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Volumn 78, Issue 4, 2008, Pages 603-612

Purification and biochemical characterization of a broad substrate specificity thermostable alkaline protease from Aspergillus nidulans

Author keywords

Alkaline; Aspergillus nidulans; Esterase; Protease; Thermostable

Indexed keywords

CHARACTERIZATION; CHROMATOGRAPHY; ENZYME ACTIVITY; ION EXCHANGE; PURIFICATION; VEGETABLE OILS;

EID: 40549101853     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-007-1324-y     Document Type: Article
Times cited : (37)

References (48)
  • 1
    • 0020546122 scopus 로고
    • Purification and properties of two neutral proteinases from Aspergillus nidulans
    • H Ansari L Stevens 1983 Purification and properties of two neutral proteinases from Aspergillus nidulans J Gen Microbiol 129 6 1637 1644 1:CAS:528:DyaL3sXltVWgsbo%3D Ansari H, Stevens L (1983) Purification and properties of two neutral proteinases from Aspergillus nidulans. J Gen Microbiol 129(6):1637–1644
    • (1983) J Gen Microbiol , vol.129 , Issue.6 , pp. 1637-1644
    • Ansari, H1    Stevens, L2
  • 2
    • 0000674457 scopus 로고
    • Production of two types of esterases with opposite positional specificity by Geotrichum sp
    • T Asahara M Matori 1993 Production of two types of esterases with opposite positional specificity by Geotrichum sp Biosci Biotechnol Biochem 57 390 394 1:CAS:528:DyaK3sXit1yrsbk%3D Asahara T, Matori M (1993) Production of two types of esterases with opposite positional specificity by Geotrichum sp. Biosci Biotechnol Biochem 57:390–394
    • (1993) Biosci Biotechnol Biochem , vol.57 , pp. 390-394
    • Asahara, T1    Matori, M2
  • 3
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • JD Bendtsen H Nielsen G Heijne von S Brunak 2004 Improved prediction of signal peptides: SignalP 3.0 J Mol Biol 340 783 795 10.1016/j.jmb.2004.05.028 1:CAS:528:DC%2BD2cXlt1emu7s%3D Bendtsen JD, Nielsen H, von Heijne G, Brunak S (2004) Improved prediction of signal peptides: SignalP 3.0. J Mol Biol 340:783–795
    • (2004) J Mol Biol , vol.340 , pp. 783-795
    • Bendtsen, JD1    Nielsen, H2    Heijne, G3    Brunak, S4
  • 4
    • 0029645279 scopus 로고
    • Catalysis of a protein folding reaction: mechanistic implications of the 2–0 A structure of the subtilisin–prodomain complex
    • P Bryan L Wang J Hoskins S Ruvinov S Strausberg 1995 Catalysis of a protein folding reaction: mechanistic implications of the 2–0 A structure of the subtilisin–prodomain complex Biochemistry 34 10310 10318 10.1021/bi00032a026 1:CAS:528:DyaK2MXntFChsr4%3D Bryan P, Wang L, Hoskins J, Ruvinov S, Strausberg S (1995) Catalysis of a protein folding reaction: mechanistic implications of the 2–0 A structure of the subtilisin–prodomain complex. Biochemistry 34:10310–10318
    • (1995) Biochemistry , vol.34 , pp. 10310-10318
    • Bryan, P1    Wang, L2    Hoskins, J3    Ruvinov, S4    Strausberg, S5
  • 5
    • 0029089388 scopus 로고
    • Vibrio mimicus arylesterase has thioesterase and chymotrypsin-like activity
    • RC Chang JC Chen JF Shaw 1995 Vibrio mimicus arylesterase has thioesterase and chymotrypsin-like activity Biochem Biophys Res Commun 213 2 475 483 10.1006/bbrc.1995.2156 1:CAS:528:DyaK2MXnsFKit7s%3D Chang RC, Chen JC, Shaw JF (1995) Vibrio mimicus arylesterase has thioesterase and chymotrypsin-like activity. Biochem Biophys Res Commun 213(2):475–483
    • (1995) Biochem Biophys Res Commun , vol.213 , Issue.2 , pp. 475-483
    • Chang, RC1    Chen, JC2    Shaw, JF3
  • 6
    • 0015892141 scopus 로고
    • The neutral and alkaline proteases of Aspergillus nidulans
    • BL Cohen 1973 The neutral and alkaline proteases of Aspergillus nidulans J Gen Microbiol 77 2 521 528 1:CAS:528:DyaE3sXltVals7c%3D Cohen BL (1973a) The neutral and alkaline proteases of Aspergillus nidulans. J Gen Microbiol 77(2):521–528
    • (1973) J Gen Microbiol , vol.77 , Issue.2 , pp. 521-528
    • Cohen, BL1
  • 7
    • 0015766295 scopus 로고
    • Regulation of intracellular and extracellular neutral and alkaline proteases in Aspergillus nidulans
    • BL Cohen 1973 Regulation of intracellular and extracellular neutral and alkaline proteases in Aspergillus nidulans J Gen Microbiol 79 311 320 1:CAS:528:DyaE2cXmvVansg%3D%3D Cohen BL (1973b) Regulation of intracellular and extracellular neutral and alkaline proteases in Aspergillus nidulans. J Gen Microbiol 79:311–320
    • (1973) J Gen Microbiol , vol.79 , pp. 311-320
    • Cohen, BL1
  • 8
    • 0028943623 scopus 로고
    • Purification and properties of an extracellular esterase from the fungus Botrytis cinerea
    • P Comménil L Belingheri 1995 Purification and properties of an extracellular esterase from the fungus Botrytis cinerea Lipids 80 351 356 10.1007/BF02536044 Comménil P, Belingheri L (1995) Purification and properties of an extracellular esterase from the fungus Botrytis cinerea. Lipids 80:351–356
    • (1995) Lipids , vol.80 , pp. 351-356
    • Comménil, P1    Belingheri, L2
  • 9
    • 0004205267 scopus 로고
    • Fundamentals of enzyme kinetics
    • A Cornish-Bowden 1995 Fundamentals of enzyme kinetics Portland London Cornish-Bowden A (1995) Fundamentals of enzyme kinetics. Portland, London
    • (1995)
    • Cornish-Bowden, A1
  • 10
    • 0001433809 scopus 로고
    • Method for the determination of the amino acid sequence in peptides
    • P Edman 1950 Method for the determination of the amino acid sequence in peptides Acta Chem Scan 4 289 298 Edman P (1950) Method for the determination of the amino acid sequence in peptides. Acta Chem Scan 4:289–298
    • (1950) Acta Chem Scan , vol.4 , pp. 289-298
    • Edman, P1
  • 11
    • 0036325533 scopus 로고    scopus 로고
    • Thermal and high-pressure inactivation of tomato polygalacturonase: a kinetic study
    • D Fachin A Loey Van L Indrawati M Hendrick 2002 Thermal and high-pressure inactivation of tomato polygalacturonase: a kinetic study J Food Sci 67 1610 1615 10.1111/j.1365-2621.2002.tb08692.x 1:CAS:528:DC%2BD38XlvV2ns7k%3D Fachin D, Van Loey A, Indrawati L, Hendrick M (2002) Thermal and high-pressure inactivation of tomato polygalacturonase: a kinetic study. J Food Sci 67:1610–1615
    • (2002) J Food Sci , vol.67 , pp. 1610-1615
    • Fachin, D1    Loey, A2    Indrawati, L3    Hendrick, M4
  • 12
    • 0030858773 scopus 로고    scopus 로고
    • Esterases in autolysed cultures of filamentous fungi
    • RO García-Lepe F Reyes 1997 Esterases in autolysed cultures of filamentous fungi Lett Appl Microbiol 25 127 130 10.1046/j.1472-765X.1997.00187.x García-Lepe RO, Reyes F (1997) Esterases in autolysed cultures of filamentous fungi. Lett Appl Microbiol 25:127–130
    • (1997) Lett Appl Microbiol , vol.25 , pp. 127-130
    • García-Lepe, RO1    Reyes, F2
  • 13
    • 0037048766 scopus 로고    scopus 로고
    • Thermal inactivation of pectin methylesterase, polygalacturonase and peroxidase in tomato juice
    • EA Gordon Y Sekine N Watanabe DM Barret 2002 Thermal inactivation of pectin methylesterase, polygalacturonase and peroxidase in tomato juice J Agric Food Chem 50 6153 6159 10.1021/jf020462r 1:CAS:528:DC%2BD38XmvFWltbg%3D Gordon EA, Sekine Y, Watanabe N, Barret DM (2002) Thermal inactivation of pectin methylesterase, polygalacturonase and peroxidase in tomato juice. J Agric Food Chem 50:6153–6159
    • (2002) J Agric Food Chem , vol.50 , pp. 6153-6159
    • Gordon, EA1    Sekine, Y2    Watanabe, N3    Barret, DM4
  • 14
    • 0023643158 scopus 로고
    • Processing of a plant vacuolar protein precursor in vitro
    • T Hattori S Ichihara K Nakamura 1987 Processing of a plant vacuolar protein precursor in vitro Eur J Biochem 166 3 533 538 10.1111/j.1432-1033.1987.tb13546.x 1:CAS:528:DyaL2sXltFWhtL8%3D Hattori T, Ichihara S, Nakamura K (1987) Processing of a plant vacuolar protein precursor in vitro. Eur J Biochem 166(3):533–538
    • (1987) Eur J Biochem , vol.166 , Issue.3 , pp. 533-538
    • Hattori, T1    Ichihara, S2    Nakamura, K3
  • 15
    • 0034000128 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular esterase from a thermophilic Rhizopus oryzae strain isolated from a palm fruit
    • A Hiol M Jonzo N Rugani 2000 Purification and characterization of an extracellular esterase from a thermophilic Rhizopus oryzae strain isolated from a palm fruit Enzyme Microb Technol 26 421 430 10.1016/S0141-0229(99)00173-8 1:CAS:528:DC%2BD3cXhsFGru78%3D Hiol A, Jonzo M, Rugani N (2000) Purification and characterization of an extracellular esterase from a thermophilic Rhizopus oryzae strain isolated from a palm fruit. Enzyme Microb Technol 26:421–430
    • (2000) Enzyme Microb Technol , vol.26 , pp. 421-430
    • Hiol, A1    Jonzo, M2    Rugani, N3
  • 16
    • 84987260425 scopus 로고
    • Isolation, purification and characterization of esterase isoenzymes from a technical Aspergillus niger
    • M Höfelmann J Hartmann 1985 Isolation, purification and characterization of esterase isoenzymes from a technical Aspergillus niger J Food Sci 50 1721 1725 10.1111/j.1365-2621.1985.tb10574.x Höfelmann M, Hartmann J (1985) Isolation, purification and characterization of esterase isoenzymes from a technical Aspergillus niger. J Food Sci 50:1721–1725
    • (1985) J Food Sci , vol.50 , pp. 1721-1725
    • Höfelmann, M1    Hartmann, J2
  • 17
    • 0034285515 scopus 로고    scopus 로고
    • Alpha/beta-hydrolase fold enzymes: structures, functions and mechanisms
    • M Holmquist 2000 Alpha/beta-hydrolase fold enzymes: structures, functions and mechanisms Curr Protein Pept Sci 1 2 209 235 10.2174/1389203003381405 1:CAS:528:DC%2BD3cXnsVeisLo%3D Holmquist M (2000) Alpha/beta-hydrolase fold enzymes: structures, functions and mechanisms. Curr Protein Pept Sci 1(2):209–235
    • (2000) Curr Protein Pept Sci , vol.1 , Issue.2 , pp. 209-235
    • Holmquist, M1
  • 18
    • 84954894721 scopus 로고
    • Purification and some properties of a thermostable esterase from Humicola lanuginosa
    • CO Ibrahim M Hayashi 1987 Purification and some properties of a thermostable esterase from Humicola lanuginosa Agric Biol Chem 51 37 45 Ibrahim CO, Hayashi M (1987) Purification and some properties of a thermostable esterase from Humicola lanuginosa. Agric Biol Chem 51:37–45
    • (1987) Agric Biol Chem , vol.51 , pp. 37-45
    • Ibrahim, CO1    Hayashi, M2
  • 19
    • 85004662218 scopus 로고
    • Crystallization and characterization of esterase from Penicillium cyclopium
    • K Isobe T Akiba S Yamaguchi 1988 Crystallization and characterization of esterase from Penicillium cyclopium Agric Biol Chem 52 41 47 1:CAS:528:DyaL1cXhs1eksrs%3D Isobe K, Akiba T, Yamaguchi S (1988) Crystallization and characterization of esterase from Penicillium cyclopium. Agric Biol Chem 52:41–47
    • (1988) Agric Biol Chem , vol.52 , pp. 41-47
    • Isobe, K1    Akiba, T2    Yamaguchi, S3
  • 20
    • 0017447640 scopus 로고
    • Meiotic and mitotic recombination in Aspergillus and its chromosomal aberrations
    • E Kafer 1977 Meiotic and mitotic recombination in Aspergillus and its chromosomal aberrations Adv Genet 19 33 131 1:CAS:528:DyaE2sXks1GjsLY%3D 10.1016/S0065-2660(08)60245-X Kafer E (1977) Meiotic and mitotic recombination in Aspergillus and its chromosomal aberrations. Adv Genet 19:33–131
    • (1977) Adv Genet , vol.19 , pp. 33-131
    • Kafer, E1
  • 21
    • 0028568211 scopus 로고
    • Isolation and characterization of an Aspergillus nidulans gene encoding an alkaline protease
    • ME Katz RN Rice BF Cheetham 1994 Isolation and characterization of an Aspergillus nidulans gene encoding an alkaline protease Gene 150 287 292 10.1016/0378-1119(94)90439-1 1:CAS:528:DyaK2MXivVKks7w%3D Katz ME, Rice RN, Cheetham BF (1994) Isolation and characterization of an Aspergillus nidulans gene encoding an alkaline protease. Gene 150:287–292
    • (1994) Gene , vol.150 , pp. 287-292
    • Katz, ME1    Rice, RN2    Cheetham, BF3
  • 22
    • 0028947702 scopus 로고
    • Aspergillus nidulans mutants affected in acetate metabolism isolated as lipid nonutilizers
    • L Kawasaki A Farres J Aguirre 1995 Aspergillus nidulans mutants affected in acetate metabolism isolated as lipid nonutilizers Exp Mycol 19 1 81 85 10.1006/emyc.1995.1009 1:CAS:528:DyaK2MXlt1ejsr4%3D Kawasaki L, Farres A, Aguirre J (1995) Aspergillus nidulans mutants affected in acetate metabolism isolated as lipid nonutilizers. Exp Mycol 19(1):81–85
    • (1995) Exp Mycol , vol.19 , Issue.1 , pp. 81-85
    • Kawasaki, L1    Farres, A2    Aguirre, J3
  • 23
    • 0035843166 scopus 로고    scopus 로고
    • Improving enzymes by using them in organic solvents
    • AM Klibanov 2001 Improving enzymes by using them in organic solvents Nature 409 241 246 10.1038/35051719 1:CAS:528:DC%2BD3MXlvFWiuw%3D%3D Klibanov AM (2001) Improving enzymes by using them in organic solvents. Nature 409:241–246
    • (2001) Nature , vol.409 , pp. 241-246
    • Klibanov, AM1
  • 24
    • 0028448470 scopus 로고
    • Purification, characterization and crystallization of two types of esterases from Rhizopus niveus
    • M Kohno W Kugimiya 1994 Purification, characterization and crystallization of two types of esterases from Rhizopus niveus Biosci Biotech Biochem 58 1007 1012 1:CAS:528:DyaK2cXlsFaqs7g%3D Kohno M, Kugimiya W (1994) Purification, characterization and crystallization of two types of esterases from Rhizopus niveus. Biosci Biotech Biochem 58:1007–1012
    • (1994) Biosci Biotech Biochem , vol.58 , pp. 1007-1012
    • Kohno, M1    Kugimiya, W2
  • 25
    • 0023119427 scopus 로고
    • Isolation and characterization of an extracellular esterase from the conidia of Neurospora crassa
    • M Kundu J Basu 1987 Isolation and characterization of an extracellular esterase from the conidia of Neurospora crassa J Gen Microbiol 133 149 153 1:CAS:528:DyaL2sXhtlCitr0%3D Kundu M, Basu J (1987) Isolation and characterization of an extracellular esterase from the conidia of Neurospora crassa. J Gen Microbiol 133:149–153
    • (1987) J Gen Microbiol , vol.133 , pp. 149-153
    • Kundu, M1    Basu, J2
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • UK Laemmli 1970 Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 680 685 10.1038/227680a0 1:CAS:528:DC%2BD3MXlsFags7s%3D Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, UK1
  • 27
    • 0035961050 scopus 로고    scopus 로고
    • Subtilisin-catalyzed synthesis of amino acid and peptide esters
    • CF Liu JP Tamp 2001 Subtilisin-catalyzed synthesis of amino acid and peptide esters Application in a two-step enzymatic ligation strategy. Org Lett 3 26 4157 4159 1:CAS:528:DC%2BD3MXos12isb0%3D Liu CF, Tamp JP (2001) Subtilisin-catalyzed synthesis of amino acid and peptide esters. Application in a two-step enzymatic ligation strategy. Org Lett 3(26):4157–4159
    • (2001) Application in a two-step enzymatic ligation strategy. Org Lett , vol.3 , Issue.26 , pp. 4157-4159
    • Liu, CF1    Tamp, JP2
  • 28
    • 0038723702 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network
    • YC Lo SC Lin JF Shaw YC Liaw 2003 Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network J Mol Biol 330 3 539 551 10.1016/S0022-2836(03)00637-5 1:CAS:528:DC%2BD3sXkvFGgsbc%3D Lo YC, Lin SC, Shaw JF, Liaw YC (2003) Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network. J Mol Biol 330(3):539–551
    • (2003) J Mol Biol , vol.330 , Issue.3 , pp. 539-551
    • Lo, YC1    Lin, SC2    Shaw, JF3    Liaw, YC4
  • 29
    • 71849104860 scopus 로고
    • Protein measurement with the folin phenol reagent
    • OH Lowry NJ Rosebrough AL Farr RJ Randall 1951 Protein measurement with the folin phenol reagent J Biol Chem 193 265 275 1:CAS:528:DyaG38XhsVyrsw%3D%3D Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the folin phenol reagent. J Biol Chem 193:265–275
    • (1951) J Biol Chem , vol.193 , pp. 265-275
    • Lowry, OH1    Rosebrough, NJ2    Farr, AL3    Randall, RJ4
  • 30
    • 0035716066 scopus 로고    scopus 로고
    • Differential esterase expression in developmental mutants of Aspergillus nidulans
    • MF Machado MA Castro-Prado de 2001 Differential esterase expression in developmental mutants of Aspergillus nidulans Biochem Genet 39 357 368 10.1023/A:1013844701953 1:CAS:528:DC%2BD38XhsFCntb4%3D Machado MF, de Castro-Prado MA (2001) Differential esterase expression in developmental mutants of Aspergillus nidulans. Biochem Genet 39:357–368
    • (2001) Biochem Genet , vol.39 , pp. 357-368
    • Machado, MF1    Castro-Prado, MA2
  • 31
    • 0029367795 scopus 로고
    • Purification and characterization of a new esterase from Fusarium sp
    • T Mase Y Matsumiya T Akiba 1995 Purification and characterization of a new esterase from Fusarium sp YM-30. Biosci Biotechnol Biochem 59 1771 1772 1:CAS:528:DyaK2MXosFShtb4%3D 10.1271/bbb.59.1771 Mase T, Matsumiya Y, Akiba T (1995) Purification and characterization of a new esterase from Fusarium sp. YM-30. Biosci Biotechnol Biochem 59:1771–1772
    • (1995) YM-30. Biosci Biotechnol Biochem , vol.59 , pp. 1771-1772
    • Mase, T1    Matsumiya, Y2    Akiba, T3
  • 32
    • 0033956850 scopus 로고    scopus 로고
    • Isolation, purification and characterization of a cold-active esterase from Aspergillus nidulans
    • I Mayordomo F Randez-Gil J Prieto 2000 Isolation, purification and characterization of a cold-active esterase from Aspergillus nidulans J Agric Food Chem 48 105 109 10.1021/jf9903354 1:CAS:528:DyaK1MXnslensbc%3D Mayordomo I, Randez-Gil F, Prieto J (2000) Isolation, purification and characterization of a cold-active esterase from Aspergillus nidulans. J Agric Food Chem 48:105–109
    • (2000) J Agric Food Chem , vol.48 , pp. 105-109
    • Mayordomo, I1    Randez-Gil, F2    Prieto, J3
  • 33
    • 0036429672 scopus 로고    scopus 로고
    • Enzymatic synthesis of sugar amino acid esters in organic solvents
    • T Murayama S Nagasawa M Goto 2002 Enzymatic synthesis of sugar amino acid esters in organic solvents J Biosci Bioeng 94 4 357 361 10.1263/jbb.94.357 Murayama T, Nagasawa S, Goto M (2002) Enzymatic synthesis of sugar amino acid esters in organic solvents. J Biosci Bioeng 94(4):357–361
    • (2002) J Biosci Bioeng , vol.94 , Issue.4 , pp. 357-361
    • Murayama, T1    Nagasawa, S2    Goto, M3
  • 34
    • 0031701836 scopus 로고    scopus 로고
    • Purification and characterization of a regiospecific esterase from Aspergillus terreus
    • P Raman K Rajendra G Rani 1998 Purification and characterization of a regiospecific esterase from Aspergillus terreus Biotechnol Appl Biochem 28 243 249 Raman P, Rajendra K, Rani G (1998) Purification and characterization of a regiospecific esterase from Aspergillus terreus. Biotechnol Appl Biochem 28:243–249
    • (1998) Biotechnol Appl Biochem , vol.28 , pp. 243-249
    • Raman, P1    Rajendra, K2    Rani, G3
  • 35
    • 0031686839 scopus 로고    scopus 로고
    • Molecular and biotechnological aspects of microbial proteases
    • MB Rao AM Tanksale MS Ghatge VV Deshpande 1998 Molecular and biotechnological aspects of microbial proteases Microbiol Mol Biol Rev 62 3 597 635 1:CAS:528:DyaK1cXmtFOjurs%3D Rao MB, Tanksale AM, Ghatge MS, Deshpande VV (1998) Molecular and biotechnological aspects of microbial proteases. Microbiol Mol Biol Rev 62(3):597–635
    • (1998) Microbiol Mol Biol Rev , vol.62 , Issue.3 , pp. 597-635
    • Rao, MB1    Tanksale, AM2    Ghatge, MS3    Deshpande, VV4
  • 36
    • 0032479388 scopus 로고    scopus 로고
    • Esterases: interfacial enzymes with attractive applications
    • RD Schmid R Verger 1998 Esterases: interfacial enzymes with attractive applications Angew Chem Int Ed 37 1608 1633 10.1002/(SICI)1521-3773(19980703)37:12<1608::AID-ANIE1608>3.0.CO;2-V Schmid RD, Verger R (1998) Esterases: interfacial enzymes with attractive applications. Angew Chem Int Ed 37:1608–1633
    • (1998) Angew Chem Int Ed , vol.37 , pp. 1608-1633
    • Schmid, RD1    Verger, R2
  • 37
    • 0029899631 scopus 로고    scopus 로고
    • Thermoalkalophilic esterase of Bacillus thermocatenulatus1. molecular cloning, nucleotide sequence, purification and some properties
    • C Schmidt-Dannert R Schmid 1996 Thermoalkalophilic esterase of Bacillus thermocatenulatus 1. molecular cloning, nucleotide sequence, purification and some properties Biochim Biophys Acta 1301 105 104 Schmidt-Dannert C, Schmid R (1996) Thermoalkalophilic esterase of Bacillus thermocatenulatus. 1. molecular cloning, nucleotide sequence, purification and some properties. Biochim Biophys Acta 1301:105–104
    • (1996) Biochim Biophys Acta , vol.1301 , pp. 105-104
    • Schmidt-Dannert, C1    Schmid, R2
  • 38
    • 0031057173 scopus 로고    scopus 로고
    • Bacillus thermocatenulatus esterase: a thermoalkalophilic esterase with interesting properties
    • C Schmidt-Dannert ML Rua S Wahl RD Schmid 1997 Bacillus thermocatenulatus esterase: a thermoalkalophilic esterase with interesting properties Biochem Soc Trans 25 178 182 1:CAS:528:DyaK2sXhvVWhtLs%3D Schmidt-Dannert C, Rua ML, Wahl S, Schmid RD (1997) Bacillus thermocatenulatus esterase: a thermoalkalophilic esterase with interesting properties. Biochem Soc Trans 25:178–182
    • (1997) Biochem Soc Trans , vol.25 , pp. 178-182
    • Schmidt-Dannert, C1    Rua, ML2    Wahl, S3    Schmid, RD4
  • 39
    • 0035725911 scopus 로고    scopus 로고
    • Production, purification, characterization and applications of esterases
    • R Sharma I Chisti BU Chand 2001 Production, purification, characterization and applications of esterases Biotechnol Adv 19 627 662 10.1016/S0734-9750(01)00086-6 1:CAS:528:DC%2BD38XhvVWrsro%3D Sharma R, Chisti I, Chand BU (2001) Production, purification, characterization and applications of esterases. Biotechnol Adv 19:627–662
    • (2001) Biotechnol Adv , vol.19 , pp. 627-662
    • Sharma, R1    Chisti, I2    Chand, BU3
  • 40
    • 0025998717 scopus 로고
    • Homology modelling and protein engineering strategy of subtilases, the family of subtilisin-like serine proteinases
    • R Siezen WM Vos de JA Leunissen BW Dijkstra 1991 Homology modelling and protein engineering strategy of subtilases, the family of subtilisin-like serine proteinases Protein Eng. 4 7 719 737 10.1093/protein/4.7.719 1:CAS:528:DyaK3MXmslCjs7s%3D Siezen R, de Vos WM, Leunissen JA, Dijkstra BW (1991) Homology modelling and protein engineering strategy of subtilases, the family of subtilisin-like serine proteinases. Protein Eng. 4(7):719–737
    • (1991) Protein Eng. , vol.4 , Issue.7 , pp. 719-737
    • Siezen, R1    Vos, WM2    Leunissen, JA3    Dijkstra, BW4
  • 41
    • 0034864538 scopus 로고    scopus 로고
    • Optimization of a thermostable esterase from Bacillus stearothermophilus P1: overexpression, purification and characterization
    • S Sinchaikul B Sookkheo S Phutrakul F Pan S Chen 2001 Optimization of a thermostable esterase from Bacillus stearothermophilus P1: overexpression, purification and characterization Protein Expr Purif 22 388 398 10.1006/prep.2001.1456 1:CAS:528:DC%2BD3MXlsFynt7g%3D Sinchaikul S, Sookkheo B, Phutrakul S, Pan F, Chen S (2001) Optimization of a thermostable esterase from Bacillus stearothermophilus P1: overexpression, purification and characterization. Protein Expr Purif 22:388–398
    • (2001) Protein Expr Purif , vol.22 , pp. 388-398
    • Sinchaikul, S1    Sookkheo, B2    Phutrakul, S3    Pan, F4    Chen, S5
  • 42
    • 0035668519 scopus 로고    scopus 로고
    • Generation of a broad esterolytic subtilisin using combined molecular evolution and periplasmic expression
    • GE Sroga JS Dordick 2001 Generation of a broad esterolytic subtilisin using combined molecular evolution and periplasmic expression Protein Eng 14 11 929 937 10.1093/protein/14.11.929 1:CAS:528:DC%2BD38XjtVemtQ%3D%3D Sroga GE, Dordick JS (2001) Generation of a broad esterolytic subtilisin using combined molecular evolution and periplasmic expression. Protein Eng 14(11):929–937
    • (2001) Protein Eng , vol.14 , Issue.11 , pp. 929-937
    • Sroga, GE1    Dordick, JS2
  • 43
    • 0027278382 scopus 로고
    • Purification and properties of an esterase from Penicillium expansum
    • W Stocklein H Sztajer U Menge R Schmid 1993 Purification and properties of an esterase from Penicillium expansum Biochim Biophys Acta 1168 181 189 1:STN:280:DyaK3s3nsl2gtg%3D%3D Stocklein W, Sztajer H, Menge U, Schmid R (1993) Purification and properties of an esterase from Penicillium expansum. Biochim Biophys Acta 1168:181–189
    • (1993) Biochim Biophys Acta , vol.1168 , pp. 181-189
    • Stocklein, W1    Sztajer, H2    Menge, U3    Schmid, R4
  • 44
    • 85121086235 scopus 로고
    • Separation and characterization of two molecular forms of Geotrichum candidum esterase
    • A Sugihara Y Shimada 1990 Separation and characterization of two molecular forms of Geotrichum candidum esterase J Biochem 100 1207 1213 Sugihara A, Shimada Y (1990) Separation and characterization of two molecular forms of Geotrichum candidum esterase. J Biochem 100:1207–1213
    • (1990) J Biochem , vol.100 , pp. 1207-1213
    • Sugihara, A1    Shimada, Y2
  • 45
    • 0026488315 scopus 로고
    • Purification and characterization of a novel thermostable esterase from Pseudomonas cepacia
    • A Sugihara M Ueshima Y Shimada S Tsunasawa Y Tominaga 1992 Purification and characterization of a novel thermostable esterase from Pseudomonas cepacia J Biochem 112 598 603 1:CAS:528:DyaK3sXislOh Sugihara A, Ueshima M, Shimada Y, Tsunasawa S, Tominaga Y (1992) Purification and characterization of a novel thermostable esterase from Pseudomonas cepacia. J Biochem 112:598–603
    • (1992) J Biochem , vol.112 , pp. 598-603
    • Sugihara, A1    Ueshima, M2    Shimada, Y3    Tsunasawa, S4    Tominaga, Y5
  • 46
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications
    • H Towbin T Staehelin J Gordon 1979 Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications Proc Natl Acad Sci USA 76 9 4350 4354 10.1073/pnas.76.9.4350 1:CAS:528:DyaE1MXmtVKltLw%3D Towbin H, Staehelin T, Gordon J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76(9):4350–4354
    • (1979) Proc Natl Acad Sci USA , vol.76 , Issue.9 , pp. 4350-4354
    • Towbin, H1    Staehelin, T2    Gordon, J3
  • 47
    • 0035976917 scopus 로고    scopus 로고
    • Folding pathway mediated by an intramolecular chaperone: propeptide release modulates activation precision of pro-subtilisin
    • Y Yabuta H Takagi M Inouye U Shinde 2001 Folding pathway mediated by an intramolecular chaperone: propeptide release modulates activation precision of pro-subtilisin J Biol Chem 276 44427 44434 10.1074/jbc.M107573200 1:CAS:528:DC%2BD3MXovFegsLo%3D Yabuta Y, Takagi H, Inouye M, Shinde U (2001) Folding pathway mediated by an intramolecular chaperone: propeptide release modulates activation precision of pro-subtilisin. J Biol Chem 276:44427–44434
    • (2001) J Biol Chem , vol.276 , pp. 44427-44434
    • Yabuta, Y1    Takagi, H2    Inouye, M3    Shinde, U4
  • 48
    • 0037674588 scopus 로고    scopus 로고
    • Folding pathway mediated by an intramolecular chaperone. A functional peptide chaperone designed using sequence databases
    • Y Yabuta E Subbian C Oiry U Shinde 2003 Folding pathway mediated by an intramolecular chaperone. A functional peptide chaperone designed using sequence databases J Biol Chem 78 15246 15251 10.1074/jbc.M212003200 1:CAS:528:DC%2BD3sXjtVClsbo%3D Yabuta Y, Subbian E, Oiry C, Shinde U (2003) Folding pathway mediated by an intramolecular chaperone. A functional peptide chaperone designed using sequence databases. J Biol Chem 78:15246–15251
    • (2003) J Biol Chem , vol.78 , pp. 15246-15251
    • Yabuta, Y1    Subbian, E2    Oiry, C3    Shinde, U4


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