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Volumn 6, Issue 6, 2002, Pages 463-468

A novel thermophilic fusion enzyme for trehalose production

Author keywords

Fusion protein; Sulfolobus solfataricus; Thermophilic enzymes; Trehalose; Trehalose forming enzyme; Trehalosyl dextrin forming enzyme

Indexed keywords

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; SULFOLOBALES; SULFOLOBUS SOLFATARICUS;

EID: 0011520985     PISSN: 14310651     EISSN: 14334909     Source Type: Journal    
DOI: 10.1007/s00792-002-0283-6     Document Type: Article
Times cited : (26)

References (23)
  • 1
    • 0033771067 scopus 로고    scopus 로고
    • Physiological roles of trehalose in bacteria and yeast: A comparative analysis
    • Arguelles JC (2000) Physiological roles of trehalose in bacteria and yeast: a comparative analysis. Arch Microbiol 174:217-224
    • (2000) Arch Microbiol , vol.174 , pp. 217-224
    • Arguelles, J.C.1
  • 3
    • 0025768057 scopus 로고
    • Multienzyme systems obtained by gene fusion
    • Bulow L, Mosbach K (1991) Multienzyme systems obtained by gene fusion. Trends Biotechnol 9:226-231
    • (1991) Trends Biotechnol , vol.9 , pp. 226-231
    • Bulow, L.1    Mosbach, K.2
  • 5
    • 0032212016 scopus 로고    scopus 로고
    • Enzymes from Sulfolobus shibatae for the production of trehalose and glucose from starch
    • Di Lernia I, Morana A, Ottombrino A, Fusco S, Rossi M, De Rosa M (1998) Enzymes from Sulfolobus shibatae for the production of trehalose and glucose from starch. Extremophiles 2:409-416
    • (1998) Extremophiles , vol.2 , pp. 409-416
    • Di Lernia, I.1    Morana, A.2    Ottombrino, A.3    Fusco, S.4    Rossi, M.5    De Rosa, M.6
  • 7
    • 0029762131 scopus 로고    scopus 로고
    • Reaction mechanism of a new glycosyltrehalose-producing enzyme isolated from the hyperthermophilic archaeum Sulfolobus solfataricus KM1
    • Kato M, Miura Y Kettoku M, Shindo K, Iwamatsu A, Kobayashi K (1996a) Reaction mechanism of a new glycosyltrehalose-producing enzyme isolated from the hyperthermophilic archaeum Sulfolobus solfataricus KM1, Biosci Biotechnol Biochem 60:921-924
    • (1996) Biosci Biotechnol Biochem , vol.60 , pp. 921-924
    • Kato, M.1    Miura, Y.2    Kettoku, M.3    Shindo, K.4    Iwamatsu, A.5    Kobayashi, K.6
  • 8
    • 0030093276 scopus 로고    scopus 로고
    • Purification and characterisation of new trehalose-producing enzymes isolated from the hyperthermophilic archaeum, Sulfolobus solfataricus KM1
    • Kato M, Miura Y, Kettoku M, Shindo K, Iwamatsu A, Kobayashi K (1996b) Purification and characterisation of new trehalose-producing enzymes isolated from the hyperthermophilic archaeum, Sulfolobus solfataricus KM1. Biosci Biotechnol Biochem 60:546-550
    • (1996) Biosci Biotechnol Biochem , vol.60 , pp. 546-550
    • Kato, M.1    Miura, Y.2    Kettoku, M.3    Shindo, K.4    Iwamatsu, A.5    Kobayashi, K.6
  • 9
    • 0033754243 scopus 로고    scopus 로고
    • Trehalose synthesis by sequential reactions of recombinant maltooligosyltrehalose synthase and maltoolisyltrehalose trehalohydrolase from Brevibacteruim helvolum
    • Kim YH, Kwon TK, Park S, Seo HS, Cheong JJ, Kim CH, Kim JK, Lee JS, Choi YD (2000) Trehalose synthesis by sequential reactions of recombinant maltooligosyltrehalose synthase and maltoolisyltrehalose trehalohydrolase from Brevibacteruim helvolum. Appl Env Microbiol 66:4620-4624
    • (2000) Appl Env Microbiol , vol.66 , pp. 4620-4624
    • Kim, Y.H.1    Kwon, T.K.2    Park, S.3    Seo, H.S.4    Cheong, J.J.5    Kim, C.H.6    Kim, J.K.7    Lee, J.S.8    Choi, Y.D.9
  • 10
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 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, U.K.1
  • 11
    • 0026594952 scopus 로고
    • Characterization of a recombinant bifunctional enzyme, galactose dehydrogenase/bacterial luciferase, displaying an improved bioluminescence in a three-enzyme system
    • Lindbladh C, Persson M, Bulow L, Mosbach K (1992) Characterization of a recombinant bifunctional enzyme, galactose dehydrogenase/bacterial luciferase, displaying an improved bioluminescence in a three-enzyme system. Eur J Biochem 15:204-241
    • (1992) Eur J Biochem , vol.15 , pp. 204-241
    • Lindbladh, C.1    Persson, M.2    Bulow, L.3    Mosbach, K.4
  • 13
    • 0030087778 scopus 로고    scopus 로고
    • Purification and characterization of thermostable maltooligosyl trehalose trehalohydrolase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius
    • Nakada T, Ikegami S, Chaen H, Kubota M, Fukuda S, Sugimoto T, Kurimoto M, Tsujisaka Y (1996) Purification and characterization of thermostable maltooligosyl trehalose trehalohydrolase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. Biosci Biotechnol Biochem 60:263-267
    • (1996) Biosci Biotechnol Biochem , vol.60 , pp. 263-267
    • Nakada, T.1    Ikegami, S.2    Chaen, H.3    Kubota, M.4    Fukuda, S.5    Sugimoto, T.6    Kurimoto, M.7    Tsujisaka, Y.8
  • 15
    • 0030309476 scopus 로고    scopus 로고
    • Biotechnological applications of the disaccharide trehalose
    • Paiva C, Panek A (1996) Biotechnological applications of the disaccharide trehalose. Biotechnol Annu Rev 2:293-314
    • (1996) Biotechnol Annu Rev , vol.2 , pp. 293-314
    • Paiva, C.1    Panek, A.2
  • 17
    • 84988146000 scopus 로고
    • Sweet taste and solution properties of α,α-trehalose
    • Portmann M, Birch G (1995) Sweet taste and solution properties of α,α-trehalose. J Sci Food Agric 69:275-281
    • (1995) J Sci Food Agric , vol.69 , pp. 275-281
    • Portmann, M.1    Birch, G.2
  • 18
    • 0032567344 scopus 로고    scopus 로고
    • Fatty acid synthase dimers containing catalytically active beta-ketoacyl synthase or malonyl/acetyltransferase domains in only one subunit can support fatty acid synthesis at the acyl carrier protein domains of both subunit
    • Rangan VS, Joshi AK, Smith S (1998) Fatty acid synthase dimers containing catalytically active beta-ketoacyl synthase or malonyl/acetyltransferase domains in only one subunit can support fatty acid synthesis at the acyl carrier protein domains of both subunit. J Biol Chem 273:34949-34953
    • (1998) J Biol Chem , vol.273 , pp. 34949-34953
    • Rangan, V.S.1    Joshi, A.K.2    Smith, S.3
  • 19
    • 50749134719 scopus 로고
    • Trehalose, a new approach to premium dried foods
    • Roser B (1991) Trehalose, a new approach to premium dried foods. Trends Food Science Technol 7:166-169
    • (1991) Trends Food Science Technol , vol.7 , pp. 166-169
    • Roser, B.1
  • 20
    • 0012023519 scopus 로고    scopus 로고
    • Characterization of a bifunctional enzyme fusion of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase of Escherichia coli
    • Seo HS, Koo JY, Song JT, Kim CH, Kim JK, Lee JS, Choi YD (2000) Characterization of a bifunctional enzyme fusion of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase of Escherichia coli. Appl Env Microbiol 66:2484-2490
    • (2000) Appl Env Microbiol , vol.66 , pp. 2484-2490
    • Seo, H.S.1    Koo, J.Y.2    Song, J.T.3    Kim, C.H.4    Kim, J.K.5    Lee, J.S.6    Choi, Y.D.7
  • 21
    • 0033909892 scopus 로고    scopus 로고
    • Trehalose is required for conformational repair of heat-denatured proteins in the yeast endoplasmic reticulum but not for maintenance of membrane traffic functions after severe heat stress
    • Simola M, Hanninen A, Stranius S, Makarow M (2000) Trehalose is required for conformational repair of heat-denatured proteins in the yeast endoplasmic reticulum but not for maintenance of membrane traffic functions after severe heat stress. Mol Microbiol 37:42-53
    • (2000) Mol Microbiol , vol.37 , pp. 42-53
    • Simola, M.1    Hanninen, A.2    Stranius, S.3    Makarow, M.4
  • 22
    • 0032039542 scopus 로고    scopus 로고
    • Multiple effects of trehalose on protein folding in vitro and in vivo
    • Singer MA, Lindquist S (1998) Multiple effects of trehalose on protein folding in vitro and in vivo. Mol Cell 1:639-648
    • (1998) Mol Cell , vol.1 , pp. 639-648
    • Singer, M.A.1    Lindquist, S.2
  • 23
    • 0030973690 scopus 로고    scopus 로고
    • The thermodynamic mechanism of protein stabilization by trehalose
    • Xie G, Timasheff SN (1997) The thermodynamic mechanism of protein stabilization by trehalose. Biophys Chem 28:25-43
    • (1997) Biophys Chem , vol.28 , pp. 25-43
    • Xie, G.1    Timasheff, S.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.