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Volumn 6, Issue 5, 2002, Pages 407-412

Increased stability of malate dehydrogenase from Halobacterium salinarum at low salt concentration in reverse micelles

Author keywords

CTAB; Halophilic enzyme; hMDH; Reverse micelles; Stability

Indexed keywords

HALOBACTERIUM SALINARUM;

EID: 0036780004     PISSN: 14310651     EISSN: 14334909     Source Type: Journal    
DOI: 10.1007/s00792-002-0272-9     Document Type: Article
Times cited : (3)

References (31)
  • 1
    • 0025942767 scopus 로고
    • Purification and some properties of an atypical alkaline p-nitrophenylphosphatase activity from Halobacterium halobium
    • Bonet ML, Llorca FI, Cadenas E (1991) Purification and some properties of an atypical alkaline p-nitrophenylphosphatase activity from Halobacterium halobium. Int J Biochem 23:1445-1451
    • (1991) Int J Biochem , vol.23 , pp. 1445-1451
    • Bonet, M.L.1    Llorca, F.I.2    Cadenas, E.3
  • 2
    • 0028034679 scopus 로고
    • Stability against denaturation mechanisms in halophilic malate dehydrogenase "adapt" to solvent conditions
    • Bonnete F, Madern D, Zaccai G (1994) Stability against denaturation mechanisms in halophilic malate dehydrogenase "adapt" to solvent conditions. J Mol Biol 244:436-447
    • (1994) J Mol Biol , vol.244 , pp. 436-447
    • Bonnete, F.1    Madern, D.2    Zaccai, G.3
  • 3
    • 0028798976 scopus 로고
    • Comparison of hydrolysis and esterification behavior of Humicola lanuginosa and Rhizomucor miehei lipases in AOT-stabilized water-in-oil microemulsions. 2. Effect of temperature on reaction kinetics and general considerations of stability and productivity
    • Crooks GE, Rees GD, Robinson BH, Svensson M, Stephenson GR (1995) Comparison of hydrolysis and esterification behavior of Humicola lanuginosa and Rhizomucor miehei lipases in AOT-stabilized water-in-oil microemulsions. 2. Effect of temperature on reaction kinetics and general considerations of stability and productivity. Biotechnol Bioeng 48:190-196
    • (1995) Biotechnol Bioeng , vol.48 , pp. 190-196
    • Crooks, G.E.1    Rees, G.D.2    Robinson, B.H.3    Svensson, M.4    Stephenson, G.R.5
  • 4
    • 0028958071 scopus 로고
    • Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium
    • Dym O, Mevarech M, Sussman JL (1995) Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium. Science 267:1344-1346
    • (1995) Science , vol.267 , pp. 1344-1346
    • Dym, O.1    Mevarech, M.2    Sussman, J.L.3
  • 5
    • 0033551441 scopus 로고    scopus 로고
    • Relative role of anions and cations in the stabilization of halophilic malate dehydrogenase
    • Ebel C, Faou P, Kernel B, Zaccai G (1999) Relative role of anions and cations in the stabilization of halophilic malate dehydrogenase. Biochemistry 38:9039-9047
    • (1999) Biochemistry , vol.38 , pp. 9039-9047
    • Ebel, C.1    Faou, P.2    Kernel, B.3    Zaccai, G.4
  • 6
    • 0032563113 scopus 로고    scopus 로고
    • Electrostatic contributions to the stability of halophilic proteins
    • Elcock AH McCammon JA (1998) Electrostatic contributions to the stability of halophilic proteins. J Mol Biol 280:731-748
    • (1998) J Mol Biol , vol.280 , pp. 731-748
    • Elcock, A.H.1    McCammon, J.A.2
  • 7
    • 0027753166 scopus 로고
    • Protein-protein interactions in reverse micelles: Trypsin shows superactivity towards a protein substrate alpha-chymotripsinogen A in reverse micelles of sodium bis(2-ethylhexyl)sulfosuccinate (AOT) in isooctane
    • Fadnavis NW, Chandraprakash Y, Deshpande A (1993) Protein-protein interactions in reverse micelles: trypsin shows superactivity towards a protein substrate alpha-chymotripsinogen A in reverse micelles of sodium bis(2-ethylhexyl)sulfosuccinate (AOT) in isooctane. Biochimie 75:995-999
    • (1993) Biochimie , vol.75 , pp. 995-999
    • Fadnavis, N.W.1    Chandraprakash, Y.2    Deshpande, A.3
  • 8
    • 0022769859 scopus 로고
    • Characteristics of lipase-catalyzed hydrolysis of olive oil in AOT-isooctane reversed micelles
    • Han D, Ree JS (1987) Characteristics of lipase-catalyzed hydrolysis of olive oil in AOT-isooctane reversed micelles. Biotechnol Bioeng 28:1250-1255
    • (1987) Biotechnol Bioeng , vol.28 , pp. 1250-1255
    • Han, D.1    Ree, J.S.2
  • 9
    • 0027976082 scopus 로고
    • Improvement of enzyme activity and stability for reverse micellar-encapsulated lipases in the presence of short-chain and polar alcohols
    • Hayes DG, Gulari E (1994) Improvement of enzyme activity and stability for reverse micellar-encapsulated lipases in the presence of short-chain and polar alcohols. Biocatalysis 11:223-231
    • (1994) Biocatalysis , vol.11 , pp. 223-231
    • Hayes, D.G.1    Gulari, E.2
  • 10
    • 0001447366 scopus 로고
    • Malate dehydrogenase from the halophilic Archaebacterium Halobacterium marismortui: Reconstitution of the enzyme after denaturation and dissociation in various denaturants
    • Hecht K, Jaenicke R (1989) Malate dehydrogenase from the halophilic Archaebacterium Halobacterium marismortui: reconstitution of the enzyme after denaturation and dissociation in various denaturants. Biochemistry 28:4979-4985
    • (1989) Biochemistry , vol.28 , pp. 4979-4985
    • Hecht, K.1    Jaenicke, R.2
  • 11
    • 0000064497 scopus 로고
    • Photosensitized production of hydrogen by hydrogenase in reversed micelles
    • USA
    • Hilhorst R, Laane C, Veeger C (1982) Photosensitized production of hydrogen by hydrogenase in reversed micelles. Proc Natl Acad Sci USA 79:3927-3930
    • (1982) Proc Natl Acad Sci , vol.79 , pp. 3927-3930
    • Hilhorst, R.1    Laane, C.2    Veeger, C.3
  • 12
    • 0026684747 scopus 로고
    • Reversed micelles of polymeric surfactants in nonpolar organic solvents: A new microheterogeneous medium for enzymatic reactions
    • Khmelnitski YL, Gladilin AK, Roubailo VL, Martinek K, Levashov AV (1992) Reversed micelles of polymeric surfactants in nonpolar organic solvents: a new microheterogeneous medium for enzymatic reactions. Eur J Biochem 206:737-745
    • (1992) Eur J Biochem , vol.206 , pp. 737-745
    • Khmelnitski, Y.L.1    Gladilin, A.K.2    Roubailo, V.L.3    Martinek, K.4    Levashov, A.V.5
  • 13
  • 14
    • 0016139829 scopus 로고
    • Salt-dependent properties of proteins from extremely halophilic bacteria
    • Lanyi JK (1974) Salt-dependent properties of proteins from extremely halophilic bacteria. Bacteriol Rev 38:272-290
    • (1974) Bacteriol Rev , vol.38 , pp. 272-290
    • Lanyi, J.K.1
  • 15
    • 0023378105 scopus 로고
    • Activity and stability of horse-liver alcohol dehydrogenase in sodium dioctylsulfosuccinate/ciclohexane reverse micelles
    • Larsson KM, Adlercreutz P, Mattiasson B (1987) Activity and stability of horse-liver alcohol dehydrogenase in sodium dioctylsulfosuccinate/ciclohexane reverse micelles. Eur J Biochem 166:157-161
    • (1987) Eur J Biochem , vol.166 , pp. 157-161
    • Larsson, K.M.1    Adlercreutz, P.2    Mattiasson, B.3
  • 17
    • 0030718555 scopus 로고    scopus 로고
    • Stabilisation of halophilic malate dehydrogenase from Haloarcula marismortui by divalent cations: Effects of temperature, water isotope, cofactor and pH
    • Madern D, Zaccai G (1997) Stabilisation of halophilic malate dehydrogenase from Haloarcula marismortui by divalent cations: effects of temperature, water isotope, cofactor and pH. Eur J Biochem 249:607-611
    • (1997) Eur J Biochem , vol.249 , pp. 607-611
    • Madern, D.1    Zaccai, G.2
  • 18
    • 0019880222 scopus 로고
    • The principles of enzyme stabilization. VI. Catalysis by water-soluble enzymes entrapped into reversed micelles of surfactants in organic solvents
    • Martinek K, Levashov AV, Klyachko NL, Pantin VI, Berezin IV (1981) The principles of enzyme stabilization. VI. Catalysis by water-soluble enzymes entrapped into reversed micelles of surfactants in organic solvents. Biochem Biophys Acta 657:277-294
    • (1981) Biochem Biophys Acta , vol.657 , pp. 277-294
    • Martinek, K.1    Levashov, A.V.2    Klyachko, N.L.3    Pantin, V.I.4    Berezin, I.V.5
  • 19
    • 0017408353 scopus 로고
    • Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 1. Purification and molecular characterization
    • Mevarech M, Eisenberg H, Neumann E (1977) Malate dehydrogenase isolated from extremely halophilic bacteria of the Dead Sea. 1. Purification and molecular characterization. Biochemistry 16:3781-3785
    • (1977) Biochemistry , vol.16 , pp. 3781-3785
    • Mevarech, M.1    Eisenberg, H.2    Neumann, E.3
  • 20
    • 0034734270 scopus 로고    scopus 로고
    • Halophilic enzymes: Proteins with a grain of salt
    • Mevarech M, Frolow F, Gloss LM (2000) Halophilic enzymes: proteins with a grain of salt. Biophys Chem 86:155-164
    • (2000) Biophys Chem , vol.86 , pp. 155-164
    • Mevarech, M.1    Frolow, F.2    Gloss, L.M.3
  • 21
    • 0025215312 scopus 로고
    • The behaviour of proteases in lecithin reverse micelles
    • Peng Q, Luisi PL (1990) The behaviour of proteases in lecithin reverse micelles. Eur J Biochem 188:471-480
    • (1990) Eur J Biochem , vol.188 , pp. 471-480
    • Peng, Q.1    Luisi, P.L.2
  • 23
    • 0019616694 scopus 로고
    • Structure and activity of malate dehydrogenase from the extreme halophilic bacteria of the Dead Sea
    • Pundak S, Aloni H, Eisenberg H (1981) Structure and activity of malate dehydrogenase from the extreme halophilic bacteria of the Dead Sea. Eur J Biochem 118:471-477
    • (1981) Eur J Biochem , vol.118 , pp. 471-477
    • Pundak, S.1    Aloni, H.2    Eisenberg, H.3
  • 24
  • 25
    • 0024999957 scopus 로고
    • Enhanced enzymatic activity in reverse micelles
    • Ruckenstein E, Karpe P (1990) Enhanced enzymatic activity in reverse micelles. Biotechnol Lett 4:241-246
    • (1990) Biotechnol Lett , vol.4 , pp. 241-246
    • Ruckenstein, E.1    Karpe, P.2
  • 31
    • 0024962259 scopus 로고
    • Stabilization of halophilic malate dehydrogenase
    • Zaccai G, Cendrin F (1989) Stabilization of halophilic malate dehydrogenase. J Mol Biol 208:491-500
    • (1989) J Mol Biol , vol.208 , pp. 491-500
    • Zaccai, G.1    Cendrin, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.