메뉴 건너뛰기




Volumn 26, Issue 8, 2010, Pages 1427-1435

A cold-active β-glucosidase (Bgl1C) from a sea bacteria Exiguobacterium oxidotolerans A011

Author keywords

Glucosidase; Cold active; Exiguobacterium oxidotolerans A001; Glycoside hydrolase family 1

Indexed keywords

ACTIVE SITE; AMINO ACID SEQUENCE; COLD-ACTIVE; COLD-ACTIVE ENZYMES; DEEP SEA; GENOMIC LIBRARIES; GLUCOPYRANOSIDE; GLUCOSIDASE; GLYCOSIDE HYDROLASE FAMILY 1; MERCAPTOETHANOL; OPEN READING FRAME; OPTIMAL CONDITIONS; SPECIFIC ACTIVITY; STRUCTURAL MODELS;

EID: 77954458394     PISSN: 09593993     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11274-010-0317-7     Document Type: Article
Times cited : (23)

References (34)
  • 2
    • 0029645413 scopus 로고
    • The crystal structure of a cyanogenic β-glucosidase from white clover, a family 1 glycosyl hydrolase
    • Barrett T, Suresh CG, Tolley SP, Dodson EJ, Hughes MA (1995) The crystal structure of a cyanogenic β-glucosidase from white clover, a family 1 glycosyl hydrolase. Structure 3: 951-960.
    • (1995) Structure , vol.3 , pp. 951-960
    • Barrett, T.1    Suresh, C.G.2    Tolley, S.P.3    Dodson, E.J.4    Hughes, M.A.5
  • 3
    • 53149114173 scopus 로고    scopus 로고
    • Crystal structure of the cold-active aminopeptidase from colwellia psychrerythraea, a close structural homologue of the human bifunctional leukotriene A4 hydrolase
    • Bauvois C, Jacquamet L, Huston AL, Borel F, Feller G, Ferrer JL (2008) Crystal structure of the cold-active aminopeptidase from colwellia psychrerythraea, a close structural homologue of the human bifunctional leukotriene A4 hydrolase. J Biol Chem 283: 23315-23325.
    • (2008) J Biol Chem , vol.283 , pp. 23315-23325
    • Bauvois, C.1    Jacquamet, L.2    Huston, A.L.3    Borel, F.4    Feller, G.5    Ferrer, J.L.6
  • 4
    • 0028088841 scopus 로고
    • The biological degradation of cellulose
    • Beguin P, Aubert JP (1994) The biological degradation of cellulose. FEMS Microbiol Rev 13: 25-58.
    • (1994) FEMS Microbiol Rev , vol.13 , pp. 25-58
    • Beguin, P.1    Aubert, J.P.2
  • 5
    • 0036448608 scopus 로고    scopus 로고
    • Microbial beta-glucosidases: Cloning, properties, and applications
    • Bhatia Y, Mishra S, Bisaria VS (2002) Microbial beta-glucosidases: cloning, properties, and applications. Crit Rev Biotechnol 22: 375-407.
    • (2002) Crit Rev Biotechnol , vol.22 , pp. 375-407
    • Bhatia, Y.1    Mishra, S.2    Bisaria, V.S.3
  • 6
    • 0032007604 scopus 로고    scopus 로고
    • β-Glucosidase components of the cellulolytic system of the edible straw mushroom, Volvariella volvacea
    • Cai Y, Buswell J, Chang S (1998) β-Glucosidase components of the cellulolytic system of the edible straw mushroom, Volvariella volvacea. Enzyme Microb Tech 22: 122-129.
    • (1998) Enzyme Microb Tech , vol.22 , pp. 122-129
    • Cai, Y.1    Buswell, J.2    Chang, S.3
  • 8
    • 78651153885 scopus 로고
    • β-glucosidase system of neurospora crassai. β-glucosidase and cellulase activities of mutant and wild-type strains
    • Eberhart B, Cross D, Chase L (1964) β-glucosidase system of neurospora crassai. β-glucosidase and cellulase activities of mutant and wild-type strains. J Bacteriol 87: 761-770.
    • (1964) J Bacteriol , vol.87 , pp. 761-770
    • Eberhart, B.1    Cross, D.2    Chase, L.3
  • 10
    • 29344453545 scopus 로고    scopus 로고
    • Galacto-oligosaccharide synthesis by immobilized Aspergillus oryzae β-galactosidase
    • Gaur R, Pant H, Jain R, Khare SK (2006) Galacto-oligosaccharide synthesis by immobilized Aspergillus oryzae β-galactosidase. Food Chem 97: 426-430.
    • (2006) Food Chem , vol.97 , pp. 426-430
    • Gaur, R.1    Pant, H.2    Jain, R.3    Khare, S.K.4
  • 13
    • 0040735677 scopus 로고    scopus 로고
    • Gonzalez-Blasco G, Sanz-Aparicio J, Gonzalez B, Hermoso JA, Polaina J (2000) Directed evolution of beta-glucosidase A from Paenibacillus polymyxa to thermal resistance. J Biol Chem 275: 13012-13708.
  • 14
    • 0141538616 scopus 로고    scopus 로고
    • The use of transgenic yeasts expressing a gene encoding a glycosyl-hydrolase as a tool to increase resveratrol content in wine
    • Gonzalez-Candelas L, Gil J, Lamuela-Raventos R, Ramon D (2000) The use of transgenic yeasts expressing a gene encoding a glycosyl-hydrolase as a tool to increase resveratrol content in wine. Int J Food Microbiol 59: 179-183.
    • (2000) Int J Food Microbiol , vol.59 , pp. 179-183
    • Gonzalez-Candelas, L.1    Gil, J.2    Lamuela-Raventos, R.3    Ramon, D.4
  • 15
    • 0024659050 scopus 로고
    • Nucleotide sequence of the Clostridium thermocellum bglb gene encoding thermostable β-glucosidase b: Homology to fungal β-glucosidases
    • Gräbnitz F, Rücknagel K, Sei M, Staudenhauer W (1989) Nucleotide sequence of the Clostridium thermocellum bglb gene encoding thermostable β-glucosidase b: Homology to fungal β-glucosidases. Mol Gen Genet 217: 70-76.
    • (1989) Mol Gen Genet , vol.217 , pp. 70-76
    • Gräbnitz, F.1    Rücknagel, K.2    Sei, M.3    Staudenhauer, W.4
  • 16
    • 27744473179 scopus 로고    scopus 로고
    • Degradation of rice bran hemicellulose by Paenibacillus sp. Strain hc1: Gene cloning, characterization and function of β-d-glucosidase as an enzyme involved in degradation
    • Harada KM, Tanaka K, Fukuda Y, Hashimoto W, Murata K (2005) Degradation of rice bran hemicellulose by Paenibacillus sp. Strain hc1: gene cloning, characterization and function of β-d-glucosidase as an enzyme involved in degradation. Arch Microbiol 184: 215-224.
    • (2005) Arch Microbiol , vol.184 , pp. 215-224
    • Harada, K.M.1    Tanaka, K.2    Fukuda, Y.3    Hashimoto, W.4    Murata, K.5
  • 17
    • 0035865504 scopus 로고    scopus 로고
    • Crystal structure of a monocotyledon (maize zmglu1) β-glucosidase and a model of its complex with p-nitrophenyl β-d-thioglucoside
    • Henrissat B, Asim E (2001) Crystal structure of a monocotyledon (maize zmglu1) β-glucosidase and a model of its complex with p-nitrophenyl β-d-thioglucoside. Biochem J 354: 37-46.
    • (2001) Biochem J , vol.354 , pp. 37-46
    • Henrissat, B.1    Asim, E.2
  • 18
    • 34547597634 scopus 로고    scopus 로고
    • Crystal structures of Paenibacillus polymyxa β-glucosidase B complexes reveal the molecular basis of substrate specificity and give new insights into the catalytic machinery of family I glycosidases
    • Isorna P, Polaina J, Latorre-García L, Cañada FJ, González B, Sanz-Aparicio J (2007) Crystal structures of Paenibacillus polymyxa β-glucosidase B complexes reveal the molecular basis of substrate specificity and give new insights into the catalytic machinery of family I glycosidases. J Mol Biol 371: 1204-1218.
    • (2007) J Mol Biol , vol.371 , pp. 1204-1218
    • Isorna, P.1    Polaina, J.2    Latorre-García, L.3    Cañada, F.J.4    González, B.5    Sanz-Aparicio, J.6
  • 19
    • 0001097735 scopus 로고
    • Characterization of β-glucosidase activity in intertidal marine sediments
    • King GM (1986) Characterization of β-glucosidase activity in intertidal marine sediments. Appl Environ Microb 51: 373-380.
    • (1986) Appl Environ Microb , vol.51 , pp. 373-380
    • King, G.M.1
  • 20
    • 85004571031 scopus 로고
    • Cyclic (1 → 2)-β-d-glucan-hydrolyzing enzymes from Acremonium sp. 15 purification and some properties of endo-(1 → 2)-β-d-glucanase and β-d-glucosidase
    • Kitahata S, Sedagawa S (1987) Cyclic (1 → 2)-β-d-glucan-hydrolyzing enzymes from Acremonium sp. 15 purification and some properties of endo-(1 → 2)-β-d-glucanase and β-d-glucosidase. Agric Biol Chem 51: 2701-2708.
    • (1987) Agric Biol Chem , vol.51 , pp. 2701-2708
    • Kitahata, S.1    Sedagawa, S.2
  • 21
    • 38549170356 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of two beta-glucosidases from isoflavone glycoside-hydrolyzing bacillus subtilis natto
    • Kuo LC, Lee KT (2008) Cloning, expression, and characterization of two beta-glucosidases from isoflavone glycoside-hydrolyzing bacillus subtilis natto. J Agric Food Chem 56: 119-125.
    • (2008) J Agric Food Chem , vol.56 , pp. 119-125
    • Kuo, L.C.1    Lee, K.T.2
  • 23
    • 0037444765 scopus 로고    scopus 로고
    • Sphingomonas paucimobilis beta-glucosidase Bgl1: A member of a new bacterial subfamily in glycoside hydrolase family 1
    • Marques AR, Coutinho PM, Videira P, Fialho AM, Sá-Correia I (2003) Sphingomonas paucimobilis beta-glucosidase Bgl1: a member of a new bacterial subfamily in glycoside hydrolase family 1. Biochem J 370: 793.
    • (2003) Biochem J , vol.370 , pp. 793
    • Marques, A.R.1    Coutinho, P.M.2    Videira, P.3    Fialho, A.M.4    Sá-Correia, I.5
  • 24
    • 35548990133 scopus 로고    scopus 로고
    • Optimization of conditions for galactooligosaccharide synthesis during lactose hydrolysis by β-galactosidase from Kluyveromyces lactis (Lactozym 3000 L HP G)
    • Martinez-Villaluenga C, Cardelle-Cobas A, Corzo N, Olano A, Villamiel M (2008) Optimization of conditions for galactooligosaccharide synthesis during lactose hydrolysis by β-galactosidase from Kluyveromyces lactis (Lactozym 3000 L HP G). Food Chem 107: 258-264.
    • (2008) Food Chem , vol.107 , pp. 258-264
    • Martinez-Villaluenga, C.1    Cardelle-Cobas, A.2    Corzo, N.3    Olano, A.4    Villamiel, M.5
  • 25
    • 0028809791 scopus 로고
    • Purification and properties of a novel thermostable galacto-oligosaccharide-producing beta-galactosidase from Sterigmatomyces elviae CBS8119
    • Onishi N, Tanaka T (1995) Purification and properties of a novel thermostable galacto-oligosaccharide-producing beta-galactosidase from Sterigmatomyces elviae CBS8119. Appl Environ Microb 61: 4026.
    • (1995) Appl Environ Microb , vol.61 , pp. 4026
    • Onishi, N.1    Tanaka, T.2
  • 26
    • 28444460239 scopus 로고    scopus 로고
    • Substrate specificity and transglycosylation catalyzed by a thermostable β-glucosidase from marine hyperthermophile thermotoga neapolitana
    • Park TH, Choi KW, Park CS, Lee SB, Kang HY, Shon KJ, Park JS, Cha J (2005) Substrate specificity and transglycosylation catalyzed by a thermostable β-glucosidase from marine hyperthermophile thermotoga neapolitana. Appl Microbiol Biot 69: 411-422.
    • (2005) Appl Microbiol Biot , vol.69 , pp. 411-422
    • Park, T.H.1    Choi, K.W.2    Park, C.S.3    Lee, S.B.4    Kang, H.Y.5    Shon, K.J.6    Park, J.S.7    Cha, J.8
  • 27
    • 0032808645 scopus 로고    scopus 로고
    • Recent progress on research and applications of non-digestible galacto-oligosaccharides
    • Sako T, Matsumoto K, Tanaka R (1999) Recent progress on research and applications of non-digestible galacto-oligosaccharides. Int Dairy J 9: 69-80.
    • (1999) Int Dairy J , vol.9 , pp. 69-80
    • Sako, T.1    Matsumoto, K.2    Tanaka, R.3
  • 28
    • 0029020380 scopus 로고
    • Application of enzymes to the synthesis of surfactants
    • Sarney D, Vulfson E (1995) Application of enzymes to the synthesis of surfactants. Trends Biotechnol 13: 164-172.
    • (1995) Trends Biotechnol , vol.13 , pp. 164-172
    • Sarney, D.1    Vulfson, E.2
  • 29
    • 23744504522 scopus 로고    scopus 로고
    • Characterization of an unusual cold-active β-glucosidase belonging to family 3 of the glycoside hydrolases from the psychrophilic isolate Paenibacillus sp. strain C7
    • Shipkowski S, Brenchley JE (2005) Characterization of an unusual cold-active β-glucosidase belonging to family 3 of the glycoside hydrolases from the psychrophilic isolate Paenibacillus sp. strain C7. Appl Environ Microb 71: 4225.
    • (2005) Appl Environ Microb , vol.71 , pp. 4225
    • Shipkowski, S.1    Brenchley, J.E.2
  • 31
    • 0034830264 scopus 로고    scopus 로고
    • Mechanism of substrate inhibition in cellulose synergistic degradation
    • Valjamae P, Pettersson G, Johansson G (2001) Mechanism of substrate inhibition in cellulose synergistic degradation. Eur J Biochem 268: 520-526.
    • (2001) Eur J Biochem , vol.268 , pp. 520-526
    • Valjamae, P.1    Pettersson, G.2    Johansson, G.3
  • 32
    • 0037470085 scopus 로고    scopus 로고
    • The structure of a cold-adapted family 8 xylanase at 1.3 Å resolution. Structural adaptations to cold and investigation of the active site
    • van Petegem F, Collins T, Meuwis MA, Gerday C, Feller G, van Beeumen J (2003) The structure of a cold-adapted family 8 xylanase at 1. 3 Å resolution. Structural adaptations to cold and investigation of the active site. J Biol Chem 278: 7531-7539.
    • (2003) J Biol Chem , vol.278 , pp. 7531-7539
    • van Petegem, F.1    Collins, T.2    Meuwis, M.A.3    Gerday, C.4    Feller, G.5    van Beeumen, J.6
  • 33
    • 0034922896 scopus 로고    scopus 로고
    • Fuel ethanol production from lignocellulose: A challenge for metabolic engineering and process integration
    • Zaldivar J, Nielsen J, Olsson L (2001) Fuel ethanol production from lignocellulose: a challenge for metabolic engineering and process integration. Appl Microbiol Biotechnol 56: 17-34.
    • (2001) Appl Microbiol Biotechnol , vol.56 , pp. 17-34
    • Zaldivar, J.1    Nielsen, J.2    Olsson, L.3
  • 34
    • 0035193637 scopus 로고    scopus 로고
    • Insights into the functional architecture of the catalytic center of a maize β-glucosidase zm-p60.1
    • Zouhar J, Vevodova J, Marek J, Damborsky J, Su XD, Brzobohaty B (2001) Insights into the functional architecture of the catalytic center of a maize β-glucosidase zm-p60. 1. Plant Physiol 127: 973-985.
    • (2001) Plant Physiol , vol.127 , pp. 973-985
    • Zouhar, J.1    Vevodova, J.2    Marek, J.3    Damborsky, J.4    Su, X.D.5    Brzobohaty, B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.