메뉴 건너뛰기




Volumn 8, Issue 4, 2004, Pages 335-343

Characterization of the trehalosyl dextrin-forming enzyme from the thermophilic archaeon Sulfolobus solfataricus ATCC 35092

Author keywords

Escherichia coli; Starch; Sulfolobus; Trehalose; Trehalosyl dextrin forming enzyme

Indexed keywords

ARCHAEA; ESCHERICHIA COLI; SULFOLOBUS; SULFOLOBUS SOLFATARICUS;

EID: 11144228871     PISSN: 14310651     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00792-004-0393-4     Document Type: Article
Times cited : (33)

References (30)
  • 1
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein, utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein, utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 2
    • 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
  • 3
    • 0031893439 scopus 로고    scopus 로고
    • Mutations to alter Aspergillus awamori glucoamylase selectivity. I. Tyr48-Phe49 → Trp, Tyr116 → Trp, Tyr175 → Phe, Arg241 → Lys, Ser411 → Ala and Ser411 → Gly
    • Fang TY, Coutinho PM, Reilly PJ, Ford C (1998a) Mutations to alter Aspergillus awamori glucoamylase selectivity. I. Tyr48-Phe49 → Trp, Tyr116 → Trp, Tyr175 → Phe, Arg241 → Lys, Ser411 → Ala and Ser411 → Gly. Protein Eng 11:119-126
    • (1998) Protein Eng , vol.11 , pp. 119-126
    • Fang, T.Y.1    Coutinho, P.M.2    Reilly, P.J.3    Ford, C.4
  • 4
    • 0031942650 scopus 로고    scopus 로고
    • Mutations to alter Aspergillus awamori glucoamylase selectivity. II. Mutation of residues 119 and 121
    • Fang TY, Honzatko RB, Reilly PJ, Ford C (1998b) Mutations to alter Aspergillus awamori glucoamylase selectivity. II. Mutation of residues 119 and 121. Protein Eng 11:127-133
    • (1998) Protein Eng , vol.11 , pp. 127-133
    • Fang, T.Y.1    Honzatko, R.B.2    Reilly, P.J.3    Ford, C.4
  • 5
    • 0033179649 scopus 로고    scopus 로고
    • Improving operating performance of glucoamylase by mutagenesis
    • Ford C (1999) Improving operating performance of glucoamylase by mutagenesis. Curr Opin Biotechnol 10:353-357
    • (1999) Curr Opin Biotechnol , vol.10 , pp. 353-357
    • Ford, C.1
  • 7
    • 0033545516 scopus 로고    scopus 로고
    • Trehalose production with a new enzymatic system from Sulfolobus solfataricus KM1
    • Kato M (1999) Trehalose production with a new enzymatic system from Sulfolobus solfataricus KM1. J Mol Catalysis B Enzymatic 6:223-233
    • (1999) J Mol Catalysis B Enzymatic , vol.6 , pp. 223-233
    • Kato, M.1
  • 8
    • 0029741760 scopus 로고    scopus 로고
    • Reaction mechanism of a new glycosyltrehalose-hydrolyzing enzyme isolated from the hyperthermophilic archaeum, Sulfolobus solfataricus KM1
    • Kato M, Miura Y, Kettoku M, Komeda T, Iwamatsu A, Kobayashi K (1996a) Reaction mechanism of a new glycosyltrehalose-hydrolyzing enzyme isolated from the hyperthermophilic archaeum, Sulfolobus solfataricus KM1. Biosci Biotechnol Biochem 60:925-928
    • (1996) Biosci Biotechnol Biochem , vol.60 , pp. 925-928
    • Kato, M.1    Miura, Y.2    Kettoku, M.3    Komeda, T.4    Iwamatsu, A.5    Kobayashi, K.6
  • 9
    • 0030093276 scopus 로고    scopus 로고
    • Purification and characterization 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 characterization 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
  • 10
    • 0034132923 scopus 로고    scopus 로고
    • Subsite structure and catalytic mechanism of a new glycosyltrehalose- producing enzyme isolated from the hyperthermophilic archaeum Sulfolobus solfataricus KM1
    • Kato M, Takehara K, Kettoku M, Kobayashi K, Shimizu T (2000) Subsite structure and catalytic mechanism of a new glycosyltrehalose-producing enzyme isolated from the hyperthermophilic archaeum Sulfolobus solfataricus KM1. Biosci Biotechnol Biochem 64:319-326
    • (2000) Biosci Biotechnol Biochem , vol.64 , pp. 319-326
    • Kato, M.1    Takehara, K.2    Kettoku, M.3    Kobayashi, K.4    Shimizu, T.5
  • 11
    • 0030937689 scopus 로고    scopus 로고
    • Production of trehalose from starch by novel trehalose-producing enzymes from Sulfolobus solfataricus KM1
    • Kobayashi K, Komeda T, Miura Y, Kettoku M, Kato M (1997) Production of trehalose from starch by novel trehalose-producing enzymes from Sulfolobus solfataricus KM1. J Ferment Bioeng 83:296-298
    • (1997) J Ferment Bioeng , vol.83 , pp. 296-298
    • Kobayashi, K.1    Komeda, T.2    Miura, Y.3    Kettoku, M.4    Kato, M.5
  • 12
    • 12544259561 scopus 로고    scopus 로고
    • Refined structure and functional implications of trehalose synthase from Sulfolobus acidocaldarius
    • Kobayashi M, Kubota M, Matsuura Y (2003) Refined structure and functional implications of trehalose synthase from Sulfolobus acidocaldarius. J Appl Glycosci 50:1-8
    • (2003) J Appl Glycosci , vol.50 , pp. 1-8
    • Kobayashi, M.1    Kubota, M.2    Matsuura, Y.3
  • 13
    • 21244497773 scopus 로고    scopus 로고
    • Structure and function analysis of malto-oligosyltrehalose synthase
    • Kubota M, Maruta K, Fukuda S (2001) Structure and function analysis of malto-oligosyltrehalose synthase. J Appl Glycosci 48:153-161
    • (2001) J Appl Glycosci , vol.48 , pp. 153-161
    • Kubota, M.1    Maruta, K.2    Fukuda, S.3
  • 16
    • 0035831255 scopus 로고    scopus 로고
    • Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes
    • MacGregor EA, Janecek S, Svensson B (2001) Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes. Biochim Biophys Acta 1546:1-20
    • (2001) Biochim Biophys Acta , vol.1546 , pp. 1-20
    • MacGregor, E.A.1    Janecek, S.2    Svensson, B.3
  • 18
    • 33747333106 scopus 로고
    • Use of dinitrosalicilic acid reagent for determination of reducing sugar
    • Miller GL (1959) Use of dinitrosalicilic acid reagent for determination of reducing sugar. Anal Chem 31:426-428
    • (1959) Anal Chem , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 20
    • 0030088142 scopus 로고    scopus 로고
    • Purification and characterization of thermostable maltooligosyl trehalose synthase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius
    • Nakada T, Ikegami S, Chaen H, Kubota M, Fukuda S, Sugimoto T, Kurimoto M, Tsujisaka Y (1996a) Purification and characterization of thermostable maltooligosyl trehalose synthase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. Biosci Biotechnol Biochem 60:263-266
    • (1996) Biosci Biotechnol Biochem , vol.60 , pp. 263-266
    • Nakada, T.1    Ikegami, S.2    Chaen, H.3    Kubota, M.4    Fukuda, S.5    Sugimoto, T.6    Kurimoto, M.7    Tsujisaka, Y.8
  • 21
    • 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 (1996b) Purification and characterization of thermostable maltooligosyl trehalose trehalohydrolase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. Biosci Biotechnol Biochem 60:267-270
    • (1996) Biosci Biotechnol Biochem , vol.60 , pp. 267-270
    • Nakada, T.1    Ikegami, S.2    Chaen, H.3    Kubota, M.4    Fukuda, S.5    Sugimoto, T.6    Kurimoto, M.7    Tsujisaka, Y.8
  • 22
    • 0032702490 scopus 로고    scopus 로고
    • Involvement of the compatible solutes trehalose and sucrose in the response to salt stress of a cyanobacterial Scytonema species isolated from desert soils
    • Page-Sharp M, Behm CA, Smith GD (1999) Involvement of the compatible solutes trehalose and sucrose in the response to salt stress of a cyanobacterial Scytonema species isolated from desert soils. Biochim Biophys Acta 1472:519-528
    • (1999) Biochim Biophys Acta , vol.1472 , pp. 519-528
    • Page-Sharp, M.1    Behm, C.A.2    Smith, G.D.3
  • 24
    • 0027948550 scopus 로고
    • Desiccation tolerance of prokaryotes
    • Potts M (1994) Desiccation tolerance of prokaryotes. Microbiol Rev 58:755-805
    • (1994) Microbiol Rev , vol.58 , pp. 755-805
    • Potts, M.1
  • 27
    • 0030741663 scopus 로고    scopus 로고
    • A possible role of trehalose in osmotolerance and ethanol tolerance in Saccharomyces cerevisiae
    • Sharma SC (1997) A possible role of trehalose in osmotolerance and ethanol tolerance in Saccharomyces cerevisiae. FEMS Microbiol Lett 152:11-15
    • (1997) FEMS Microbiol Lett , vol.152 , pp. 11-15
    • Sharma, S.C.1
  • 29
    • 0032213339 scopus 로고    scopus 로고
    • Thermotolerance in Saccharomyces cerevisiae: The Yin and Yang of trehalose
    • Singer MA, Lindquist S (1998) Thermotolerance in Saccharomyces cerevisiae: the Yin and Yang of trehalose. Trends Biotechnol 16:460-468
    • (1998) Trends Biotechnol , vol.16 , pp. 460-468
    • Singer, M.A.1    Lindquist, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.