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Volumn 35, Issue 2, 2016, Pages 154-162

Effects of Pulsed Electric Field (PEF) Treatment on Enhancing Activity and Conformation of α-Amylase

Author keywords

Enzymatic kinetic; Enzymatic structure; PEF; Storage stability; Amylase

Indexed keywords

AMINO ACID; AMYLASE; TRYPTOPHAN; BACTERIAL PROTEIN;

EID: 84958745392     PISSN: 15723887     EISSN: 18758355     Source Type: Journal    
DOI: 10.1007/s10930-016-9649-y     Document Type: Article
Times cited : (48)

References (45)
  • 1
  • 3
    • 84904307695 scopus 로고    scopus 로고
    • New insights into the effectiveness of alpha-amylase enzyme presentation on the Bacillus subtilis spore surface by adsorption and covalent immobilization
    • Gashtasbi F, Ahmadian G, Noghabi KA (2014) New insights into the effectiveness of alpha-amylase enzyme presentation on the Bacillus subtilis spore surface by adsorption and covalent immobilization. Enzyme Microb Technol 64:17–23
    • (2014) Enzyme Microb Technol , vol.64 , pp. 17-23
    • Gashtasbi, F.1    Ahmadian, G.2    Noghabi, K.A.3
  • 4
    • 79953267462 scopus 로고    scopus 로고
    • Single step purification and characterization of a thermostable and calcium independent α-amylase from Bacillus amyloliquifaciens TSWK1-1 isolated from Tulsi Shyam hot spring reservoir, Gujarat (India)
    • COI: 1:CAS:528:DC%2BC3MXksFymsrg%3D
    • Kikani BA, Singh SP (2011) Single step purification and characterization of a thermostable and calcium independent α-amylase from Bacillus amyloliquifaciens TSWK1-1 isolated from Tulsi Shyam hot spring reservoir, Gujarat (India). Int J Biol Macromol 48:676–681
    • (2011) Int J Biol Macromol , vol.48 , pp. 676-681
    • Kikani, B.A.1    Singh, S.P.2
  • 5
    • 84890047134 scopus 로고    scopus 로고
    • Glutaraldehyde in bio-catalysts design: a useful cross linker and a versatile tool in enzyme immobilization
    • COI: 1:CAS:528:DC%2BC3sXhvVyqsb3L
    • Barbosa O, Ortiz C, Berenguer-Murcia Á, Torres R, Rodrigues RC, Fernandez-Lafuente R (2014) Glutaraldehyde in bio-catalysts design: a useful cross linker and a versatile tool in enzyme immobilization. RSC Adv 4:1583–1600
    • (2014) RSC Adv , vol.4 , pp. 1583-1600
    • Barbosa, O.1    Ortiz, C.2    Berenguer-Murcia, Á.3    Torres, R.4    Rodrigues, R.C.5    Fernandez-Lafuente, R.6
  • 7
    • 84907487264 scopus 로고    scopus 로고
    • Gene cloning and characterization of a thermostable organic-tolerant α-amylase from Bacillus subtilis DR8806
    • COI: 1:CAS:528:DC%2BC2cXhsVOmsrjO
    • Emtenani S, Asoodeh A, Emtenani S (2015) Gene cloning and characterization of a thermostable organic-tolerant α-amylase from Bacillus subtilis DR8806. Int J Biol Macromol 72:290–298
    • (2015) Int J Biol Macromol , vol.72 , pp. 290-298
    • Emtenani, S.1    Asoodeh, A.2    Emtenani, S.3
  • 8
    • 79751533142 scopus 로고    scopus 로고
    • Immobilization of soybean (Glycine max) α-amylase onto Chitosan and Amberlite MB-150 beads: optimization and characterization
    • COI: 1:CAS:528:DC%2BC3MXhsFyksLY%3D
    • Kumari A, Kayastha AM (2011) Immobilization of soybean (Glycine max) α-amylase onto Chitosan and Amberlite MB-150 beads: optimization and characterization. J Mol Catal B Enzym 69(1–2):8–14
    • (2011) J Mol Catal B Enzym , vol.69 , Issue.1-2 , pp. 8-14
    • Kumari, A.1    Kayastha, A.M.2
  • 9
    • 34548240693 scopus 로고    scopus 로고
    • Evaluation of culture conditions for cellulase production by two Trichoderma reesei mutants under solid-state fermentation conditions
    • COI: 1:CAS:528:DC%2BD2sXpvVamtbw%3D
    • Latifian M, Hamidi-Esfahani Z, Barzegar M (2007) Evaluation of culture conditions for cellulase production by two Trichoderma reesei mutants under solid-state fermentation conditions. Bioresour Technol 98:3634–3637
    • (2007) Bioresour Technol , vol.98 , pp. 3634-3637
    • Latifian, M.1    Hamidi-Esfahani, Z.2    Barzegar, M.3
  • 10
    • 0342585512 scopus 로고
    • Enhancement of catalytic activity of porcine pancreatic lipase by reductive alkylation
    • COI: 1:CAS:528:DyaL1MXhs12ju7Y%3D
    • Kaimal TNB, Saroja M (1989) Enhancement of catalytic activity of porcine pancreatic lipase by reductive alkylation. Biotechnol Lett 11:31–36
    • (1989) Biotechnol Lett , vol.11 , pp. 31-36
    • Kaimal, T.N.B.1    Saroja, M.2
  • 11
    • 73249127566 scopus 로고    scopus 로고
    • Effects of static magnetic field on activity and stability of immobilized α-amylases in chitosan bead
    • COI: 1:CAS:528:DC%2BC3cXktlSisw%3D%3D
    • Liu Y, Jia S, Ran J, Ran J, Wu S (2010) Effects of static magnetic field on activity and stability of immobilized α-amylases in chitosan bead. Catal Commun 11:364–367
    • (2010) Catal Commun , vol.11 , pp. 364-367
    • Liu, Y.1    Jia, S.2    Ran, J.3    Ran, J.4    Wu, S.5
  • 13
    • 84884352224 scopus 로고    scopus 로고
    • Effect of ultrasound and high hydrostatic pressure (US/HHP) on the degradation of dextran catalyzed by dextranase
    • COI: 1:CAS:528:DC%2BC3sXptFKqs7k%3D
    • Bashari M, Abdelhai MH, Abbas S, Eibaid A, Xu X, Jin Z (2014) Effect of ultrasound and high hydrostatic pressure (US/HHP) on the degradation of dextran catalyzed by dextranase. Ultrason Sonochem 21:76–83
    • (2014) Ultrason Sonochem , vol.21 , pp. 76-83
    • Bashari, M.1    Abdelhai, M.H.2    Abbas, S.3    Eibaid, A.4    Xu, X.5    Jin, Z.6
  • 14
    • 84885342461 scopus 로고    scopus 로고
    • Effect of pulsed electric field treatment on enzyme kinetics and thermostability of endogenous ascorbic acid oxidase in carrots (Daucus carota cv. Nantes)
    • COI: 1:CAS:528:DC%2BC3sXhs1ykt7zI
    • Leong SY, Oey I (2014) Effect of pulsed electric field treatment on enzyme kinetics and thermostability of endogenous ascorbic acid oxidase in carrots (Daucus carota cv. Nantes). Food Chem 146:538–547
    • (2014) Food Chem , vol.146 , pp. 538-547
    • Leong, S.Y.1    Oey, I.2
  • 15
    • 79956088512 scopus 로고    scopus 로고
    • Microbial and enzymatic stability of fruit juice-milk beverages treated by high intensity pulsed electric fields or heat during refrigerated storage
    • COI: 1:CAS:528:DC%2BC3MXmsVymtrk%3D
    • Salvia-Trujillo L, Morales-de la Peña M, Rojas-Graü MA, Martín-Belloso O (2011) Microbial and enzymatic stability of fruit juice-milk beverages treated by high intensity pulsed electric fields or heat during refrigerated storage. Food Control 22:1639–1646
    • (2011) Food Control , vol.22 , pp. 1639-1646
    • Salvia-Trujillo, L.1    Morales-de la Peña, M.2    Rojas-Graü, M.A.3    Martín-Belloso, O.4
  • 16
    • 58549100890 scopus 로고    scopus 로고
    • Changes in quality attributes throughout storage of strawberry juice processed by high-intensity pulsed electric fields or heat treatments
    • COI: 1:CAS:528:DC%2BD1MXhtVCmtL8%3D
    • Aguilo-Aguayo I, Oms-Oliu G, Soliva-Fortuny R, Martín-Belloso O (2009) Changes in quality attributes throughout storage of strawberry juice processed by high-intensity pulsed electric fields or heat treatments. LWT Food Sci Technol 42:813–818
    • (2009) LWT Food Sci Technol , vol.42 , pp. 813-818
    • Aguilo-Aguayo, I.1    Oms-Oliu, G.2    Soliva-Fortuny, R.3    Martín-Belloso, O.4
  • 17
    • 84899851999 scopus 로고    scopus 로고
    • A novel application of pulsed electric field (PEF) processing for improving glutathione (GSH) antioxidant activity
    • COI: 1:CAS:528:DC%2BC2cXnvFChtb0%3D
    • Wang J, Wang K, Wang Y, Lin SY, Zhao P, Jones G (2014) A novel application of pulsed electric field (PEF) processing for improving glutathione (GSH) antioxidant activity. Food Chem 161:361–366
    • (2014) Food Chem , vol.161 , pp. 361-366
    • Wang, J.1    Wang, K.2    Wang, Y.3    Lin, S.Y.4    Zhao, P.5    Jones, G.6
  • 18
    • 84904886353 scopus 로고    scopus 로고
    • Reduction of bacterial counts and inactivation of enzymes in bovine whole milk using pulsed electric fields
    • COI: 1:CAS:528:DC%2BC2cXhtlClt7bL
    • Sharma P, Oey I, Bremer P, Everetta DW (2014) Reduction of bacterial counts and inactivation of enzymes in bovine whole milk using pulsed electric fields. Int Dairy J 39(1):146–156
    • (2014) Int Dairy J , vol.39 , Issue.1 , pp. 146-156
    • Sharma, P.1    Oey, I.2    Bremer, P.3    Everetta, D.W.4
  • 19
    • 84892448920 scopus 로고    scopus 로고
    • Pulsed electric field processing of different fruit juices: impact of pH and temperature on inactivation of spoilage and pathogenic micro-organisms
    • COI: 1:STN:280:DC%2BC2czkslahsA%3D%3D
    • Timmermans RAH, Groot MN, Nederhoff AL, Boekel MAJS, Matser AM, Mastwijk HC (2014) Pulsed electric field processing of different fruit juices: impact of pH and temperature on inactivation of spoilage and pathogenic micro-organisms. Int J Food Microbiol 173:105–111
    • (2014) Int J Food Microbiol , vol.173 , pp. 105-111
    • Timmermans, R.A.H.1    Groot, M.N.2    Nederhoff, A.L.3    Boekel, M.A.J.S.4    Matser, A.M.5    Mastwijk, H.C.6
  • 20
    • 33845632424 scopus 로고    scopus 로고
    • Influence of pulsed electric field on various enzyme activities
    • COI: 1:CAS:528:DC%2BD2sXpvFCg
    • Ohshima T, Tamura T, Sato M (2007) Influence of pulsed electric field on various enzyme activities. J Electrostat 65:156–161
    • (2007) J Electrostat , vol.65 , pp. 156-161
    • Ohshima, T.1    Tamura, T.2    Sato, M.3
  • 21
    • 84897095745 scopus 로고    scopus 로고
    • Pulsed electric field treatment combined with commercial enzymes converts major ginsenoside Rb1 to minor ginsenoside Rd
    • COI: 1:CAS:528:DC%2BC2cXis1Cmtrw%3D
    • Lu C, Yin Y (2014) Pulsed electric field treatment combined with commercial enzymes converts major ginsenoside Rb1 to minor ginsenoside Rd. Innov Food Sci Emerg 22:95–101
    • (2014) Innov Food Sci Emerg , vol.22 , pp. 95-101
    • Lu, C.1    Yin, Y.2
  • 22
    • 84878114797 scopus 로고    scopus 로고
    • A mild pulsed electric field condition that improves acid tolerance, growth, and protease activity of Lactobacillus acidophilus LA-K and Lactobacillus delbrueckii subspecies bulgaricus LB-12
    • COI: 1:CAS:528:DC%2BC3sXmtVaktro%3D
    • Najim N, Aryana KJ (2013) A mild pulsed electric field condition that improves acid tolerance, growth, and protease activity of Lactobacillus acidophilus LA-K and Lactobacillus delbrueckii subspecies bulgaricus LB-12. J Dairy Sci 96:3424–3434
    • (2013) J Dairy Sci , vol.96 , pp. 3424-3434
    • Najim, N.1    Aryana, K.J.2
  • 23
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • COI: 1:CAS:528:DyaG1MXmtFKiuw%3D%3D
    • Miller GL (1959) Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal Chem 31:426–428
    • (1959) Anal Chem , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 24
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • COI: 1:CAS:528:DC%2BD2cXlvFKmsbc%3D
    • Whitmore L, Wallace BA (2004) DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res 32:W668–W673
    • (2004) Nucleic Acids Res , vol.32 , pp. W668-W673
    • Whitmore, L.1    Wallace, B.A.2
  • 25
    • 4344678139 scopus 로고    scopus 로고
    • Production, purification and properties of endoglucanase from a newly isolated strain of Mucor circinelloides
    • COI: 1:CAS:528:DC%2BD2cXmvFyktrc%3D
    • Saha BC (2004) Production, purification and properties of endoglucanase from a newly isolated strain of Mucor circinelloides. Process Biochem 39:1871–1876
    • (2004) Process Biochem , vol.39 , pp. 1871-1876
    • Saha, B.C.1
  • 26
    • 0036291188 scopus 로고    scopus 로고
    • Inactivation of peach polyphenoloxidase by exposure to pulsed electric fields
    • COI: 1:CAS:528:DC%2BD38XkvVyqt7s%3D
    • Giner J, Ortega M, Mesegué M, Gimeno V, Barbosa-Cánovas GV, Martín O (2002) Inactivation of peach polyphenoloxidase by exposure to pulsed electric fields. J Food Sci 67:1467–1472
    • (2002) J Food Sci , vol.67 , pp. 1467-1472
    • Giner, J.1    Ortega, M.2    Mesegué, M.3    Gimeno, V.4    Barbosa-Cánovas, G.V.5    Martín, O.6
  • 27
    • 0014021894 scopus 로고
    • The circular dichroism of the β structure of poly-l-lysine
    • COI: 1:CAS:528:DyaF28XktVCqs7o%3D
    • Townend R, Kumosinski TF, Timasheff SN (1966) The circular dichroism of the β structure of poly-l-lysine. Biochem Biophys Res Commun 23:163–169
    • (1966) Biochem Biophys Res Commun , vol.23 , pp. 163-169
    • Townend, R.1    Kumosinski, T.F.2    Timasheff, S.N.3
  • 28
    • 34548847733 scopus 로고    scopus 로고
    • Using circular dichroism spectra to estimate protein secondary structure
    • COI: 1:CAS:528:DC%2BD2sXhtFGjtLrM
    • Greenfield NJ (2006) Using circular dichroism spectra to estimate protein secondary structure. Nat Protoc 1:2876–2890
    • (2006) Nat Protoc , vol.1 , pp. 2876-2890
    • Greenfield, N.J.1
  • 29
    • 0032939813 scopus 로고    scopus 로고
    • Applications of circular dichroism in protein and peptide analysis
    • COI: 1:CAS:528:DyaK1MXislSgsrs%3D
    • Greenfield NJ (1999) Applications of circular dichroism in protein and peptide analysis. Trac Trend Anal Chem 18:236–244
    • (1999) Trac Trend Anal Chem , vol.18 , pp. 236-244
    • Greenfield, N.J.1
  • 30
    • 0033004568 scopus 로고    scopus 로고
    • Contribution of separate tryptophan residues to intrinsic fluorescence of actin. Analysis of 3D structure
    • COI: 1:CAS:528:DyaK1MXkt1Cqsbw%3D
    • Kuznetsova IM, Yakusheva TA, Turoverov KK (1999) Contribution of separate tryptophan residues to intrinsic fluorescence of actin. Analysis of 3D structure. FEBS Lett 452:205–210
    • (1999) FEBS Lett , vol.452 , pp. 205-210
    • Kuznetsova, I.M.1    Yakusheva, T.A.2    Turoverov, K.K.3
  • 31
    • 1342293174 scopus 로고    scopus 로고
    • Conformational transitions in β-lactoglobulin induced by cationic amphiphiles: equilibrium studies
    • COI: 1:CAS:528:DC%2BD2cXivF2ntrk%3D
    • Viseu MI, Carvalho TI, Costa SM (2004) Conformational transitions in β-lactoglobulin induced by cationic amphiphiles: equilibrium studies. Biophys J 86:2392–2402
    • (2004) Biophys J , vol.86 , pp. 2392-2402
    • Viseu, M.I.1    Carvalho, T.I.2    Costa, S.M.3
  • 32
    • 49849099692 scopus 로고    scopus 로고
    • Influence of high-intensity pulsed electric field processing on lipoxygenase and β-glucosidase activities in strawberry juice
    • Aguiló-Aguayo I, Sobrino-López Á, Soliva-Fortuny R, Martín-Belloso O (2008) Influence of high-intensity pulsed electric field processing on lipoxygenase and β-glucosidase activities in strawberry juice. Innov Food Sci Emerg 9:455–462
    • (2008) Innov Food Sci Emerg , vol.9 , pp. 455-462
    • Aguiló-Aguayo, I.1    Sobrino-López, Á.2    Soliva-Fortuny, R.3    Martín-Belloso, O.4
  • 33
    • 14644416474 scopus 로고    scopus 로고
    • High intensity pulsed electric fields and heat treatments applied to a protease from Bacillus subtilis. A comparison study of multiple systems
    • Bendicho S, Marsellés-Fontanet AR, Barbosa-Cánovas GV, Martín-Bellosoa O (2005) High intensity pulsed electric fields and heat treatments applied to a protease from Bacillus subtilis. A comparison study of multiple systems. J Food Eng 69(3):317–323
    • (2005) J Food Eng , vol.69 , Issue.3 , pp. 317-323
    • Bendicho, S.1    Marsellés-Fontanet, A.R.2    Barbosa-Cánovas, G.V.3    Martín-Bellosoa, O.4
  • 34
    • 0030784326 scopus 로고    scopus 로고
    • Effects of high field electric pulses on the activity of selected enzymes
    • Ho SY, Mittal GS, Cross JD (1997) Effects of high field electric pulses on the activity of selected enzymes. J Food Eng 31(1):69–84
    • (1997) J Food Eng , vol.31 , Issue.1 , pp. 69-84
    • Ho, S.Y.1    Mittal, G.S.2    Cross, J.D.3
  • 35
    • 41949138699 scopus 로고    scopus 로고
    • The effect of pulsed electric fields on the inactivation and structure of lysozyme
    • COI: 1:CAS:528:DC%2BD1cXkvVelu74%3D
    • Zhao W, Yang R (2008) The effect of pulsed electric fields on the inactivation and structure of lysozyme. Food Chem 110:334–343
    • (2008) Food Chem , vol.110 , pp. 334-343
    • Zhao, W.1    Yang, R.2
  • 37
    • 41549106602 scopus 로고    scopus 로고
    • Using low intensity ultrasound to improve the efficiency of biological phosphorus removal
    • COI: 1:CAS:528:DC%2BD1cXks1eisb4%3D
    • Xie B, Wang L, Liu H (2008) Using low intensity ultrasound to improve the efficiency of biological phosphorus removal. Ultrason Sonochem 15:775–781
    • (2008) Ultrason Sonochem , vol.15 , pp. 775-781
    • Xie, B.1    Wang, L.2    Liu, H.3
  • 38
    • 22344448223 scopus 로고    scopus 로고
    • Reduction of pectinesterase activity in a commercial enzyme preparation by pulsed electric fields: comparison of inactivation kinetic models
    • COI: 1:CAS:528:DC%2BD2MXmsVaru7s%3D
    • Giner J, Grouberman P, Gimeno V, Martín O (2005) Reduction of pectinesterase activity in a commercial enzyme preparation by pulsed electric fields: comparison of inactivation kinetic models. J Sci Food Agric 85:1613–1621
    • (2005) J Sci Food Agric , vol.85 , pp. 1613-1621
    • Giner, J.1    Grouberman, P.2    Gimeno, V.3    Martín, O.4
  • 39
    • 84896342915 scopus 로고    scopus 로고
    • Extraction, partial purification and characterization of polyphenol oxidase from Solanum lycocarpum fruits
    • COI: 1:CAS:528:DC%2BC2cXlvFCitbs%3D
    • Batista KA, Batista GLA, Alves GL, Fernandes KF (2014) Extraction, partial purification and characterization of polyphenol oxidase from Solanum lycocarpum fruits. J Mol Catal B Enzym 102:211–217
    • (2014) J Mol Catal B Enzym , vol.102 , pp. 211-217
    • Batista, K.A.1    Batista, G.L.A.2    Alves, G.L.3    Fernandes, K.F.4
  • 40
    • 3042825076 scopus 로고    scopus 로고
    • Kinetic properties and thermal behaviour of polygalacturonase used in fruit juice clarification
    • COI: 1:CAS:528:DC%2BD2cXlsFeqs7Y%3D
    • Ortega N, Diego S, Perez-Mateos M, Busto MD (2004) Kinetic properties and thermal behaviour of polygalacturonase used in fruit juice clarification. Food Chem 88:209–217
    • (2004) Food Chem , vol.88 , pp. 209-217
    • Ortega, N.1    Diego, S.2    Perez-Mateos, M.3    Busto, M.D.4
  • 41
    • 70350496788 scopus 로고    scopus 로고
    • Microbial glucoamylases: characteristics and applications
    • COI: 1:CAS:528:DC%2BD1MXhtVCns73M
    • Kumar P, Satyanarayana T (2009) Microbial glucoamylases: characteristics and applications. Crit Rev Biotechnol 29:225–255
    • (2009) Crit Rev Biotechnol , vol.29 , pp. 225-255
    • Kumar, P.1    Satyanarayana, T.2
  • 43
    • 84867401834 scopus 로고    scopus 로고
    • Recent advances in the action of pulsed electric fields on enzymes and food component proteins
    • COI: 1:CAS:528:DC%2BC38XosValu7s%3D
    • Zhao W, Yang R, Zhang HQ (2012) Recent advances in the action of pulsed electric fields on enzymes and food component proteins. Trends Food Sci Technol 27:83–96
    • (2012) Trends Food Sci Technol , vol.27 , pp. 83-96
    • Zhao, W.1    Yang, R.2    Zhang, H.Q.3
  • 44
    • 84867743907 scopus 로고    scopus 로고
    • Influence of low ultrasound intensity on the degradation of dextran catalyzed by dextranase
    • COI: 1:CAS:528:DC%2BC38XhtVyjs7nJ
    • Bashari M, Eibaid A, Wang J, Tian Y, Xu X, Jin Z (2013) Influence of low ultrasound intensity on the degradation of dextran catalyzed by dextranase. Ultrason Sonochem 20:155–161
    • (2013) Ultrason Sonochem , vol.20 , pp. 155-161
    • Bashari, M.1    Eibaid, A.2    Wang, J.3    Tian, Y.4    Xu, X.5    Jin, Z.6
  • 45
    • 84895072413 scopus 로고    scopus 로고
    • Effect of ultrasound on the activity and conformation of α-amylase, papain and pepsin
    • COI: 1:CAS:528:DC%2BC3sXhvFWrt7bJ
    • Yu ZL, Zeng WC, Zhang WH, Liao XP, Shi B (2014) Effect of ultrasound on the activity and conformation of α-amylase, papain and pepsin. Ultrason Sonochem 21:930–993
    • (2014) Ultrason Sonochem , vol.21 , pp. 930-993
    • Yu, Z.L.1    Zeng, W.C.2    Zhang, W.H.3    Liao, X.P.4    Shi, B.5


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