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Volumn 91, Issue 1, 2016, Pages 59-64

Effect of modification of citraconic anhydrides on catalytic activity and thermostability of enzymes

Author keywords

Chemically modified enzyme; Enzymatic reaction; Lipase; Thermostability; chymotrypsin

Indexed keywords

AMINO ACIDS; CATALYST ACTIVITY; ENZYMES; LIPASES; STABILITY;

EID: 84954244318     PISSN: 02682575     EISSN: 10974660     Source Type: Journal    
DOI: 10.1002/jctb.4556     Document Type: Article
Times cited : (9)

References (31)
  • 1
    • 11044221115 scopus 로고    scopus 로고
    • Strategies for improving enzymes for efficient biocatalysis
    • Adamczak M and Krishna SH, Strategies for improving enzymes for efficient biocatalysis. Food Technol Biotechnol 42:251-264 (2004).
    • (2004) Food Technol Biotechnol , vol.42 , pp. 251-264
    • Adamczak, M.1    Krishna, S.H.2
  • 2
    • 1642489328 scopus 로고    scopus 로고
    • Enzyme stabilization-recent experimental progress
    • Ó'Fágáin C, Enzyme stabilization-recent experimental progress. Enzyme Microb Technol 33:137-149 (2003).
    • (2003) Enzyme Microb Technol , vol.33 , pp. 137-149
    • Ó'Fágáin, C.1
  • 3
    • 80051787511 scopus 로고    scopus 로고
    • Coupling chemical modification and immobilization to improve the catalytic performance of enzymes
    • Rodrigues RC, Berenguer-Murcia Á and Fernandez-Laufuente R, Coupling chemical modification and immobilization to improve the catalytic performance of enzymes. Adv Syn Catal 353:2216-2238 (2011).
    • (2011) Adv Syn Catal , vol.353 , pp. 2216-2238
    • Rodrigues, R.C.1    Berenguer-Murcia, A.2    Fernandez-Laufuente, R.3
  • 4
    • 79953318981 scopus 로고    scopus 로고
    • Chemical modification in the creation of novel biocatalysis
    • Díaz-Rodríguez A and Davies BG, Chemical modification in the creation of novel biocatalysis. Curr Opin Chem Biol 15:211-219 (2011).
    • (2011) Curr Opin Chem Biol , vol.15 , pp. 211-219
    • Díaz-Rodríguez, A.1    Davies, B.G.2
  • 5
    • 84856622930 scopus 로고    scopus 로고
    • Horseradish peroxidase: modulation of properties by chemical modification of protein and heme
    • Zakharova GS, Uporov IV and Tishkov VI, Horseradish peroxidase: modulation of properties by chemical modification of protein and heme. Biochemistry (Moscow) 76:1391-1401 (2011).
    • (2011) Biochemistry (Moscow) , vol.76 , pp. 1391-1401
    • Zakharova, G.S.1    Uporov, I.V.2    Tishkov, V.I.3
  • 7
    • 13544272805 scopus 로고    scopus 로고
    • Chemical modification of lysine residues in Bacillus licheniformis a-amylase: conversion of an Endo- to an Exo-type enzyme
    • Habibi AE, Khajeh K and Nemat-Gorgani M, Chemical modification of lysine residues in Bacillus licheniformis a-amylase: conversion of an Endo- to an Exo-type enzyme. J Biochem Mol Biol 37:642-647 (2004).
    • (2004) J Biochem Mol Biol , vol.37 , pp. 642-647
    • Habibi, A.E.1    Khajeh, K.2    Nemat-Gorgani, M.3
  • 8
    • 0037164183 scopus 로고    scopus 로고
    • Increased thermostability and phenol removal efficiency by chemical modified horseradish peroxidase
    • Liu JZ, Song HY, Weng LP and Ji LN, Increased thermostability and phenol removal efficiency by chemical modified horseradish peroxidase. J Mol Catal B: Enz 18:225-232 (2002).
    • (2002) J Mol Catal B: Enz , vol.18 , pp. 225-232
    • Liu, J.Z.1    Song, H.Y.2    Weng, L.P.3    Ji, L.N.4
  • 9
    • 0037375304 scopus 로고    scopus 로고
    • Treatment of aqueous chlorophenol by phthalic anhydride-modified horseradish peroxidase
    • Song HY, Liu JZ, Xiong YH, Weng LP and Ji LN, Treatment of aqueous chlorophenol by phthalic anhydride-modified horseradish peroxidase. J Mol Catal B: Enz 22:37-44 (2003).
    • (2003) J Mol Catal B: Enz , vol.22 , pp. 37-44
    • Song, H.Y.1    Liu, J.Z.2    Xiong, Y.H.3    Weng, L.P.4    Ji, L.N.5
  • 10
    • 0347297131 scopus 로고    scopus 로고
    • Effects of phthalic anhydride modification on horseradish peroxidase stability and activity
    • O'Brien AM, Smith AT and Ó'Fágáin C, Effects of phthalic anhydride modification on horseradish peroxidase stability and activity. Biotechnol Bioeng 81:233-240 (2003).
    • (2003) Biotechnol Bioeng , vol.81 , pp. 233-240
    • O'Brien, A.M.1    Smith, A.T.2    Ó'Fágáin, C.3
  • 11
    • 13244283460 scopus 로고    scopus 로고
    • Effects of phthalic anhydride modification on horseradish peroxidase stability and structure
    • Song HY, Yao JH, Liu JZ, Zhou SJ, Xiong YH and Ji LN, Effects of phthalic anhydride modification on horseradish peroxidase stability and structure. Enzyme Microb Technol 36:605-611 (2005).
    • (2005) Enzyme Microb Technol , vol.36 , pp. 605-611
    • Song, H.Y.1    Yao, J.H.2    Liu, J.Z.3    Zhou, S.J.4    Xiong, Y.H.5    Ji, L.N.6
  • 12
    • 27844536480 scopus 로고    scopus 로고
    • Horseradish peroxidase thermostabilization: the combinatorial effects of the surface modification and the polyols
    • Hassani L, Ranjbar B, Khajeh K, Nemat-Gorgani H, Nemat-Gorgani M and Sadeghi K, Horseradish peroxidase thermostabilization: the combinatorial effects of the surface modification and the polyols. Enzyme Microb Technol 38:118-125 (2006).
    • (2006) Enzyme Microb Technol , vol.38 , pp. 118-125
    • Hassani, L.1    Ranjbar, B.2    Khajeh, K.3    Nemat-Gorgani, H.4    Nemat-Gorgani, M.5    Sadeghi, K.6
  • 13
    • 33746746447 scopus 로고    scopus 로고
    • Enhanced dye decolorization efficiency by citraconic anhydride-modified horseradish peroxidase
    • Liu JZ, Wang TL and Ji LN, Enhanced dye decolorization efficiency by citraconic anhydride-modified horseradish peroxidase. J Mol Catal B: Enz 41:81-86 (2006).
    • (2006) J Mol Catal B: Enz , vol.41 , pp. 81-86
    • Liu, J.Z.1    Wang, T.L.2    Ji, L.N.3
  • 14
  • 15
    • 84863726269 scopus 로고    scopus 로고
    • The effect of chemical modification with pyromellitic anhydride on structure, function, and thermal stability of horseradish peroxidase
    • Hassani L, The effect of chemical modification with pyromellitic anhydride on structure, function, and thermal stability of horseradish peroxidase. Appl Biochem Biotechnol 167:489-497 (2012).
    • (2012) Appl Biochem Biotechnol , vol.167 , pp. 489-497
    • Hassani, L.1
  • 16
    • 84899414760 scopus 로고    scopus 로고
    • Modification of lysine residues on horseradish peroxidase and its effect of stability and structure of the enzyme
    • Hassani L and Nourozi R, Modification of lysine residues on horseradish peroxidase and its effect of stability and structure of the enzyme. Appl Biochem Biotechnol 172:3558-3569 (2014).
    • (2014) Appl Biochem Biotechnol , vol.172 , pp. 3558-3569
    • Hassani, L.1    Nourozi, R.2
  • 17
    • 34250343031 scopus 로고    scopus 로고
    • Improvement of activity and stability of chloroperoxidase by chemical modification
    • Liu JZ and Wang M, Improvement of activity and stability of chloroperoxidase by chemical modification. BMC Biotechnol 7:23-30 (2007).
    • (2007) BMC Biotechnol , vol.7 , pp. 23-30
    • Liu, J.Z.1    Wang, M.2
  • 18
    • 33644536734 scopus 로고    scopus 로고
    • Chemical modification of papain for use in alkaline medium
    • Sangeetha K and Abraham TE, Chemical modification of papain for use in alkaline medium. J Mol Catal B: Enz 38:171-177 (2006).
    • (2006) J Mol Catal B: Enz , vol.38 , pp. 171-177
    • Sangeetha, K.1    Abraham, T.E.2
  • 20
    • 0026928606 scopus 로고
    • High stability to irreversible inactivation at elevated temperatures of enzymes covalently modified by hydrophilic reagents: α-chymotrypsin
    • Mozhaev VV, Melik-Nubarov NS, Levitsky V, Siksnis VA and Martinek K, High stability to irreversible inactivation at elevated temperatures of enzymes covalently modified by hydrophilic reagents: α-chymotrypsin. Biotechnol Bioeng 4:650-662 (1992).
    • (1992) Biotechnol Bioeng , vol.4 , pp. 650-662
    • Mozhaev, V.V.1    Melik-Nubarov, N.S.2    Levitsky, V.3    Siksnis, V.A.4    Martinek, K.5
  • 21
    • 0032874901 scopus 로고    scopus 로고
    • Solvation energy and thermal stability of hydrophilization-modified α-chymotrypsin
    • He Z and Zhang Z, Solvation energy and thermal stability of hydrophilization-modified α-chymotrypsin. J Protein Chem 18:557-564 (1999).
    • (1999) J Protein Chem , vol.18 , pp. 557-564
    • He, Z.1    Zhang, Z.2
  • 22
    • 0035177344 scopus 로고    scopus 로고
    • The chemical modification of α-chymotrypsin with both hydrophobic and hydrophilic compounds stabilizes the enzyme against denaturation in water-organic media
    • Vinogradov AA, Kudryashova EV, Grinberg VYa, Grinberg NV, Burova TV and Levashov AV, The chemical modification of α-chymotrypsin with both hydrophobic and hydrophilic compounds stabilizes the enzyme against denaturation in water-organic media. Protein Eng 1:683-689 (2001).
    • (2001) Protein Eng , vol.1 , pp. 683-689
    • Vinogradov, A.A.1    Kudryashova, E.V.2    Vya, G.3    Grinberg, N.V.4    Burova, T.V.5    Levashov, A.V.6
  • 24
    • 0031257411 scopus 로고    scopus 로고
    • Effects of polyols and organic solvents on thermostability of lipase
    • Matsumoto M, Kida K and Kondo K, Effects of polyols and organic solvents on thermostability of lipase. J Chem Technol Biotechnol 70:188-192 (1997).
    • (1997) J Chem Technol Biotechnol , vol.70 , pp. 188-192
    • Matsumoto, M.1    Kida, K.2    Kondo, K.3
  • 25
    • 0034848456 scopus 로고    scopus 로고
    • Enhanced thermostability of α-chymotrypsin enclosed in inorganic microcapsules
    • Matsumoto M and Kondo K, Enhanced thermostability of α-chymotrypsin enclosed in inorganic microcapsules. J Biosci Bioeng 92:197-199 (2001).
    • (2001) J Biosci Bioeng , vol.92 , pp. 197-199
    • Matsumoto, M.1    Kondo, K.2
  • 26
    • 0037375814 scopus 로고    scopus 로고
    • Effect of immobilization on thermostability of lipase from Candida rugosa
    • Matsumoto M and Ohashi K, Effect of immobilization on thermostability of lipase from Candida rugosa. Biochem Eng J 14:75-77 (2003).
    • (2003) Biochem Eng J , vol.14 , pp. 75-77
    • Matsumoto, M.1    Ohashi, K.2
  • 27
    • 0001647744 scopus 로고
    • Kinetic properties on subtilisin type Carlsberg in the crystalline state
    • Tüchsen E and Ottesen M, Kinetic properties on subtilisin type Carlsberg in the crystalline state. Carlsberg Res Commun 42:407-420 (1977).
    • (1977) Carlsberg Res Commun , vol.42 , pp. 407-420
    • Tüchsen, E.1    Ottesen, M.2
  • 28
    • 0342617775 scopus 로고    scopus 로고
    • Molecular reasons for lipase-sensitivity against acetaldehyde
    • Weber HK, Zuegg J, Faber K and Pleiss J, Molecular reasons for lipase-sensitivity against acetaldehyde. J Mol Catal B: Enz 3:131-138 (1997).
    • (1997) J Mol Catal B: Enz , vol.3 , pp. 131-138
    • Weber, H.K.1    Zuegg, J.2    Faber, K.3    Pleiss, J.4
  • 29
    • 0022013872 scopus 로고
    • Categorization of enzyme deactivations using a series-type mechanism
    • Henley JP and Sadana A, Categorization of enzyme deactivations using a series-type mechanism. Enzyme Microb Technol 7:50-60 (1985).
    • (1985) Enzyme Microb Technol , vol.7 , pp. 50-60
    • Henley, J.P.1    Sadana, A.2
  • 30
    • 0024142757 scopus 로고
    • Enzyme deactivation
    • Sadana A, Enzyme deactivation. Biotechnol Adv 6:349-446 (1988).
    • (1988) Biotechnol Adv , vol.6 , pp. 349-446
    • Sadana, A.1
  • 31
    • 8644243613 scopus 로고
    • Partition coefficients and their uses
    • Leo A, Hansch C and Elkins D, Partition coefficients and their uses. Chem Rev 71:525-616 (1971).
    • (1971) Chem Rev , vol.71 , pp. 525-616
    • Leo, A.1    Hansch, C.2    Elkins, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.