
Lykourinou, Chen, Wang, Meng, Hoang, Ming, Musselman, Ma (bb0005) 2011; 133
Liu, Yang, Chen, Lirio, Wu, Lin, Huang (bb0065) 2015; 21
Nadar, Rathod (bb0130) 2018; 108
Huang, Cheng (bb0060) 2008; 144
Raja, Liu, Huang, Lin (bb0120) 2015; 35
Silva, Vilela, Tome, Almeida Paz (bb0110) 2015; 44
Aghababaie, Beheshti, Razmjou, Bordbar (bb0030) 2017; 7269
Lian, Fang, Joseph, Wang, Li, Banerjee, Lollar, Wang, Zhou (bb0090) 2017; 46
Zhou, Zhou, Gao, Kong, Chen (bb0165) 2017; 7
Manrich, Komesu, Adriano, Tardioli (bb0220) 2010; 161
Rivero, Palomo (bb0010) 2016; 6
Shih, Lo, Yang, Singco, Cheng, Wu, Chang, Huang, Lin (bb0135) 2012; 77
Lin, Kong, Chen (bb0080) 2012; 2
Pisklak, Macias, Coutinho, Huang, Balkus (bb0115) 2006; 38
He, Chen (bb0095) 2014
Sohrabi, Rasouli, Torkzadeh (bb0170) 2014; 240
Foresti, Ferreira (bb0175) 2004; 5
Barbosa, Torres, Ortiz, Berenguer-Murcia, Rodrigues, Fernandez-Lafuente (bb0155) 2013; 14
Chiou, Wu (bb0070) 2004; 25
Aghababaie, Beheshti, Razmjou, Bordbar (bb0045) 2016; 100
Zhou, Chen, Yang (bb0185) 2009; 119
Rios, Pinheiro, dos Santos, Fonseca, Lima, de Mattos, Freire, da Silva, Rodríguez-Aguado, Gonçalves (bb0025) 2016; 133
Bansode, Rathod (bb0040) 2017; 38
Zhu, Xu (bb0100) 2014; 43
Akova, Ustun (bb0200) 2000; 22
Trivedi, Laurence, Siahaan (bb0195) 2009; 10
Jung, Kim, Kim, Kwon, Huh, Park (bb0125) 2011; 47
Pace, Grimsley, Scholtz (bb0190) 2009; 284
Palomo, Fuentes, Fernández-Lorente, Mateo, Guisan, Fernández-Lafuente (bb0230) 2003; 4
Peng, Zhu-Ping, Yong-Juan, Peng-Cheng, Ji-Jun (bb0225) 2013; 94
Yan, Yan, Liu, Hu, Wang (bb0180) 2011; 102
Wu, Hou, Ge (bb0075) 2015; 5
Esmaeilnejad-Ahranjani, Kazemeini, Singh, Arpanaei (bb0210) 2016; 32
Khan, Rathod (bb0035) 2015; 50
Gkaniatsou, Sicard, Ricoux, Mahy, Steunou, Serre (bb0085) 2017; 4
Wang, Zhao, Yu (bb0145) 2016; 0
Samui, Ray Chowdhuri, Mahto, Sahu (bb0215) 2016; 6
Hanefeld, Gardossi, Magner (bb0015) 2009; 38
Bradford (bb0160) 1976; 72
Amirkhani, Moghaddas, Jafarizadeh-Malmiri (bb0055) 2016; 6
Ferey (bb0150) 2005; 309
Czaja, Trukhan, Muller (bb0105) 2009; 38
Liu, Lo, Singco, Yang, Huang, Lin (bb0140) 2013; 1
Ranjbakhsh, Bordbar, Abbasi, Khosropour, Shams (bb0050) 2012; 179
Yan (10.1016/j.molliq.2018.01.097_bb0180) 2011; 102
Gkaniatsou (10.1016/j.molliq.2018.01.097_bb0085) 2017; 4
Trivedi (10.1016/j.molliq.2018.01.097_bb0195) 2009; 10
Raja (10.1016/j.molliq.2018.01.097_bb0120) 2015; 35
Nadar (10.1016/j.molliq.2018.01.097_bb0130) 2018; 108
Aghababaie (10.1016/j.molliq.2018.01.097_bb0045) 2016; 100
Aghababaie (10.1016/j.molliq.2018.01.097_bb0030) 2017; 7269
Zhu (10.1016/j.molliq.2018.01.097_bb0100) 2014; 43
Rivero (10.1016/j.molliq.2018.01.097_bb0010) 2016; 6
Bansode (10.1016/j.molliq.2018.01.097_bb0040) 2017; 38
Jung (10.1016/j.molliq.2018.01.097_bb0125) 2011; 47
Samui (10.1016/j.molliq.2018.01.097_bb0215) 2016; 6
Rios (10.1016/j.molliq.2018.01.097_bb0025) 2016; 133
Wang (10.1016/j.molliq.2018.01.097_bb0145) 2016; 0
Sohrabi (10.1016/j.molliq.2018.01.097_bb0170) 2014; 240
Silva (10.1016/j.molliq.2018.01.097_bb0110) 2015; 44
Amirkhani (10.1016/j.molliq.2018.01.097_bb0055) 2016; 6
Peng (10.1016/j.molliq.2018.01.097_bb0225) 2013; 94
He (10.1016/j.molliq.2018.01.097_bb0095) 2014
Zhou (10.1016/j.molliq.2018.01.097_bb0185) 2009; 119
Shih (10.1016/j.molliq.2018.01.097_bb0135) 2012; 77
Pisklak (10.1016/j.molliq.2018.01.097_bb0115) 2006; 38
Bradford (10.1016/j.molliq.2018.01.097_bb0160) 1976; 72
Zhou (10.1016/j.molliq.2018.01.097_bb0165) 2017; 7
Adlercreutz (10.1016/j.molliq.2018.01.097_bb0020) 2013; 42
Wu (10.1016/j.molliq.2018.01.097_bb0075) 2015; 5
Lin (10.1016/j.molliq.2018.01.097_bb0080) 2012; 2
Ferey (10.1016/j.molliq.2018.01.097_bb0150) 2005; 309
Pace (10.1016/j.molliq.2018.01.097_bb0190) 2009; 284
Esmaeilnejad-Ahranjani (10.1016/j.molliq.2018.01.097_bb0210) 2016; 32
Hanefeld (10.1016/j.molliq.2018.01.097_bb0015) 2009; 38
Liu (10.1016/j.molliq.2018.01.097_bb0065) 2015; 21
Lykourinou (10.1016/j.molliq.2018.01.097_bb0005) 2011; 133
Czaja (10.1016/j.molliq.2018.01.097_bb0105) 2009; 38
Liu (10.1016/j.molliq.2018.01.097_bb0140) 2013; 1
Chiou (10.1016/j.molliq.2018.01.097_bb0070) 2004; 25
Manrich (10.1016/j.molliq.2018.01.097_bb0220) 2010; 161
Barbosa (10.1016/j.molliq.2018.01.097_bb0155) 2013; 14
Grochulski (10.1016/j.molliq.2018.01.097_bb0205) 1994; 3
Foresti (10.1016/j.molliq.2018.01.097_bb0175) 2004; 5
Ranjbakhsh (10.1016/j.molliq.2018.01.097_bb0050) 2012; 179
Akova (10.1016/j.molliq.2018.01.097_bb0200) 2000; 22
Khan (10.1016/j.molliq.2018.01.097_bb0035) 2015; 50
Huang (10.1016/j.molliq.2018.01.097_bb0060) 2008; 144
Lian (10.1016/j.molliq.2018.01.097_bb0090) 2017; 46
Palomo (10.1016/j.molliq.2018.01.097_bb0230) 2003; 4
References_xml – volume: 35
  start-page: 332
  year: 2015
  end-page: 350
  ident: bb0120
  article-title: Immobilization of protein on nanoporous metal-organic framework materials, comments
  publication-title: Inorg. Chem.
  contributor:
    fullname: Lin
– volume: 10
  start-page: 614
  year: 2009
  end-page: 625
  ident: bb0195
  article-title: The role of thiols and disulfides on protein stability
  publication-title: Curr. Protein Pept. Sci.
  contributor:
    fullname: Siahaan
– volume: 144
  start-page: 103
  year: 2008
  end-page: 109
  ident: bb0060
  article-title: Immobilization of lipase on chemically modified bimodal ceramic foams for olive oil hydrolysis
  publication-title: Chem. Eng. J.
  contributor:
    fullname: Cheng
– volume: 32
  start-page: 3242
  year: 2016
  end-page: 3252
  ident: bb0210
  article-title: Study of molecular conformation and activity-related properties of lipase immobilized onto core-shell structured polyacrylic acid-coated magnetic silica nanocomposite particles
  publication-title: Langmuir
  contributor:
    fullname: Arpanaei
– volume: 7
  start-page: 3713
  year: 2017
  end-page: 3719
  ident: bb0165
  article-title: Facile synthesis of MOFs with uncoordinated carboxyl groups for selective CO
  publication-title: RSC Adv.
  contributor:
    fullname: Chen
– volume: 94
  start-page: 69
  year: 2013
  end-page: 76
  ident: bb0225
  article-title: Effect of support surface chemistry on lipase adsorption and activity
  publication-title: J. Mol. Catal. B Enzym.
  contributor:
    fullname: Ji-Jun
– volume: 50
  start-page: 1793
  year: 2015
  end-page: 1806
  ident: bb0035
  article-title: Enzyme catalyzed synthesis of cosmetic esters and its intensification: a review
  publication-title: Process Biochem.
  contributor:
    fullname: Rathod
– volume: 179
  start-page: 272
  year: 2012
  end-page: 276
  ident: bb0050
  article-title: Enhancement of stability and catalytic activity of immobilized lipase on silica-coated modified magnetite nanoparticles
  publication-title: Chem. Eng. J.
  contributor:
    fullname: Shams
– volume: 14
  start-page: 2433
  year: 2013
  end-page: 2462
  ident: bb0155
  article-title: Heterofunctional supports in enzyme immobilization: from traditional immobilization protocols to opportunities in tuning enzyme properties
  publication-title: Biomacromolecules
  contributor:
    fullname: Fernandez-Lafuente
– volume: 77
  start-page: 982
  year: 2012
  end-page: 986
  ident: bb0135
  article-title: Trypsin-immobilized metal-organic framework as a biocatalyst in proteomics analysis
  publication-title: Chem. Aust.
  contributor:
    fullname: Lin
– volume: 119
  start-page: 223
  year: 2009
  end-page: 229
  ident: bb0185
  article-title: Comparative studies on catalytic properties of immobilized
  publication-title: Microporous Mesoporous Mater.
  contributor:
    fullname: Yang
– volume: 3
  start-page: 82
  year: 1994
  end-page: 91
  ident: bb0205
  article-title: Two conformational states of
  publication-title: Protein Sci.
  contributor:
    fullname: Cygler
– volume: 4
  start-page: 1
  year: 2003
  end-page: 6
  ident: bb0230
  article-title: General trend of lipase to self-assemble giving bimolecular aggregates greatly modifies the enzyme functionality
  publication-title: Biomacromolecules
  contributor:
    fullname: Fernández-Lafuente
– volume: 108
  start-page: 11
  year: 2018
  end-page: 20
  ident: bb0130
  article-title: Encapsulation of lipase within metal-organic framework (MOF) with enhanced activity intensified under ultrasound
  publication-title: Enzym. Microb. Technol.
  contributor:
    fullname: Rathod
– volume: 6
  start-page: 115
  year: 2016
  ident: bb0010
  article-title: Covalent immobilization of
  publication-title: Catalysts.
  contributor:
    fullname: Palomo
– volume: 100
  start-page: 351
  year: 2016
  end-page: 360
  ident: bb0045
  article-title: Covalent immobilization of
  publication-title: Food Bioprod. Process.
  contributor:
    fullname: Bordbar
– volume: 38
  start-page: 453
  year: 2009
  end-page: 468
  ident: bb0015
  article-title: Understanding enzyme immobilisation
  publication-title: Chem. Soc. Rev.
  contributor:
    fullname: Magner
– volume: 5
  start-page: 2366
  year: 2004
  end-page: 2375
  ident: bb0175
  article-title: Computational approach to solvent-free synthesis of ethyl oleate using
  publication-title: Biomacromolecules
  contributor:
    fullname: Ferreira
– volume: 42
  start-page: 6406
  year: 2013
  end-page: 6436
  ident: bb0020
  article-title: Immobilisation and application of lipases in organic media
  publication-title: Chem. Soc. Rev.
  contributor:
    fullname: Adlercreutz
– volume: 46
  start-page: 3386
  year: 2017
  end-page: 3401
  ident: bb0090
  article-title: Enzyme–MOF (metal–organic framework) composites
  publication-title: Chem. Soc. Rev.
  contributor:
    fullname: Zhou
– volume: 43
  start-page: 5648-5512
  year: 2014
  ident: bb0100
  article-title: Metal-organic framework composites
  publication-title: Chem. Soc. Rev.
  contributor:
    fullname: Xu
– volume: 38
  start-page: 503
  year: 2017
  end-page: 529
  ident: bb0040
  article-title: An investigation of lipase catalysed sonochemical synthesis: a review
  publication-title: Ultrason. Sonochem.
  contributor:
    fullname: Rathod
– volume: 38
  start-page: 269
  year: 2006
  end-page: 278
  ident: bb0115
  article-title: Hybrid materials for immobilization of MP-11 catalyst
  publication-title: Top. Catal.
  contributor:
    fullname: Balkus
– volume: 21
  start-page: 115
  year: 2015
  end-page: 119
  ident: bb0065
  article-title: Lipase-supported metal-organic framework bioreactor catalyzes warfarin synthesis
  publication-title: Chemistry
  contributor:
    fullname: Huang
– volume: 47
  start-page: 2904
  year: 2011
  end-page: 2906
  ident: bb0125
  article-title: Bio-functionalization of metal-organic frameworks by covalent protein conjugation
  publication-title: Chem. Commun. (Camb.)
  contributor:
    fullname: Park
– volume: 6
  start-page: 12676
  year: 2016
  end-page: 12687
  ident: bb0055
  article-title: lipase immobilization on magnetic silica aerogel nanodispersion
  publication-title: RSC Adv.
  contributor:
    fullname: Jafarizadeh-Malmiri
– volume: 7269
  start-page: 1
  year: 2017
  end-page: 7
  ident: bb0030
  article-title: Enzymatic biodiesel production from crude
  publication-title: Biofuels.
  contributor:
    fullname: Bordbar
– volume: 4
  start-page: 55
  year: 2017
  end-page: 63
  ident: bb0085
  article-title: Metal–organic frameworks: a novel host platform for enzymatic catalysis and detection
  publication-title: Mater. Horiz.
  contributor:
    fullname: Serre
– volume: 102
  start-page: 4755
  year: 2011
  end-page: 4758
  ident: bb0180
  article-title: Preparation of cross-linked lipase-coated micro-crystals for biodiesel production from waste cooking oil
  publication-title: Bioresour. Technol.
  contributor:
    fullname: Wang
– volume: 5
  start-page: 5077
  year: 2015
  end-page: 5085
  ident: bb0075
  article-title: Metal–organic frameworks and inorganic nanoflowers: a type of emerging inorganic crystal nanocarrier for enzyme immobilization
  publication-title: Catal. Sci. Technol.
  contributor:
    fullname: Ge
– volume: 2
  start-page: 6417
  year: 2012
  ident: bb0080
  article-title: Direct synthesis of amine-functionalized MIL-101(Cr) nanoparticles and application for CO
  publication-title: RSC Adv.
  contributor:
    fullname: Chen
– volume: 44
  start-page: 6774
  year: 2015
  end-page: 6803
  ident: bb0110
  article-title: Multifunctional metal-organic frameworks: from academia to industrial applications
  publication-title: Chem. Soc. Rev.
  contributor:
    fullname: Almeida Paz
– volume: 309
  start-page: 2040
  year: 2005
  end-page: 2042
  ident: bb0150
  article-title: A chromium terephthalate-based solid with unusually large pore volumes and surface area
  publication-title: Science
  contributor:
    fullname: Ferey
– volume: 240
  start-page: 426
  year: 2014
  end-page: 433
  ident: bb0170
  article-title: Enhanced stability and catalytic activity of immobilized α-amylase on modified Fe
  publication-title: Chem. Eng. J.
  contributor:
    fullname: Torkzadeh
– volume: 0
  start-page: 1
  year: 2016
  end-page: 7
  ident: bb0145
  article-title: Facile preparation of Fe
  publication-title: Chem. Eng.
  contributor:
    fullname: Yu
– start-page: 1
  year: 2014
  end-page: 23
  ident: bb0095
  article-title: Mesoporous metal-organic frameworks
  publication-title: Encycl. Inorg. Bioinorg. Chem.
  contributor:
    fullname: Chen
– volume: 1
  start-page: 928
  year: 2013
  end-page: 932
  ident: bb0140
  article-title: Novel trypsin–FITC@ MOF bioreactor efficiently catalyzes protein digestion
  publication-title: J. Mater. Chem. B
  contributor:
    fullname: Lin
– volume: 6
  start-page: 66385
  year: 2016
  end-page: 66393
  ident: bb0215
  article-title: Fabrication of magnetic nanoparticles embedded NH
  publication-title: RSC Adv.
  contributor:
    fullname: Sahu
– volume: 22
  start-page: 355
  year: 2000
  end-page: 359
  ident: bb0200
  article-title: Activity and adsorption of lipase from
  publication-title: Biotechnol. Lett.
  contributor:
    fullname: Ustun
– volume: 161
  start-page: 455
  year: 2010
  end-page: 467
  ident: bb0220
  article-title: Immobilization and stabilization of xylanase by multipoint covalent attachment on agarose and on chitosan supports
  publication-title: Appl. Biochem. Biotechnol.
  contributor:
    fullname: Tardioli
– volume: 133
  start-page: 246
  year: 2016
  end-page: 258
  ident: bb0025
  article-title: Strategies of covalent immobilization of a recombinant
  publication-title: J. Mol. Catal. B Enzym.
  contributor:
    fullname: Gonçalves
– volume: 133
  start-page: 10382
  year: 2011
  end-page: 10385
  ident: bb0005
  article-title: Immobilization of MP-11 into a mesoporous metal-organic framework, MP-11@mesoMOF: a new platform for enzymatic catalysis
  publication-title: J. Am. Chem. Soc.
  contributor:
    fullname: Ma
– volume: 284
  start-page: 13285
  year: 2009
  end-page: 13289
  ident: bb0190
  article-title: Protein ionizable groups: pK values and their contribution to protein stability and solubility
  publication-title: J. Biol. Chem.
  contributor:
    fullname: Scholtz
– volume: 72
  start-page: 248
  year: 1976
  end-page: 254
  ident: bb0160
  article-title: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  publication-title: Anal. Biochem.
  contributor:
    fullname: Bradford
– volume: 38
  start-page: 1284
  year: 2009
  end-page: 1293
  ident: bb0105
  article-title: Industrial applications of metal-organic frameworks
  publication-title: Chem. Soc. Rev.
  contributor:
    fullname: Muller
– volume: 25
  start-page: 197
  year: 2004
  end-page: 204
  ident: bb0070
  article-title: Immobilization of
  publication-title: Biomaterials
  contributor:
    fullname: Wu
– volume: 108
  start-page: 11
  year: 2018
  ident: 10.1016/j.molliq.2018.01.097_bb0130
  article-title: Encapsulation of lipase within metal-organic framework (MOF) with enhanced activity intensified under ultrasound
  publication-title: Enzym. Microb. Technol.
  doi: 10.1016/j.enzmictec.2017.08.008
  contributor:
    fullname: Nadar
– start-page: 1
  year: 2014
  ident: 10.1016/j.molliq.2018.01.097_bb0095
  article-title: Mesoporous metal-organic frameworks
  publication-title: Encycl. Inorg. Bioinorg. Chem.
  contributor:
    fullname: He
– volume: 133
  start-page: 10382
  year: 2011
  ident: 10.1016/j.molliq.2018.01.097_bb0005
  article-title: Immobilization of MP-11 into a mesoporous metal-organic framework, MP-11@mesoMOF: a new platform for enzymatic catalysis
  publication-title: J. Am. Chem. Soc.
  doi: 10.1021/ja2038003
  contributor:
    fullname: Lykourinou
– volume: 6
  start-page: 12676
  year: 2016
  ident: 10.1016/j.molliq.2018.01.097_bb0055
  article-title: Candida rugosa lipase immobilization on magnetic silica aerogel nanodispersion
  publication-title: RSC Adv.
  doi: 10.1039/C5RA24441B
  contributor:
    fullname: Amirkhani
– volume: 10
  start-page: 614
  year: 2009
  ident: 10.1016/j.molliq.2018.01.097_bb0195
  article-title: The role of thiols and disulfides on protein stability
  publication-title: Curr. Protein Pept. Sci.
  doi: 10.2174/138920309789630534
  contributor:
    fullname: Trivedi
– volume: 94
  start-page: 69
  year: 2013
  ident: 10.1016/j.molliq.2018.01.097_bb0225
  article-title: Effect of support surface chemistry on lipase adsorption and activity
  publication-title: J. Mol. Catal. B Enzym.
  doi: 10.1016/j.molcatb.2013.04.015
  contributor:
    fullname: Peng
– volume: 102
  start-page: 4755
  year: 2011
  ident: 10.1016/j.molliq.2018.01.097_bb0180
  article-title: Preparation of cross-linked lipase-coated micro-crystals for biodiesel production from waste cooking oil
  publication-title: Bioresour. Technol.
  doi: 10.1016/j.biortech.2011.01.006
  contributor:
    fullname: Yan
– volume: 42
  start-page: 6406
  year: 2013
  ident: 10.1016/j.molliq.2018.01.097_bb0020
  article-title: Immobilisation and application of lipases in organic media
  publication-title: Chem. Soc. Rev.
  doi: 10.1039/c3cs35446f
  contributor:
    fullname: Adlercreutz
– volume: 133
  start-page: 246
  year: 2016
  ident: 10.1016/j.molliq.2018.01.097_bb0025
  article-title: Strategies of covalent immobilization of a recombinant Candida antarctica lipase B on pore-expanded SBA-15 and its application in the kinetic resolution of (R,S)-phenylethyl acetate
  publication-title: J. Mol. Catal. B Enzym.
  doi: 10.1016/j.molcatb.2016.08.009
  contributor:
    fullname: Rios
– volume: 44
  start-page: 6774
  year: 2015
  ident: 10.1016/j.molliq.2018.01.097_bb0110
  article-title: Multifunctional metal-organic frameworks: from academia to industrial applications
  publication-title: Chem. Soc. Rev.
  doi: 10.1039/C5CS00307E
  contributor:
    fullname: Silva
– volume: 38
  start-page: 453
  year: 2009
  ident: 10.1016/j.molliq.2018.01.097_bb0015
  article-title: Understanding enzyme immobilisation
  publication-title: Chem. Soc. Rev.
  doi: 10.1039/B711564B
  contributor:
    fullname: Hanefeld
– volume: 144
  start-page: 103
  year: 2008
  ident: 10.1016/j.molliq.2018.01.097_bb0060
  article-title: Immobilization of lipase on chemically modified bimodal ceramic foams for olive oil hydrolysis
  publication-title: Chem. Eng. J.
  doi: 10.1016/j.cej.2008.05.015
  contributor:
    fullname: Huang
– volume: 3
  start-page: 82
  year: 1994
  ident: 10.1016/j.molliq.2018.01.097_bb0205
  article-title: Two conformational states of Candida rugosa lipase
  publication-title: Protein Sci.
  doi: 10.1002/pro.5560030111
  contributor:
    fullname: Grochulski
– volume: 240
  start-page: 426
  year: 2014
  ident: 10.1016/j.molliq.2018.01.097_bb0170
  article-title: Enhanced stability and catalytic activity of immobilized α-amylase on modified Fe3O4 nanoparticles
  publication-title: Chem. Eng. J.
  doi: 10.1016/j.cej.2013.11.059
  contributor:
    fullname: Sohrabi
– volume: 38
  start-page: 503
  year: 2017
  ident: 10.1016/j.molliq.2018.01.097_bb0040
  article-title: An investigation of lipase catalysed sonochemical synthesis: a review
  publication-title: Ultrason. Sonochem.
  doi: 10.1016/j.ultsonch.2017.02.028
  contributor:
    fullname: Bansode
– volume: 21
  start-page: 115
  year: 2015
  ident: 10.1016/j.molliq.2018.01.097_bb0065
  article-title: Lipase-supported metal-organic framework bioreactor catalyzes warfarin synthesis
  publication-title: Chemistry
  doi: 10.1002/chem.201405252
  contributor:
    fullname: Liu
– volume: 77
  start-page: 982
  year: 2012
  ident: 10.1016/j.molliq.2018.01.097_bb0135
  article-title: Trypsin-immobilized metal-organic framework as a biocatalyst in proteomics analysis
  publication-title: Chem. Aust.
  contributor:
    fullname: Shih
– volume: 161
  start-page: 455
  year: 2010
  ident: 10.1016/j.molliq.2018.01.097_bb0220
  article-title: Immobilization and stabilization of xylanase by multipoint covalent attachment on agarose and on chitosan supports
  publication-title: Appl. Biochem. Biotechnol.
  doi: 10.1007/s12010-009-8897-0
  contributor:
    fullname: Manrich
– volume: 35
  start-page: 332
  year: 2015
  ident: 10.1016/j.molliq.2018.01.097_bb0120
  article-title: Immobilization of protein on nanoporous metal-organic framework materials, comments
  publication-title: Inorg. Chem.
  contributor:
    fullname: Raja
– volume: 22
  start-page: 355
  year: 2000
  ident: 10.1016/j.molliq.2018.01.097_bb0200
  article-title: Activity and adsorption of lipase from Nigella sativa seeds on Celite at different pH values
  publication-title: Biotechnol. Lett.
  doi: 10.1023/A:1005668500716
  contributor:
    fullname: Akova
– volume: 119
  start-page: 223
  year: 2009
  ident: 10.1016/j.molliq.2018.01.097_bb0185
  article-title: Comparative studies on catalytic properties of immobilized Candida rugosa lipase in ordered mesoporous rod-like silica and vesicle-like silica
  publication-title: Microporous Mesoporous Mater.
  doi: 10.1016/j.micromeso.2008.10.013
  contributor:
    fullname: Zhou
– volume: 38
  start-page: 1284
  year: 2009
  ident: 10.1016/j.molliq.2018.01.097_bb0105
  article-title: Industrial applications of metal-organic frameworks
  publication-title: Chem. Soc. Rev.
  doi: 10.1039/b804680h
  contributor:
    fullname: Czaja
– volume: 6
  start-page: 66385
  year: 2016
  ident: 10.1016/j.molliq.2018.01.097_bb0215
  article-title: Fabrication of magnetic nanoparticles embedded NH2-MIL-88B MOFs hybrid for highly efficient covalent immobilization of lipase
  publication-title: RSC Adv.
  doi: 10.1039/C6RA10885G
  contributor:
    fullname: Samui
– volume: 7269
  start-page: 1
  year: 2017
  ident: 10.1016/j.molliq.2018.01.097_bb0030
  article-title: Enzymatic biodiesel production from crude Eruca sativa oil using Candida rugosa lipase in a solvent-free system using response surface methodology
  publication-title: Biofuels.
  contributor:
    fullname: Aghababaie
– volume: 179
  start-page: 272
  year: 2012
  ident: 10.1016/j.molliq.2018.01.097_bb0050
  article-title: Enhancement of stability and catalytic activity of immobilized lipase on silica-coated modified magnetite nanoparticles
  publication-title: Chem. Eng. J.
  doi: 10.1016/j.cej.2011.10.097
  contributor:
    fullname: Ranjbakhsh
– volume: 43
  start-page: 5648-5512
  year: 2014
  ident: 10.1016/j.molliq.2018.01.097_bb0100
  article-title: Metal-organic framework composites
  publication-title: Chem. Soc. Rev.
  doi: 10.1039/C3CS60472A
  contributor:
    fullname: Zhu
– volume: 38
  start-page: 269
  year: 2006
  ident: 10.1016/j.molliq.2018.01.097_bb0115
  article-title: Hybrid materials for immobilization of MP-11 catalyst
  publication-title: Top. Catal.
  doi: 10.1007/s11244-006-0025-6
  contributor:
    fullname: Pisklak
– volume: 7
  start-page: 3713
  year: 2017
  ident: 10.1016/j.molliq.2018.01.097_bb0165
  article-title: Facile synthesis of MOFs with uncoordinated carboxyl groups for selective CO2 capture via postsynthetic covalent modification
  publication-title: RSC Adv.
  doi: 10.1039/C6RA25396B
  contributor:
    fullname: Zhou
– volume: 0
  start-page: 1
  year: 2016
  ident: 10.1016/j.molliq.2018.01.097_bb0145
  article-title: Facile preparation of Fe3O4@MOF core-shell microspheres for lipase immobilization, J. Taiwan Inst
  publication-title: Chem. Eng.
  contributor:
    fullname: Wang
– volume: 4
  start-page: 1
  year: 2003
  ident: 10.1016/j.molliq.2018.01.097_bb0230
  article-title: General trend of lipase to self-assemble giving bimolecular aggregates greatly modifies the enzyme functionality
  publication-title: Biomacromolecules
  doi: 10.1021/bm025729+
  contributor:
    fullname: Palomo
– volume: 50
  start-page: 1793
  year: 2015
  ident: 10.1016/j.molliq.2018.01.097_bb0035
  article-title: Enzyme catalyzed synthesis of cosmetic esters and its intensification: a review
  publication-title: Process Biochem.
  doi: 10.1016/j.procbio.2015.07.014
  contributor:
    fullname: Khan
– volume: 284
  start-page: 13285
  year: 2009
  ident: 10.1016/j.molliq.2018.01.097_bb0190
  article-title: Protein ionizable groups: pK values and their contribution to protein stability and solubility
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.R800080200
  contributor:
    fullname: Pace
– volume: 72
  start-page: 248
  year: 1976
  ident: 10.1016/j.molliq.2018.01.097_bb0160
  article-title: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  publication-title: Anal. Biochem.
  doi: 10.1016/0003-2697(76)90527-3
  contributor:
    fullname: Bradford
– volume: 25
  start-page: 197
  year: 2004
  ident: 10.1016/j.molliq.2018.01.097_bb0070
  article-title: Immobilization of Candida rugosa lipase on chitosan with activation of the hydroxyl groups
  publication-title: Biomaterials
  doi: 10.1016/S0142-9612(03)00482-4
  contributor:
    fullname: Chiou
– volume: 47
  start-page: 2904
  year: 2011
  ident: 10.1016/j.molliq.2018.01.097_bb0125
  article-title: Bio-functionalization of metal-organic frameworks by covalent protein conjugation
  publication-title: Chem. Commun. (Camb.)
  doi: 10.1039/c0cc03288c
  contributor:
    fullname: Jung
– volume: 309
  start-page: 2040
  year: 2005
  ident: 10.1016/j.molliq.2018.01.097_bb0150
  article-title: A chromium terephthalate-based solid with unusually large pore volumes and surface area
  publication-title: Science
  doi: 10.1126/science.1116275
  contributor:
    fullname: Ferey
– volume: 32
  start-page: 3242
  year: 2016
  ident: 10.1016/j.molliq.2018.01.097_bb0210
  article-title: Study of molecular conformation and activity-related properties of lipase immobilized onto core-shell structured polyacrylic acid-coated magnetic silica nanocomposite particles
  publication-title: Langmuir
  doi: 10.1021/acs.langmuir.5b03614
  contributor:
    fullname: Esmaeilnejad-Ahranjani
– volume: 100
  start-page: 351
  year: 2016
  ident: 10.1016/j.molliq.2018.01.097_bb0045
  article-title: Covalent immobilization of Candida rugosa lipase on a novel functionalized Fe3O4@SiO2 dip-coated nanocomposite membrane
  publication-title: Food Bioprod. Process.
  doi: 10.1016/j.fbp.2016.07.016
  contributor:
    fullname: Aghababaie
– volume: 6
  start-page: 115
  year: 2016
  ident: 10.1016/j.molliq.2018.01.097_bb0010
  article-title: Covalent immobilization of Candida rugosa lipase at alkaline pH and their application in the regioselective deprotection of per-O-acetylated thymidine
  publication-title: Catalysts.
  doi: 10.3390/catal6080115
  contributor:
    fullname: Rivero
– volume: 5
  start-page: 5077
  year: 2015
  ident: 10.1016/j.molliq.2018.01.097_bb0075
  article-title: Metal–organic frameworks and inorganic nanoflowers: a type of emerging inorganic crystal nanocarrier for enzyme immobilization
  publication-title: Catal. Sci. Technol.
  doi: 10.1039/C5CY01181G
  contributor:
    fullname: Wu
– volume: 14
  start-page: 2433
  year: 2013
  ident: 10.1016/j.molliq.2018.01.097_bb0155
  article-title: Heterofunctional supports in enzyme immobilization: from traditional immobilization protocols to opportunities in tuning enzyme properties
  publication-title: Biomacromolecules
  doi: 10.1021/bm400762h
  contributor:
    fullname: Barbosa
– volume: 1
  start-page: 928
  year: 2013
  ident: 10.1016/j.molliq.2018.01.097_bb0140
  article-title: Novel trypsin–FITC@ MOF bioreactor efficiently catalyzes protein digestion
  publication-title: J. Mater. Chem. B
  doi: 10.1039/c3tb00257h
  contributor:
    fullname: Liu
– volume: 46
  start-page: 3386
  year: 2017
  ident: 10.1016/j.molliq.2018.01.097_bb0090
  article-title: Enzyme–MOF (metal–organic framework) composites
  publication-title: Chem. Soc. Rev.
  doi: 10.1039/C7CS00058H
  contributor:
    fullname: Lian
– volume: 5
  start-page: 2366
  year: 2004
  ident: 10.1016/j.molliq.2018.01.097_bb0175
  article-title: Computational approach to solvent-free synthesis of ethyl oleate using Candida rugosa and Candida antarctica B lipases. I. Interfacial activation and substrate (ethanol, oleic acid) adsorption
  publication-title: Biomacromolecules
  doi: 10.1021/bm049688o
  contributor:
    fullname: Foresti
– volume: 2
  start-page: 6417
  year: 2012
  ident: 10.1016/j.molliq.2018.01.097_bb0080
  article-title: Direct synthesis of amine-functionalized MIL-101(Cr) nanoparticles and application for CO2 capture
  publication-title: RSC Adv.
  doi: 10.1039/c2ra20641b
  contributor:
    fullname: Lin
– volume: 4
  start-page: 55
  year: 2017
  ident: 10.1016/j.molliq.2018.01.097_bb0085
  article-title: Metal–organic frameworks: a novel host platform for enzymatic catalysis and detection
  publication-title: Mater. Horiz.
  doi: 10.1039/C6MH00312E
  contributor:
    fullname: Gkaniatsou
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Snippet The paper seeks to immobilize Candida rugosa lipase (CRL) on Chromium terephthalate MIL-101 (MIL-101(Cr)) and its three chemically modified forms: amino...
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elsevier
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StartPage 137
SubjectTerms Candida rugosa lipase (CRL)
Immobilization
Metal organic frameworks
MIL-101(Cr)
Stability
Title Candida rugosa lipase immobilization on various chemically modified Chromium terephthalate MIL-101
URI https://dx.doi.org/10.1016/j.molliq.2018.01.097
Volume 254
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