메뉴 건너뛰기




Volumn 28, Issue 2, 2012, Pages 541-548

Catalytic characteristics of plant-esterase from wheat flour

Author keywords

Carbamates; Characterization; Organophosphates; Plant esterase

Indexed keywords

ACTIVE SITE; AMINO ACID RESIDUES; AQUEOUS TWO PHASE SYSTEM; CARBAMATES; CARBOFURANS; CATALYTIC EFFICIENCIES; CONCENTRATION-DEPENDENT; DICHLORVOS; N-BROMOSUCCINIMIDE; OPTIMAL CONDITIONS; ORGANOPHOSPHATES; PEG1000; PLANT- ESTERASE; REACTION CONDITIONS; SENSING MATERIAL; WHEAT FLOURS;

EID: 84856434269     PISSN: 09593993     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11274-011-0845-9     Document Type: Article
Times cited : (26)

References (38)
  • 1
    • 0343193275 scopus 로고
    • Serum esterases. 1.2 types of esterase (a and b) hydrolysing para-nitrophenyl acetate, propionate and butyrate, and a method for their determination
    • Aldrige WN (1953) Serum esterases. 1. 2 types of esterase (a and b) hydrolysing para-nitrophenyl acetate, propionate and butyrate, and a method for their determination. Biochem J 53: 110-117.
    • (1953) Biochem J , vol.53 , pp. 110-117
    • Aldrige, W.N.1
  • 2
    • 77955159789 scopus 로고    scopus 로고
    • Effects of exposure to oxamyl, carbofuran, dichlorvos, and lindane on acetylcholinesterase activity in the gills of the Pacific oyster Crassostrea gigas
    • Anguiano GA, Amador A, Moreno-legorreta M, Arcos-Ortega F, Vazquez-Boucard C (2010) Effects of exposure to oxamyl, carbofuran, dichlorvos, and lindane on acetylcholinesterase activity in the gills of the Pacific oyster Crassostrea gigas. Environ Toxicol 25: 327-332.
    • (2010) Environ Toxicol , vol.25 , pp. 327-332
    • Anguiano, G.A.1    Amador, A.2    Moreno-Legorreta, M.3    Arcos-Ortega, F.4    Vazquez-Boucard, C.5
  • 4
    • 78649457343 scopus 로고    scopus 로고
    • Characterization of acetylcholinesterase from the brain of the Amazonian tambaqui (Colossoma macropomum) and in vitro effect of organophosphorus and carbamate pesticides
    • Assis CR, Castro PF, Amaral IP, Carvalho EV, Carvalho LB Jr, Bezerra RS (2010) Characterization of acetylcholinesterase from the brain of the Amazonian tambaqui (Colossoma macropomum) and in vitro effect of organophosphorus and carbamate pesticides. Environ Toxicol Chem 29: 2243-2248.
    • (2010) Environ Toxicol Chem , vol.29 , pp. 2243-2248
    • Assis, C.R.1    Castro, P.F.2    Amaral, I.P.3    Carvalho, E.V.4    Carvalho Jr., L.B.5    Bezerra, R.S.6
  • 5
    • 80555128229 scopus 로고    scopus 로고
    • Degradation of organophosphorus pesticide induced by oxygen plasma: effects of operating parameters and reaction mechanisms
    • Bai YH, Chen JR, Yang Y, Guo LM, Zhang CH (2010) Degradation of organophosphorus pesticide induced by oxygen plasma: effects of operating parameters and reaction mechanisms. Chemosphere 81: 408-414.
    • (2010) Chemosphere , vol.81 , pp. 408-414
    • Bai, Y.H.1    Chen, J.R.2    Yang, Y.3    Guo, L.M.4    Zhang, C.H.5
  • 6
    • 0345373886 scopus 로고    scopus 로고
    • Crystal structure of human carboxylesterase 1 complexed with the Alzheimer's drug tacrine: from binding promiscuity to selective inhibition
    • Bencharit S, Morton CL, Hyatt JL, Kuhn P, Danks MK, Potter PM, Redinbo MR (2003) Crystal structure of human carboxylesterase 1 complexed with the Alzheimer's drug tacrine: from binding promiscuity to selective inhibition. Chem Biol 10: 341-349.
    • (2003) Chem Biol , vol.10 , pp. 341-349
    • Bencharit, S.1    Morton, C.L.2    Hyatt, J.L.3    Kuhn, P.4    Danks, M.K.5    Potter, P.M.6    Redinbo, M.R.7
  • 7
    • 0025049104 scopus 로고
    • Characterization and assay conditions for usd of ACHe activity from several marine species in pollution monitoring
    • Bocquene G, Galgani F, Truquet P (1990) Characterization and assay conditions for usd of ACHe activity from several marine species in pollution monitoring. Mar Environ Res 30: 75-89.
    • (1990) Mar Environ Res , vol.30 , pp. 75-89
    • Bocquene, G.1    Galgani, F.2    Truquet, P.3
  • 9
    • 33846928747 scopus 로고    scopus 로고
    • Rapid detection of chlorpyrifos residues using a plant hydrolase
    • Chen F, Chen HL (2005) Rapid detection of chlorpyrifos residues using a plant hydrolase. Environ Sci Technol 28: 48-50.
    • (2005) Environ Sci Technol , vol.28 , pp. 48-50
    • Chen, F.1    Chen, H.L.2
  • 10
    • 70350153783 scopus 로고    scopus 로고
    • Comparison of active sites of butyrylcholinesterase and acetylcholinesterase based on inhibition by geometric isomers of benzene-di-N-substituted carbamates
    • Chiou SY, Huang CF, Hwang MT, Lin G (2009) Comparison of active sites of butyrylcholinesterase and acetylcholinesterase based on inhibition by geometric isomers of benzene-di-N-substituted carbamates. J Biochem Mol Toxic 23: 303-308.
    • (2009) J Biochem Mol Toxic , vol.23 , pp. 303-308
    • Chiou, S.Y.1    Huang, C.F.2    Hwang, M.T.3    Lin, G.4
  • 11
    • 33947309206 scopus 로고    scopus 로고
    • Comparative study of acetylcholinesterase and butyrylcholinesterase in brain and serum of several freshwater fish: specific activities and in vitro inhibition by DDVP, an organophosphorus pesticide
    • Chuiko GM (2000) Comparative study of acetylcholinesterase and butyrylcholinesterase in brain and serum of several freshwater fish: specific activities and in vitro inhibition by DDVP, an organophosphorus pesticide. Comp Biochem Phys C 127: 233-242.
    • (2000) Comp Biochem Phys C , vol.127 , pp. 233-242
    • Chuiko, G.M.1
  • 12
    • 4944255198 scopus 로고    scopus 로고
    • Purification and cloning of an esterase from the weed black-grass (Alopecurus myosuroides), which bioactivates aryloxyphenoxypropionate herbicides
    • Cummins I, Edwards R (2004) Purification and cloning of an esterase from the weed black-grass (Alopecurus myosuroides), which bioactivates aryloxyphenoxypropionate herbicides. Plant J 39: 894-904.
    • (2004) Plant J , vol.39 , pp. 894-904
    • Cummins, I.1    Edwards, R.2
  • 13
    • 0035688405 scopus 로고    scopus 로고
    • Biochemical characterisation of esterases active in hydrolysing xenobiotics in wheat and competing weeds
    • Cummins I, Burnet M, Edwatds R (2001) Biochemical characterisation of esterases active in hydrolysing xenobiotics in wheat and competing weeds. Physilol Plantarum 113: 477-485.
    • (2001) Physilol Plantarum , vol.113 , pp. 477-485
    • Cummins, I.1    Burnet, M.2    Edwatds, R.3
  • 14
    • 0000667057 scopus 로고    scopus 로고
    • The gene encoding polyneuridine aldehyde esterase of monoterpenoid indole alkaloid biosynthesis in plants is an ortholog of the alpha/betahydrolase super family
    • Dogru E, Warzecha H, Seibel F, Haebel S, Lottspeich F, Stockigt J (2000) The gene encoding polyneuridine aldehyde esterase of monoterpenoid indole alkaloid biosynthesis in plants is an ortholog of the alpha/betahydrolase super family. Eur J Biochem 267: 1397-1406.
    • (2000) Eur J Biochem , vol.267 , pp. 1397-1406
    • Dogru, E.1    Warzecha, H.2    Seibel, F.3    Haebel, S.4    Lottspeich, F.5    Stockigt, J.6
  • 15
    • 34547129626 scopus 로고    scopus 로고
    • Role of a carboxylesterase in herbicide bioactivation in Arabidopsis thaliana
    • Gershater MC, Cummins I, Edwards R (2007) Role of a carboxylesterase in herbicide bioactivation in Arabidopsis thaliana. J Biol Chem 282: 21460-21466.
    • (2007) J Biol Chem , vol.282 , pp. 21460-21466
    • Gershater, M.C.1    Cummins, I.2    Edwards, R.3
  • 16
    • 33847632518 scopus 로고    scopus 로고
    • Active site directed chemical modification of alpha-galactosidase from Bacillus stearothermophilus (NCIM 5146): Involvement of lysine, tryptophan and carboxylate residues in catalytic site
    • Gote MM, Khan MI, Khire JM (2007) Active site directed chemical modification of alpha-galactosidase from Bacillus stearothermophilus (NCIM 5146): Involvement of lysine, tryptophan and carboxylate residues in catalytic site. Enzym Microb Tech 40: 1312-1320.
    • (2007) Enzym Microb Tech , vol.40 , pp. 1312-1320
    • Gote, M.M.1    Khan, M.I.2    Khire, J.M.3
  • 17
    • 0033153557 scopus 로고    scopus 로고
    • Of barn owls and bankers: a lush variety of alpha/beta hydrolases
    • Heikinheimo P, Goldman A, Jeffries C, Ollis DL (1999) Of barn owls and bankers: a lush variety of alpha/beta hydrolases. Structure 7: R141-R146.
    • (1999) Structure , vol.7
    • Heikinheimo, P.1    Goldman, A.2    Jeffries, C.3    Ollis, D.L.4
  • 18
    • 0034870609 scopus 로고    scopus 로고
    • A census of carbohydrate-active enzymes in the genome of Arabidopsis thaliana
    • Henrissat B, Coutinho PM, Davies GJ (2001) A census of carbohydrate-active enzymes in the genome of Arabidopsis thaliana. Plant Mol Biol 47: 55-72.
    • (2001) Plant Mol Biol , vol.47 , pp. 55-72
    • Henrissat, B.1    Coutinho, P.M.2    Davies, G.J.3
  • 19
    • 64949180616 scopus 로고    scopus 로고
    • Comparison of rapid detection based on two enzymes inhibition by organophosphorus pesticide residues in vegetables
    • Huang ZY, Yuan Y, Lv YZ (2003) Comparison of rapid detection based on two enzymes inhibition by organophosphorus pesticide residues in vegetables. Food Sci 24: 135-137.
    • (2003) Food Sci , vol.24 , pp. 135-137
    • Huang, Z.Y.1    Yuan, Y.2    Lv, Y.Z.3
  • 20
    • 67649217264 scopus 로고    scopus 로고
    • Optical detection of dimethyl methyl-phosphonate with monosulfonate tetraphenyl porphyrin-plant-esterase complex
    • Huo DQ, Yang LM, Hou CJ (2009) Optical detection of dimethyl methyl-phosphonate with monosulfonate tetraphenyl porphyrin-plant-esterase complex. Sens Lett 7: 72-78.
    • (2009) Sens Lett , vol.7 , pp. 72-78
    • Huo, D.Q.1    Yang, L.M.2    Hou, C.J.3
  • 21
    • 0021164483 scopus 로고
    • Purification and properties of a wheat esterase hydrolyzing the plasticizer chemical, bis(2-ethyl-hexyl)phthalate
    • Krell HW, Sandermann H (1984) Purification and properties of a wheat esterase hydrolyzing the plasticizer chemical, bis(2-ethyl-hexyl)phthalate. Eur J Biochem 143: 57-62.
    • (1984) Eur J Biochem , vol.143 , pp. 57-62
    • Krell, H.W.1    Sandermann, H.2
  • 22
    • 77956222611 scopus 로고    scopus 로고
    • Purification and characterization of highly thermostable alpha-amylase from thermophilic alicyclobacillus acidocaldarius
    • Kumar GS, Chandra MS, Mallaiah KV, Sreenivasulu P, Choi YL (2010) Purification and characterization of highly thermostable alpha-amylase from thermophilic alicyclobacillus acidocaldarius. Biotechnol Bioprocess E 15: 435-440.
    • (2010) Biotechnol Bioprocess E , vol.15 , pp. 435-440
    • Kumar, G.S.1    Chandra, M.S.2    Mallaiah, K.V.3    Sreenivasulu, P.4    Choi, Y.L.5
  • 23
    • 0000399944 scopus 로고
    • Inactivation of myosin by 2, 4-dinitrophenol and protection by adenosine triphosphate and other phosphate compounds
    • Levy HM, Leber PD, Ryan EM (1963) Inactivation of myosin by 2, 4-dinitrophenol and protection by adenosine triphosphate and other phosphate compounds. J Biol Chem 238: 3654-3659.
    • (1963) J Biol Chem , vol.238 , pp. 3654-3659
    • Levy, H.M.1    Leber, P.D.2    Ryan, E.M.3
  • 24
    • 84873489119 scopus 로고    scopus 로고
    • Optimization of determination condition for the activities of plant-esterases using α-naphthyl as substrates
    • Liu CH, Feng ZB (2008) Optimization of determination condition for the activities of plant-esterases using α-naphthyl as substrates. Sci Technol Food Ind 29: 145-147.
    • (2008) Sci Technol Food Ind , vol.29 , pp. 145-147
    • Liu, C.H.1    Feng, Z.B.2
  • 25
    • 76349122463 scopus 로고    scopus 로고
    • Purification and biological characterization of a halophilic thermostable protease from Haloferax lucentensis VKMM 007
    • Manikandan M, Pasic L, Kannan V (2009) Purification and biological characterization of a halophilic thermostable protease from Haloferax lucentensis VKMM 007. World J Microb Biot 25: 2247-2256.
    • (2009) World J Microb Biot , vol.25 , pp. 2247-2256
    • Manikandan, M.1    Pasic, L.2    Kannan, V.3
  • 26
    • 0033486287 scopus 로고    scopus 로고
    • Carboxy/cholinesterases:a case study of the evolution of a successful multigene family
    • Oakeshott JG, Claudianos C, Russell RJ, Robin GC (1999) Carboxy/cholinesterases: a case study of the evolution of a successful multigene family. Bio Essays 21: 1031-1042.
    • (1999) Bio Essays , vol.21 , pp. 1031-1042
    • Oakeshott, J.G.1    Claudianos, C.2    Russell, R.J.3    Robin, G.C.4
  • 27
    • 77956180737 scopus 로고    scopus 로고
    • Myeloperoxidase-mediated oxidation of organophosphorus pesticides as a pre-step in their determination by AChE based bioanalytical methods
    • Pasti TL, Momic T, Onjia A, Vujisic L, Vasic V (2010) Myeloperoxidase-mediated oxidation of organophosphorus pesticides as a pre-step in their determination by AChE based bioanalytical methods. Microchim Acta 170: 289-297.
    • (2010) Microchim Acta , vol.170 , pp. 289-297
    • Pasti, T.L.1    Momic, T.2    Onjia, A.3    Vujisic, L.4    Vasic, V.5
  • 28
    • 84987141707 scopus 로고
    • Partial purification of an esterase from tomato cell-suspension cultures hydrolyzing the pyrethroid insecticide cyfluthrin
    • Preiss U, Wallnofer PR, Engelhardt G (1988) Partial purification of an esterase from tomato cell-suspension cultures hydrolyzing the pyrethroid insecticide cyfluthrin. Pestic Sci 23: 13-14.
    • (1988) Pestic Sci , vol.23 , pp. 13-14
    • Preiss, U.1    Wallnofer, P.R.2    Engelhardt, G.3
  • 29
    • 3242805974 scopus 로고    scopus 로고
    • Cloning and expression of a tomato cDNA encoding a methyl jasmonate cleaving esterase
    • Stuhlfelder C, Mueller MJ, Warzecha H (2004) Cloning and expression of a tomato cDNA encoding a methyl jasmonate cleaving esterase. Eur J Biochem 271: 2976-2983.
    • (2004) Eur J Biochem , vol.271 , pp. 2976-2983
    • Stuhlfelder, C.1    Mueller, M.J.2    Warzecha, H.3
  • 30
    • 77952543863 scopus 로고    scopus 로고
    • Chromatographic preparation and kinetic analysis of interactions between tabun enantiomers and acetylcholinesterase
    • Tenberken O, Thiermann H, Worek F, Reiter G (2010) Chromatographic preparation and kinetic analysis of interactions between tabun enantiomers and acetylcholinesterase. Toxicol Lett 195: 142-146.
    • (2010) Toxicol Lett , vol.195 , pp. 142-146
    • Tenberken, O.1    Thiermann, H.2    Worek, F.3    Reiter, G.4
  • 31
    • 33645910088 scopus 로고
    • A study of housefly esterases by means of a sensitive colorimetric method
    • van Asperen K (1962) A study of housefly esterases by means of a sensitive colorimetric method. J Insect Physiol 8: 401-416.
    • (1962) J Insect Physiol , vol.8 , pp. 401-416
    • van Asperen, K.1
  • 32
    • 50949098665 scopus 로고    scopus 로고
    • Studies on sensitivity and detection limit of phytoesterase on organophosphate pesticides
    • Wen YX, Li JK, Zhang XM, Xu J (2006) Studies on sensitivity and detection limit of phytoesterase on organophosphate pesticides. Food Sci 27: 186-187.
    • (2006) Food Sci , vol.27 , pp. 186-187
    • Wen, Y.X.1    Li, J.K.2    Zhang, X.M.3    Xu, J.4
  • 33
    • 77956174444 scopus 로고    scopus 로고
    • Study on purification and properties of soyben esterase
    • Wen YX, Lan WL, Li JK (2008) Study on purification and properties of soyben esterase. Food Sci 29: 292-294.
    • (2008) Food Sci , vol.29 , pp. 292-294
    • Wen, Y.X.1    Lan, W.L.2    Li, J.K.3
  • 34
    • 77956171000 scopus 로고    scopus 로고
    • Purification of plant-esterase in PEG1000/NaH2PO4 aqueous two-phase system by a two-step extraction
    • Yang LM, Huo DQ, Hou CJ, He K, Lv FJ, Fa HB, Luo XG (2010) Purification of plant-esterase in PEG1000/NaH2PO4 aqueous two-phase system by a two-step extraction. Process Biochem 45: 1664-1671.
    • (2010) Process Biochem , vol.45 , pp. 1664-1671
    • Yang, L.M.1    Huo, D.Q.2    Hou, C.J.3    He, K.4    Lv, F.J.5    Fa, H.B.6    Luo, X.G.7
  • 36
    • 54249148446 scopus 로고    scopus 로고
    • Characterization and malathion degradability of carboxylesterase in wheat kernels
    • Yoshii K, Tonogai Y, Katakawa J, Ueno H, Nakamuro K (2008) Characterization and malathion degradability of carboxylesterase in wheat kernels. J Health Sci 54: 535-543.
    • (2008) J Health Sci , vol.54 , pp. 535-543
    • Yoshii, K.1    Tonogai, Y.2    Katakawa, J.3    Ueno, H.4    Nakamuro, K.5
  • 37
    • 77956177788 scopus 로고    scopus 로고
    • Study on purification and characterization of plant-esterase for detection the residues of organophosphate pesticides
    • Zhou YM, Liu D, Hu R, Wei E, Wang X, Li XN, Yu N (2008) Study on purification and characterization of plant-esterase for detection the residues of organophosphate pesticides. Food Sci Tec 3: 54-56.
    • (2008) Food Sci Tec , vol.3 , pp. 54-56
    • Zhou, Y.M.1    Liu, D.2    Hu, R.3    Wei, E.4    Wang, X.5    Li, X.N.6    Yu, N.7
  • 38
    • 78649636018 scopus 로고    scopus 로고
    • Purification and characterization of phenoloxidase from the hemocytes of Eurygaster integriceps (Hemiptera: Scutelleridae)
    • Zibaee A, Bandani AR, Malagoli D (2011) Purification and characterization of phenoloxidase from the hemocytes of Eurygaster integriceps (Hemiptera: Scutelleridae). Comp Biochem Phys B 158(1): 117-123.
    • (2011) Comp Biochem Phys B , vol.158 , Issue.1 , pp. 117-123
    • Zibaee, A.1    Bandani, A.R.2    Malagoli, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.