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Volumn 40, Issue 2, 2007, Pages 236-241

Cold-active α-l-rhamnosidase from psychrotolerant bacteria isolated from a sub-Antarctic ecosystem

Author keywords

l Rhamnosidase; Pseudoalteromonas; Psychrotolerant; Ralstonia

Indexed keywords

BACTERIA; BIOASSAY; ECOSYSTEMS; FOOD PROCESSING; MOLECULAR DYNAMICS; REACTION KINETICS;

EID: 33751163696     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2006.04.002     Document Type: Article
Times cited : (43)

References (30)
  • 1
    • 0031608378 scopus 로고    scopus 로고
    • Molecular adaptations in psychrophilic bacteria: potential for biotechnological applications
    • Russell N.J. Molecular adaptations in psychrophilic bacteria: potential for biotechnological applications. Adv Biochem Eng Biotechnol 61 (1998) 1-21
    • (1998) Adv Biochem Eng Biotechnol , vol.61 , pp. 1-21
    • Russell, N.J.1
  • 2
    • 0034170458 scopus 로고    scopus 로고
    • Toward a molecular understanding of cold activity of enzymes from psychrophiles
    • Russell N.J. Toward a molecular understanding of cold activity of enzymes from psychrophiles. Extremophiles 4 (2000) 83-90
    • (2000) Extremophiles , vol.4 , pp. 83-90
    • Russell, N.J.1
  • 3
    • 0034997442 scopus 로고    scopus 로고
    • Structural adaptation of enzymes to low temperatures
    • Gianese G., Argos P., and Pascarella S. Structural adaptation of enzymes to low temperatures. Protein Eng 14 (2001) 141-148
    • (2001) Protein Eng , vol.14 , pp. 141-148
    • Gianese, G.1    Argos, P.2    Pascarella, S.3
  • 5
    • 0028414151 scopus 로고
    • Kinetic and inmobilization studies on fungal glycosidases for aroma enhancement in wine
    • Caldini C., Bonomi F., Pifferi P.G., Lanzarini G., and Galante Y. Kinetic and inmobilization studies on fungal glycosidases for aroma enhancement in wine. Enzyme Microb Technol 16 (1994) 286-291
    • (1994) Enzyme Microb Technol , vol.16 , pp. 286-291
    • Caldini, C.1    Bonomi, F.2    Pifferi, P.G.3    Lanzarini, G.4    Galante, Y.5
  • 6
    • 0032919809 scopus 로고    scopus 로고
    • The filamentous fungus produces Aspergillus nidulans produces an α-l-rhamnosidase of potential oenological interest
    • Orejas M., Ibáñez E., and Ramón D. The filamentous fungus produces Aspergillus nidulans produces an α-l-rhamnosidase of potential oenological interest. Lett Appl Microbiol 28 (1999) 383-388
    • (1999) Lett Appl Microbiol , vol.28 , pp. 383-388
    • Orejas, M.1    Ibáñez, E.2    Ramón, D.3
  • 7
    • 0034293707 scopus 로고    scopus 로고
    • Purification and characterization of an α-l-rhamnosidase from Pichia angusta X349
    • Yanai T., and Sato M. Purification and characterization of an α-l-rhamnosidase from Pichia angusta X349. Biosci Biotechnol Biochem 64 (2000) 2179-2185
    • (2000) Biosci Biotechnol Biochem , vol.64 , pp. 2179-2185
    • Yanai, T.1    Sato, M.2
  • 8
    • 0031573765 scopus 로고    scopus 로고
    • Purification and characterization of an α-l-rhamnosidase from Aspergillus niger
    • Manzanares P., de Graaff H., and Visser J. Purification and characterization of an α-l-rhamnosidase from Aspergillus niger. FEMS Microbiol Lett 157 (1997) 279-283
    • (1997) FEMS Microbiol Lett , vol.157 , pp. 279-283
    • Manzanares, P.1    de Graaff, H.2    Visser, J.3
  • 9
    • 0035348295 scopus 로고    scopus 로고
    • Purification and characterization of two different α-l-rhamnosidases, RhaA and RhaB, from Aspergillus aculeatus
    • Manzanares P., van den Broeck H.C., de Graaff L.H., and Visser J. Purification and characterization of two different α-l-rhamnosidases, RhaA and RhaB, from Aspergillus aculeatus. Appl Environ Microbiol 67 (2001) 2230-2234
    • (2001) Appl Environ Microbiol , vol.67 , pp. 2230-2234
    • Manzanares, P.1    van den Broeck, H.C.2    de Graaff, L.H.3    Visser, J.4
  • 10
    • 0034307497 scopus 로고    scopus 로고
    • A simple method for purifying glycosidases: α-l-rhamnopyranosidase of Aspergillus niger to increase the aroma of Moscato wine
    • Spagna G., Barbagallo R., Martino A., and Pifferi P. A simple method for purifying glycosidases: α-l-rhamnopyranosidase of Aspergillus niger to increase the aroma of Moscato wine. Enzyme Microb Technol 27 (2000) 522-530
    • (2000) Enzyme Microb Technol , vol.27 , pp. 522-530
    • Spagna, G.1    Barbagallo, R.2    Martino, A.3    Pifferi, P.4
  • 11
    • 0033199021 scopus 로고    scopus 로고
    • Biocatalysis in organic media using enzymes from extremophiles
    • Sellek G.A., and Chaudhuri J.B. Biocatalysis in organic media using enzymes from extremophiles. Enzyme Microb Technol 25 (1999) 471-482
    • (1999) Enzyme Microb Technol , vol.25 , pp. 471-482
    • Sellek, G.A.1    Chaudhuri, J.B.2
  • 12
    • 0021324568 scopus 로고
    • Improved method for detection of glycosidases in bacterial colonies
    • Paoni N., and Arroyo R. Improved method for detection of glycosidases in bacterial colonies. Appl Environ Microbiol 47 (1984) 208-209
    • (1984) Appl Environ Microbiol , vol.47 , pp. 208-209
    • Paoni, N.1    Arroyo, R.2
  • 13
    • 0036780067 scopus 로고    scopus 로고
    • Revision on taxonomic position of the xylanolytic Bacillus sp. MIR32 strain reidentified as Bacillus halodurans and plasmid mediated transformation of B. halodurans species
    • Martinez M.A., Delgado O.D., Breccia J.D., Baigori M.D., and Siñeriz F. Revision on taxonomic position of the xylanolytic Bacillus sp. MIR32 strain reidentified as Bacillus halodurans and plasmid mediated transformation of B. halodurans species. Extremophiles 6 (2002) 391-395
    • (2002) Extremophiles , vol.6 , pp. 391-395
    • Martinez, M.A.1    Delgado, O.D.2    Breccia, J.D.3    Baigori, M.D.4    Siñeriz, F.5
  • 14
    • 0033985123 scopus 로고    scopus 로고
    • Purification and characterization of intracellular α-l-rhamnosidase from Pseudomonas paucimobilis FP2001
    • Miake F., Satho T., Takesue H., Yanagida F., Kashige N., and Watanabe K. Purification and characterization of intracellular α-l-rhamnosidase from Pseudomonas paucimobilis FP2001. Arch Microbiol 173 (2000) 65-70
    • (2000) Arch Microbiol , vol.173 , pp. 65-70
    • Miake, F.1    Satho, T.2    Takesue, H.3    Yanagida, F.4    Kashige, N.5    Watanabe, K.6
  • 15
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of proteins utilizing protein-dye binding
    • Bradford M.M. A rapid and sensitive method for quantitation of microgram quantities of proteins utilizing protein-dye binding. Anal Biochem 72 (1976) 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 16
    • 0030054296 scopus 로고    scopus 로고
    • New approaches to typing and identification of bacteria using the 16S-23S rDNA spacer region
    • Gürtler V., and Stanisich V.A. New approaches to typing and identification of bacteria using the 16S-23S rDNA spacer region. Microbiology 142 (1996) 3-16
    • (1996) Microbiology , vol.142 , pp. 3-16
    • Gürtler, V.1    Stanisich, V.A.2
  • 17
    • 0032704521 scopus 로고    scopus 로고
    • Marine Pseudoalteromonas species are associated with higher organisms and produce biologically active extracellular agents
    • Holmström C., and Kjelleberg S. Marine Pseudoalteromonas species are associated with higher organisms and produce biologically active extracellular agents. FEMS Microb Ecol 30 (1999) 285-293
    • (1999) FEMS Microb Ecol , vol.30 , pp. 285-293
    • Holmström, C.1    Kjelleberg, S.2
  • 18
    • 0033802245 scopus 로고    scopus 로고
    • Antimicrobial activity of flavonoids in medicinal plants from Tafi del Valle (Tucuman, Argentina)
    • Hernandez N.E., Tereschuk M.L., and Abdala L.R. Antimicrobial activity of flavonoids in medicinal plants from Tafi del Valle (Tucuman, Argentina). J Ethnopharmacol 73 (2000) 317-322
    • (2000) J Ethnopharmacol , vol.73 , pp. 317-322
    • Hernandez, N.E.1    Tereschuk, M.L.2    Abdala, L.R.3
  • 19
    • 0036849077 scopus 로고    scopus 로고
    • The biochemistry and medical significance of the flavonoids
    • Havsteen V.H. The biochemistry and medical significance of the flavonoids. Pharmacol Therapeut 96 (2002) 67-202
    • (2002) Pharmacol Therapeut , vol.96 , pp. 67-202
    • Havsteen, V.H.1
  • 20
    • 0036035999 scopus 로고    scopus 로고
    • Viral and bacterial production in the North Water: in situ measurements, batch-culture experiments and characterization and distribution of virus-host system
    • Middelboe M., Nielsen T.G., and Bjørnsen P.K. Viral and bacterial production in the North Water: in situ measurements, batch-culture experiments and characterization and distribution of virus-host system. Deep Sea Res II 49 (2002) 5063-5079
    • (2002) Deep Sea Res II , vol.49 , pp. 5063-5079
    • Middelboe, M.1    Nielsen, T.G.2    Bjørnsen, P.K.3
  • 22
    • 0036708587 scopus 로고    scopus 로고
    • Pseudoalteromonas translucida sp. nov. and Pseudoalteromonas paragorgicola sp. nov., and emended description of the genus
    • Ivanova E.P., Sawabe T., Lysenko A., Gorshkova N., Hayashi K., Zhukova N., et al. Pseudoalteromonas translucida sp. nov. and Pseudoalteromonas paragorgicola sp. nov., and emended description of the genus. Int J Syst Evol Microbiol 52 (2002) 1759-1766
    • (2002) Int J Syst Evol Microbiol , vol.52 , pp. 1759-1766
    • Ivanova, E.P.1    Sawabe, T.2    Lysenko, A.3    Gorshkova, N.4    Hayashi, K.5    Zhukova, N.6
  • 25
    • 0037044546 scopus 로고    scopus 로고
    • Characterization of pectin subunits released by an optimised combination of enzymes
    • Bonnin E., Dolo E., Le Goff A., and Thibault J.F. Characterization of pectin subunits released by an optimised combination of enzymes. Carbohydr Res 337 (2002) 1687-1696
    • (2002) Carbohydr Res , vol.337 , pp. 1687-1696
    • Bonnin, E.1    Dolo, E.2    Le Goff, A.3    Thibault, J.F.4
  • 26
    • 0030115551 scopus 로고    scopus 로고
    • Physicochemical characteristics of flaxseed gum
    • Cui W., and Mazza G. Physicochemical characteristics of flaxseed gum. Food Res Int 29 (1996) 397-402
    • (1996) Food Res Int , vol.29 , pp. 397-402
    • Cui, W.1    Mazza, G.2
  • 27
    • 0036482883 scopus 로고    scopus 로고
    • Purification and characterization of ginsenoside-α-l-rhamnosidase
    • Hongshan Y., Jinmei G., Chunzhi Z., and Fengxie J. Purification and characterization of ginsenoside-α-l-rhamnosidase. Chem Pharmaceut Bull 50 (2002) 175-178
    • (2002) Chem Pharmaceut Bull , vol.50 , pp. 175-178
    • Hongshan, Y.1    Jinmei, G.2    Chunzhi, Z.3    Fengxie, J.4
  • 29
    • 0035021431 scopus 로고    scopus 로고
    • Purification and characterization of an alpha-l-rhamnosidase from Aspergillus terreus of interest in winemaking
    • Gallego M.V., Pinaga F., Ramon D., and Valles S. Purification and characterization of an alpha-l-rhamnosidase from Aspergillus terreus of interest in winemaking. J Food Sci 66 (2001) 204-209
    • (2001) J Food Sci , vol.66 , pp. 204-209
    • Gallego, M.V.1    Pinaga, F.2    Ramon, D.3    Valles, S.4
  • 30
    • 0002036594 scopus 로고    scopus 로고
    • Enzymes in winemaking: harnessing natural catalysts for efficient bio-transformations
    • [special issue]
    • Van Rensburg P., and Pretorius I.S. Enzymes in winemaking: harnessing natural catalysts for efficient bio-transformations. S Afr J Enol Viticult 21 (2000) [special issue]
    • (2000) S Afr J Enol Viticult , vol.21
    • Van Rensburg, P.1    Pretorius, I.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.