메뉴 건너뛰기




Volumn 97, Issue 15, 2013, Pages 6749-6757

Biochemical characterization of a thermostable β-1,3-xylanase from the hyperthermophilic eubacterium, Thermotoga neapolitana strain DSM 4359

Author keywords

1,3 Xylan; 1,3 Xylanase; Hyperthermophilic bacterium; Thermostable enzyme; Thermotoga neapolitana

Indexed keywords

BIOCHEMICAL CHARACTERIZATION; BIOCHEMICAL PROPERTIES; CATALYTIC EFFICIENCIES; HYDROLYTIC ACTIVITIES; HYDROLYTIC REACTIONS; HYPERTHERMOPHILIC BACTERIA; THERMOSTABLE ENZYMES; THERMOTOGANEAPOLITANA;

EID: 84880509147     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-012-4555-5     Document Type: Article
Times cited : (22)

References (29)
  • 2
  • 3
    • 33750426204 scopus 로고    scopus 로고
    • Preparation of recombinant polysaccharide-degrading enzymes from the marine bacterium, Pseudomonas sp. ND137 for the production of protoplasts of Porphyra yezoensis
    • 10.1080/09670260600801682 1:CAS:528:DC%2BD28XhtVyisL3I
    • Aoki Y, Kamei Y (2006) Preparation of recombinant polysaccharide- degrading enzymes from the marine bacterium, Pseudomonas sp. ND137 for the production of protoplasts of Porphyra yezoensis. Eur J Phycol 41:321-328
    • (2006) Eur J Phycol , vol.41 , pp. 321-328
    • Aoki, Y.1    Kamei, Y.2
  • 4
    • 85010123518 scopus 로고
    • Purification and characterization of an endo-β-1,3-xylanase from Vibrio sp
    • 10.2331/suisan.54.277 1:CAS:528:DyaL1cXksFSmur0%3D
    • Aoki T, Araki T, Kitamikado M (1988) Purification and characterization of an endo-β-1,3-xylanase from Vibrio sp. Nippon Suisan Gakkaishi 54:277-281
    • (1988) Nippon Suisan Gakkaishi , vol.54 , pp. 277-281
    • Aoki, T.1    Araki, T.2    Kitamikado, M.3
  • 5
    • 0028254290 scopus 로고
    • Isolation and regeneration of haploid protoplasts from Bangia atropurpurea (Rhodophyta) with marine bacterial enzymes
    • 10.1111/j.0022-3646.1994.01040.x
    • Araki T, Hayakawa M, Tamaru Y, Yoshimatsu K, Morishita T (1994) Isolation and regeneration of haploid protoplasts from Bangia atropurpurea (Rhodophyta) with marine bacterial enzymes. J Phycol 30:1040-1046
    • (1994) J Phycol , vol.30 , pp. 1040-1046
    • Araki, T.1    Hayakawa, M.2    Tamaru, Y.3    Yoshimatsu, K.4    Morishita, T.5
  • 6
    • 0031771148 scopus 로고    scopus 로고
    • Purification and characterization of β-1,3-xylanase from a marine bacterium, Alcaligenes sp. XY-234
    • 12501421 10.2323/jgam.44.269 1:CAS:528:DyaK1MXislek
    • Araki T, Inoue N, Morishita T (1998) Purification and characterization of β-1,3-xylanase from a marine bacterium, Alcaligenes sp. XY-234. J Gen Appl Microbiol 44:269-274
    • (1998) J Gen Appl Microbiol , vol.44 , pp. 269-274
    • Araki, T.1    Inoue, N.2    Morishita, T.3
  • 7
    • 0033219358 scopus 로고    scopus 로고
    • Purification and characterization of β-1,3-xylanase from a marine bacterium, Vibrio sp. XY-214
    • 10635569 10.1271/bbb.63.2017 1:CAS:528:DyaK1MXnvVCktb0%3D
    • Araki T, Tani S, Maeda K, Hashikawa S, Nakagawa H, Morishita T (1999) Purification and characterization of β-1,3-xylanase from a marine bacterium, Vibrio sp. XY-214. Biosci Biotechnol Biochem 63:2017-2019
    • (1999) Biosci Biotechnol Biochem , vol.63 , pp. 2017-2019
    • Araki, T.1    Tani, S.2    Maeda, K.3    Hashikawa, S.4    Nakagawa, H.5    Morishita, T.6
  • 8
    • 0034126851 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression in Escherichia coli of the new gene encoding β-1,3-xylanase from a marine bacterium, Vibrio sp. strain XY-214
    • 10742274 10.1128/AEM.66.4.1741-1743.2000 1:CAS:528:DC%2BD3cXisVWltro%3D
    • Araki T, Hashikawa S, Morishita T (2000) Cloning, sequencing, and expression in Escherichia coli of the new gene encoding β-1,3-xylanase from a marine bacterium, Vibrio sp. strain XY-214. Appl Environ Microbiol 66:1741-1743
    • (2000) Appl Environ Microbiol , vol.66 , pp. 1741-1743
    • Araki, T.1    Hashikawa, S.2    Morishita, T.3
  • 9
    • 0000266365 scopus 로고
    • Colour reactions given by sugars and diphenylamine-aniline spray reagents on paper chromatograms
    • 10.1016/S0021-9673(01)98394-3 1:CAS:528:DyaF3MXitFOntA%3D%3D
    • Bailey RW, Bourne EJ (1960) Colour reactions given by sugars and diphenylamine-aniline spray reagents on paper chromatograms. J Chromatogr 4:206-213
    • (1960) J Chromatogr , vol.4 , pp. 206-213
    • Bailey, R.W.1    Bourne, E.J.2
  • 10
    • 0022541209 scopus 로고
    • A new sulfur-reducing, extremely thermophilic eubacterium from a submarine thermal vent
    • 16347075 1:CAS:528:DyaL28Xkt1Wnuro%3D
    • Belkin S, Wirsen CO, Jannasch HW (1986) A new sulfur-reducing, extremely thermophilic eubacterium from a submarine thermal vent. Appl Environ Microbiol 51:1180-1185
    • (1986) Appl Environ Microbiol , vol.51 , pp. 1180-1185
    • Belkin, S.1    Wirsen, C.O.2    Jannasch, H.W.3
  • 11
    • 0030466871 scopus 로고    scopus 로고
    • Mannanase A from Pseudomonas fluorescens ssp. cellulosa is a retaining glycosyl hydrolase in which E212 and E320 are the putative catalytic residues
    • 8973192 10.1021/bi961866d 1:CAS:528:DyaK28XntVyisL8%3D
    • Bolam DN, Hughes N, Virden R, Lakey JH, Hazlewood GP, Henrissat B, Braithwaite KL, Gilbert HJ (1996) Mannanase A from Pseudomonas fluorescens ssp. cellulosa is a retaining glycosyl hydrolase in which E212 and E320 are the putative catalytic residues. Biochemistry 35:16195-16204
    • (1996) Biochemistry , vol.35 , pp. 16195-16204
    • Bolam, D.N.1    Hughes, N.2    Virden, R.3    Lakey, J.H.4    Hazlewood, G.P.5    Henrissat, B.6    Braithwaite, K.L.7    Gilbert, H.J.8
  • 12
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 942051 10.1016/0003-2697(76)90527-3 1:CAS:528:DyaE28XksVehtrY%3D
    • 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
  • 13
    • 58149200943 scopus 로고    scopus 로고
    • The Carbohydrate-Active EnZymes database (CAZy): An expert resource for glycogenomics
    • 18838391 10.1093/nar/gkn663 1:CAS:528:DC%2BD1cXhsFejtL7K
    • Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, Henrissat B (2009) The Carbohydrate-Active EnZymes database (CAZy): an expert resource for glycogenomics. Nucleic Acids Res 37:D233-D238
    • (2009) Nucleic Acids Res , vol.37
    • Cantarel, B.L.1    Coutinho, P.M.2    Rancurel, C.3    Bernard, T.4    Lombard, V.5    Henrissat, B.6
  • 14
    • 0000679042 scopus 로고
    • Purification and some properties of β-1,3-xylanase from Aspergillus terreus A-07
    • 10.1271/bbb1961.50.1183 1:CAS:528:DyaL28Xkt1Srt74%3D
    • Chen WP, Matsuo M, Yasui T (1986) Purification and some properties of β-1,3-xylanase from Aspergillus terreus A-07. Agric Biol Chem 50:1183-1194
    • (1986) Agric Biol Chem , vol.50 , pp. 1183-1194
    • Chen, W.P.1    Matsuo, M.2    Yasui, T.3
  • 15
    • 23644454654 scopus 로고    scopus 로고
    • The first crystal structure of a family 31 carbohydrate-binding module with affinity to β-1,3-xylan
    • 16061225 10.1016/j.febslet.2005.06.062 1:CAS:528:DC%2BD2MXnslygtbc%3D
    • Hashimoto H, Tamai Y, Okazaki F, Tamaru Y, Shimizu T, Araki T, Sato M (2005) The first crystal structure of a family 31 carbohydrate-binding module with affinity to β-1,3-xylan. FEBS Lett 579:4324-4328
    • (2005) FEBS Lett , vol.579 , pp. 4324-4328
    • Hashimoto, H.1    Tamai, Y.2    Okazaki, F.3    Tamaru, Y.4    Shimizu, T.5    Araki, T.6    Sato, M.7
  • 16
    • 0035903165 scopus 로고    scopus 로고
    • Crystal structure of mannanase 26A from Pseudomonas cellulosa and analysis of residues involved in substrate binding
    • 11382747 10.1074/jbc.M010290200 1:CAS:528:DC%2BD3MXmsVejs7w%3D
    • Hogg D, Woo EJ, Bolam DN, McKie VA, Gilbert HJ, Pickersgill RW (2001) Crystal structure of mannanase 26A from Pseudomonas cellulosa and analysis of residues involved in substrate binding. J Biol Chem 276:31186-31192
    • (2001) J Biol Chem , vol.276 , pp. 31186-31192
    • Hogg, D.1    Woo, E.J.2    Bolam, D.N.3    McKie, V.A.4    Gilbert, H.J.5    Pickersgill, R.W.6
  • 17
    • 0002219895 scopus 로고
    • Xylan of siphonaceous green algae
    • 13852998 10.1038/187082a0 1:CAS:528:DyaF3cXhtF2gs74%3D
    • Iriki Y, Suzuki T, Nisizawa K, Miwa T (1960) Xylan of siphonaceous green algae. Nature 187:82-83
    • (1960) Nature , vol.187 , pp. 82-83
    • Iriki, Y.1    Suzuki, T.2    Nisizawa, K.3    Miwa, T.4
  • 18
    • 21744449952 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel β-1,3-xylanase possessing two putative carbohydrate-binding modules from a marine bacterium Vibrio sp. strain AX-4
    • 15743273 10.1042/BJ20050190 1:CAS:528:DC%2BD2MXkvVGhtb4%3D
    • Kiyohara M, Sakaguchi K, Yamaguchi K, Araki T, Nakamura T, Ito M (2005) Molecular cloning and characterization of a novel β-1,3-xylanase possessing two putative carbohydrate-binding modules from a marine bacterium Vibrio sp. strain AX-4. Biochem J 388:949-957
    • (2005) Biochem J , vol.388 , pp. 949-957
    • Kiyohara, M.1    Sakaguchi, K.2    Yamaguchi, K.3    Araki, T.4    Nakamura, T.5    Ito, M.6
  • 19
    • 33750706909 scopus 로고    scopus 로고
    • Structure of β-1,3-xylooligosaccharides generated from Caulerpa racemosa var. laete-virens β-1,3-xylan by the action of β-1,3-xylanase
    • 16891637 10.1093/jb/mvj173 1:CAS:528:DC%2BD28XhtFems73O
    • Kiyohara M, Hama Y, Yamaguchi K, Ito M (2006) Structure of β-1,3-xylooligosaccharides generated from Caulerpa racemosa var. laete-virens β-1,3-xylan by the action of β-1,3-xylanase. J Biochem 140:369-373
    • (2006) J Biochem , vol.140 , pp. 369-373
    • Kiyohara, M.1    Hama, Y.2    Yamaguchi, K.3    Ito, M.4
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 5432063 10.1038/227680a0 1:CAS:528:DC%2BD3MXlsFags7s%3D
    • 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
  • 21
    • 0036226314 scopus 로고    scopus 로고
    • Novel carbohydrate-binding module of β-1,3-xylanase from a marine bacterium, Alcaligenes sp strain XY-234
    • 11948152 10.1128/JB.184.9.2399-2403.2002 1:CAS:528:DC%2BD38XjvFeisrg%3D
    • Okazaki F, Tamaru Y, Hashikawa S, Li YT, Araki T (2002) Novel carbohydrate-binding module of β-1,3-xylanase from a marine bacterium, Alcaligenes sp strain XY-234. J Bacteriol 184:2399-2403
    • (2002) J Bacteriol , vol.184 , pp. 2399-2403
    • Okazaki, F.1    Tamaru, Y.2    Hashikawa, S.3    Li, Y.T.4    Araki, T.5
  • 22
    • 28644444145 scopus 로고    scopus 로고
    • The first thermodynamic characterization of β-1,3-xylanase from a marine bacterium
    • 16328734 10.1007/s10930-005-7637-8 1:CAS:528:DC%2BD2MXht1OqsbnP
    • Okazaki F, Shiraki K, Tamaru Y, Araki T, Takagi M (2005) The first thermodynamic characterization of β-1,3-xylanase from a marine bacterium. Protein J 24:413-421
    • (2005) Protein J , vol.24 , pp. 413-421
    • Okazaki, F.1    Shiraki, K.2    Tamaru, Y.3    Araki, T.4    Takagi, M.5
  • 23
    • 79960963626 scopus 로고    scopus 로고
    • Expression, crystallization and preliminary X-ray diffraction studies of thermostable β-1,3-xylanase from Thermotoga neapolitana strain DSM 4359
    • 21795792 10.1107/S1744309111017222 1:CAS:528:DC%2BC3MXptlylu70%3D
    • Okazaki F, Ogino C, Kondo A, Mikami B, Kurebayashi Y, Tsuruta H (2011) Expression, crystallization and preliminary X-ray diffraction studies of thermostable β-1,3-xylanase from Thermotoga neapolitana strain DSM 4359. Acta Crystallogr Sect F Struct Biol Cryst Commun 67:779-781
    • (2011) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.67 , pp. 779-781
    • Okazaki, F.1    Ogino, C.2    Kondo, A.3    Mikami, B.4    Kurebayashi, Y.5    Tsuruta, H.6
  • 24
    • 0026525312 scopus 로고
    • Purification and characterization of a NADH oxidase from the thermophile Thermus thermophilus HB8
    • 1577005 10.1111/j.1432-1033.1992.tb16853.x 1:CAS:528:DyaK38XksVentbc%3D
    • Park HJ, Reiser CO, Kondruweit S, Erdmann H, Schmid RD, Sprinzl M (1992) Purification and characterization of a NADH oxidase from the thermophile Thermus thermophilus HB8. Eur J Biochem 205:881-885
    • (1992) Eur J Biochem , vol.205 , pp. 881-885
    • Park, H.J.1    Reiser, C.O.2    Kondruweit, S.3    Erdmann, H.4    Schmid, R.D.5    Sprinzl, M.6
  • 25
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: Discriminating signal peptides from transmembrane regions
    • 21959131 10.1038/nmeth.1701 1:CAS:528:DC%2BC3MXht1CrtrbL
    • Petersen TN, Brunak S, von Heijne G, Nielsen H (2011) SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat Methods 8:785-786
    • (2011) Nat Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    Von Heijne, G.3    Nielsen, H.4
  • 26
    • 33750423631 scopus 로고
    • Notes on sugar determination
    • 1:CAS:528:DyaG38XivFegsw%3D%3D
    • Somogyi M (1952) Notes on sugar determination. J Biol Chem 195:19-23
    • (1952) J Biol Chem , vol.195 , pp. 19-23
    • Somogyi, M.1
  • 27
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • 7984417 10.1093/nar/22.22.4673 1:CAS:528:DyaK2MXitlSgu74%3D
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22:4673-4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 28
    • 84855341461 scopus 로고    scopus 로고
    • D-xylose isomerase from a marine bacterium, Vibrio sp. strain XY-214, and D-xylulose production from β-1,3-xylan
    • 10.1007/s10126-011-9380-9 1:CAS:528:DC%2BC38XjtFartw%3D%3D
    • Umemoto Y, Shibata T, Araki T (2012) D-xylose isomerase from a marine bacterium, Vibrio sp. strain XY-214, and D-xylulose production from β-1,3-xylan. Mar Biotechnol (NY) 14:10-20
    • (2012) Mar Biotechnol (NY) , vol.14 , pp. 10-20
    • Umemoto, Y.1    Shibata, T.2    Araki, T.3
  • 29
    • 0025407308 scopus 로고
    • Purification and some properties of endo-1,3-β-D-xylanase from Pseudomonas sp. Pt-5
    • 1368551 10.1271/bbb1961.54.921 1:CAS:528:DyaK3cXktF2qsrc%3D
    • Yamaura I, Matsumoto T, Funatsu M, Mukai E (1990) Purification and some properties of endo-1,3-β-D-xylanase from Pseudomonas sp. Pt-5. Agric Biol Chem 54:921-926
    • (1990) Agric Biol Chem , vol.54 , pp. 921-926
    • Yamaura, I.1    Matsumoto, T.2    Funatsu, M.3    Mukai, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.