메뉴 건너뛰기




Volumn 25, Issue 12, 2009, Pages 2165-2172

Overexpression of β-glucosidase from Thermotoga maritima for the production of highly purified aglycone isoflavones from soy flour

Author keywords

Glucosidase; Aglycone isoflavones; Overexpression; Thermotoga maritima

Indexed keywords

AGLYCONES; GLUCOSIDASE; ISOFLAVONES; OVER-EXPRESSION; THERMOTOGA MARITIMA;

EID: 76349119948     PISSN: 09593993     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11274-009-0121-4     Document Type: Article
Times cited : (20)

References (26)
  • 1
    • 33746513906 scopus 로고    scopus 로고
    • Structural basis of the destabilization produced by an amino-terminal tag in the β-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus
    • Ausili A, Cobucci-Ponzano B, Di Lauro B, D'Avino R, Scirè A, Rossi M, Tanfani F, Moracci M (2006) Structural basis of the destabilization produced by an amino-terminal tag in the β-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus. Biochimie 88: 807-817.
    • (2006) Biochimie , vol.88 , pp. 807-817
    • Ausili, A.1    Cobucci-Ponzano, B.2    Di Lauro, B.3    D'Avino, R.4    Scirè, A.5    Rossi, M.6    Tanfani, F.7    Moracci, M.8
  • 2
    • 23944471715 scopus 로고    scopus 로고
    • Purification of an isoflavonoid 7-O-β-apiosyl-glucoside β-glycosidase and its substrates from Dalbergianigrescens Kurz
    • Chuankhayan P, Hua Y, Svasti J, Sakdarat S, Sullivan PA, Ketudat-Cairns JR (2005) Purification of an isoflavonoid 7-O-β-apiosyl-glucoside β-glycosidase and its substrates from Dalbergianigrescens Kurz. Phytochemistry 66: 1880-1889.
    • (2005) Phytochemistry , vol.66 , pp. 1880-1889
    • Chuankhayan, P.1    Hua, Y.2    Svasti, J.3    Sakdarat, S.4    Sullivan, P.A.5    Ketudat-Cairns, J.R.6
  • 3
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability
    • Claire V, Gregory JZ (2001) Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol Mol Biol Rev 65: 1-43.
    • (2001) Microbiol Mol Biol Rev , vol.65 , pp. 1-43
    • Claire, V.1    Gregory, J.Z.2
  • 4
    • 0141885250 scopus 로고    scopus 로고
    • Genistein appears to prevent early postmenopausal bone loss as effectively as hormone replacement therapy
    • Cotter A, Cashman KD (2003) Genistein appears to prevent early postmenopausal bone loss as effectively as hormone replacement therapy. Nutr Rev 61: 346-351.
    • (2003) Nutr Rev , vol.61 , pp. 346-351
    • Cotter, A.1    Cashman, K.D.2
  • 5
    • 0032566518 scopus 로고    scopus 로고
    • Deglycosylation of flavonoid and isoflavonoid glycosides by human small intestine and liver β-l-glucosidase activity
    • Day AJ, DuPont MS, Ridley S, Rhodes M, Rhodes MJ, Morgan MR, Williamson G (1998) Deglycosylation of flavonoid and isoflavonoid glycosides by human small intestine and liver β-l-glucosidase activity. FEBS Lett 436: 71-75.
    • (1998) FEBS Lett , vol.436 , pp. 71-75
    • Day, A.J.1    Dupont, D.P.2    Ridley, R.3    Rhodes, R.4    Rhodes, M.J.5    Morgan, M.R.6    Williamson, G.7
  • 6
    • 0027420381 scopus 로고
    • Purification and properties of recombinant β-glucosidase of the hyperthermophilic bacterium Thermotoga maritima
    • Gabelsberger J, Liebl W, Schleifer KH (1993) Purification and properties of recombinant β-glucosidase of the hyperthermophilic bacterium Thermotoga maritima. Appl Microbiol Biotechnol 40: 44-52.
    • (1993) Appl Microbiol Biotechnol , vol.40 , pp. 44-52
    • Gabelsberger, J.1    Liebl, W.2    Schleifer, K.H.3
  • 7
    • 0035965060 scopus 로고    scopus 로고
    • Characterization of a thermostable β-glucosidase (BglB) from Thermotoga maritima showing transglycosylation activity
    • Goyal K, Selvakumar P, Hayashi K (2001) Characterization of a thermostable β-glucosidase (BglB) from Thermotoga maritima showing transglycosylation activity. J Mol Cat B: Enzymatic 15: 45-53.
    • (2001) J Mol Cat B: Enzymatic , vol.15 , pp. 45-53
    • Goyal, K.1    Selvakumar, P.2    Hayashi, K.3
  • 8
    • 0022522022 scopus 로고
    • Thermotoga maritima sp. nov. represents a new genus of unique extremely thermophilic eubacteria growing up 90°C
    • Huber R, Langworthy TA, Konig H, Thomm M, Woese CR, Sleytr UB, Stetter KO (1986) Thermotoga maritima sp. nov. represents a new genus of unique extremely thermophilic eubacteria growing up 90°C. Arch Microbiol 144: 324-333.
    • (1986) Arch Microbiol , vol.144 , pp. 324-333
    • Huber, R.1    Langworthy, T.A.2    Konig, H.3    Thomm, M.4    Woese, C.R.5    Sleytr, U.B.6    Stetter, K.O.7
  • 10
    • 16244389982 scopus 로고    scopus 로고
    • Comparison of regulative functions between dietary soy isoflavones aglycone and glucoside on lipid metabolism in rats fed cholesterol
    • Kawakami Y, Tsurugasaki W, Nakamura S, Osada K (2005) Comparison of regulative functions between dietary soy isoflavones aglycone and glucoside on lipid metabolism in rats fed cholesterol. J Nutr Biochem 16: 205-212.
    • (2005) J Nutr Biochem , vol.16 , pp. 205-212
    • Kawakami, Y.1    Tsurugasaki, W.2    Nakamura, S.3    Osada, K.4
  • 12
    • 0034086069 scopus 로고    scopus 로고
    • Protection against breast cancer with genistein: A component of soy
    • Lamartiniere CA (2000) Protection against breast cancer with genistein: a component of soy. Am J Clin Nutr 71(6): 1705-1707.
    • (2000) Am J Clin Nutr , vol.71 , Issue.6 , pp. 1705-1707
    • Lamartiniere, C.A.1
  • 13
    • 1842430871 scopus 로고    scopus 로고
    • Purification and characterization of an isoflavone-conjugates-hydrolyzing β-glucosidase from endophytic bacterium
    • Liu Y, Zhou SN, Chen ZS, Zhong YC, Liu YH (2004) Purification and characterization of an isoflavone-conjugates-hydrolyzing β-glucosidase from endophytic bacterium. J Agric Food Chem 52: 1940-1944.
    • (2004) J Agric Food Chem , vol.52 , pp. 1940-1944
    • Liu, Y.1    Zhou, S.N.2    Chen, Z.S.3    Zhong, Y.C.4    Liu, Y.H.5
  • 14
    • 33750469308 scopus 로고    scopus 로고
    • Heat and pH effects on the conjugated forms of genistin and daidzin isoflavones
    • Mathias K, Baraem I, Carlos MC, Kirby DH (2006) Heat and pH effects on the conjugated forms of genistin and daidzin isoflavones. J Agric Food Chem 54: 7495-7502.
    • (2006) J Agric Food Chem , vol.54 , pp. 7495-7502
    • Mathias, K.1    Baraem, I.2    Carlos, M.C.3    Kirby, D.H.4
  • 15
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugars
    • Miller GL (1959) Use of dinitrosalicylic acid reagent for determination of reducing sugars. Analyt Chem 31: 426-428.
    • (1959) Analyt Chem , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 17
    • 34147169561 scopus 로고    scopus 로고
    • Hydrolysis of soybean isoflavonoid glycosides by Dalbergia β-glucosidases
    • Phimonphan C, Thipwarin R, Jisnuson S, James RKC (2007b) Hydrolysis of soybean isoflavonoid glycosides by Dalbergia β-glucosidases. J Agric Food Chem 55: 2407-2412.
    • (2007) J Agric Food Chem , vol.55 , pp. 2407-2412
    • Phimonphan, C.1    Thipwarin, R.2    Jisnuson, S.3    James, R.K.C.4
  • 20
    • 0036073599 scopus 로고    scopus 로고
    • Evidence for lack of absorption of soy isoflavone glycosides in humans, supporting the crucial role of intestinal metabolism for bioavailability
    • Setchell KD, Brown NM, Zimmer-Nechemias L, Brashear WT, Wolfe BE, Kirschner AS, Heubi JE (2002) Evidence for lack of absorption of soy isoflavone glycosides in humans, supporting the crucial role of intestinal metabolism for bioavailability. Am J Clin Nutr 76: 447-453.
    • (2002) Am J Clin Nutr , vol.76 , pp. 447-453
    • Setchell, K.D.1    Brown, N.M.2    Zimmer-Nechemias, L.3    Brashear, W.T.4    Wolfe, B.E.5    Kirschner, A.S.6    Heubi, J.E.7
  • 22
    • 18344381664 scopus 로고    scopus 로고
    • Soy isoflavones and bone health: The relationship is still unclear
    • Weaver CM, Cheong JM (2005) Soy isoflavones and bone health: the relationship is still unclear. J Nutr 135: 1243-1247.
    • (2005) J Nutr , vol.135 , pp. 1243-1247
    • Weaver, C.M.1    Cheong, J.M.2
  • 23
    • 0028123353 scopus 로고
    • Comparative amino acid sequence analysis of Thermotoga maritima beta-glucosidase (BglA) deduced from the nucleotide sequence of the gene indicates distant relationship between p-glucosidases of the BGA family and other families of beta-l, 4-glycosyl hydrolases
    • Wolfgang L, Josef G, Karl-Heinz S (1994) Comparative amino acid sequence analysis of Thermotoga maritima beta-glucosidase (BglA) deduced from the nucleotide sequence of the gene indicates distant relationship between p-glucosidases of the BGA family and other families of beta-l, 4-glycosyl hydrolases. Mol Gen Genet 242: 111-115.
    • (1994) Mol Gen Genet , vol.242 , pp. 111-115
    • Wolfgang, L.1    Josef, G.2    Karl-Heinz, S.3
  • 24
    • 0029146781 scopus 로고
    • Bioavailability of soybean isoflavones depends upon gut microflora in women
    • Xu X, Hariss KS, Wang HJ, Murphy PA, Hendrich S (1995) Bioavailability of soybean isoflavones depends upon gut microflora in women. J Nutr 125: 2307-2315.
    • (1995) J Nutr , vol.125 , pp. 2307-2315
    • Xu, X.1    Hariss, K.S.2    Wang, H.J.3    Murphy, P.A.4    Hendrich, S.5
  • 25
    • 33645859900 scopus 로고    scopus 로고
    • High-level expression of an α-l-arabinofuranosidase from Thermotoga maritima in Escherichia coli for the production of xylobiose from xylan
    • Xue YM, Wu AL, Zeng HY, Shao WL (2006) High-level expression of an α-l-arabinofuranosidase from Thermotoga maritima in Escherichia coli for the production of xylobiose from xylan. Biotechnology Lett 28: 351-356.
    • (2006) Biotechnology Lett , vol.28 , pp. 351-356
    • Xue, Y.M.1    Wu, A.L.2    Zeng, H.Y.3    Shao, W.L.4
  • 26
    • 38949170567 scopus 로고    scopus 로고
    • Characterization of a thermostable extracellular β-glucosidase with activities of exoglucanase and transglycosylation from Paecilomyces thermophila
    • Yang SQ, Jiang ZQ, Yan QJ, Zhu HF (2008) Characterization of a thermostable extracellular β-glucosidase with activities of exoglucanase and transglycosylation from Paecilomyces thermophila. J Agric Food Chem 56: 602-608.
    • (2008) J Agric Food Chem , vol.56 , pp. 602-608
    • Yang, S.Q.1    Jiang, Z.Q.2    Yan, Q.J.3    Zhu, H.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.