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Volumn 80, Issue 3, 2014, Pages 1108-1115

Novel maltotriose-hydrolyzing thermoacidophilic type III pullulan hydrolase from Thermococcus kodakarensisxs

Author keywords

[No Author keywords available]

Indexed keywords

ACETATE BUFFERS; AMYLASE ACTIVITY; CITRATE BUFFER; GLYCOSIDIC LINKAGES; HYPERTHERMOPHILIC ARCHAEON; INDUSTRIAL CONDITIONS; PULLULANASE; UNIQUE FEATURES;

EID: 84893023329     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.03139-13     Document Type: Article
Times cited : (38)

References (36)
  • 1
    • 0242575106 scopus 로고    scopus 로고
    • Biotechnological production and applications of pullulan
    • Leathers TD. 2003. Biotechnological production and applications of pullulan. Appl. Microbiol. Biotech. 62:468-473. http://dx.doi.org/10.1007/s00253-003-1386-4.
    • (2003) Appl. Microbiol. Biotech. , vol.62 , pp. 468-473
    • Leathers, T.D.1
  • 2
    • 84868259379 scopus 로고    scopus 로고
    • Pullulanase: role in starch hydrolysis and potential industrial applications
    • Hii SL, Tan JS, Ling TC, Ariff AB. 2012. Pullulanase: role in starch hydrolysis and potential industrial applications. Enzyme Res. 2012: 921362. http://dx.doi.org/10.1155/2012/921362.
    • (2012) Enzyme Res. , vol.2012 , pp. 921362
    • Hii, S.L.1    Tan, J.S.2    Ling, T.C.3    Ariff, A.B.4
  • 3
    • 0037187437 scopus 로고    scopus 로고
    • Properties and applications of starch-converting enzymes of the alpha-amylase family
    • van der Maarel MJ, van der Veen B, Uitdehaag JC, Leemhuis H, Dijkhuizen L. 2002. Properties and applications of starch-converting enzymes of the alpha-amylase family. J. Biotechnol. 94:137-155. http://dx.doi.org/10.1016/S0168-1656(01)00407-2.
    • (2002) J. Biotechnol. , vol.94 , pp. 137-155
    • van der Maarel, M.J.1    van der Veen, B.2    Uitdehaag, J.C.3    Leemhuis, H.4    Dijkhuizen, L.5
  • 5
    • 0036525719 scopus 로고    scopus 로고
    • Starch-hydrolyzing enzymes from thermophilic archaea and bacteria
    • Bertoldo C, Antranikian G. 2002. Starch-hydrolyzing enzymes from thermophilic archaea and bacteria. Curr. Opin. Chem. Biol. 6:151-160. http://dx.doi.org/10.1016/S1367-5931(02)00311-3.
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 151-160
    • Bertoldo, C.1    Antranikian, G.2
  • 6
    • 84899863334 scopus 로고    scopus 로고
    • α-Amylase: an enzyme specificity found in various families of glycoside hydrolases
    • 27 June
    • Janeček Š, Svensson B, MacGregor EA. 27 June 2013. α-Amylase: an enzyme specificity found in various families of glycoside hydrolases. Cell. Mol. Life Sci. http://dx.doi.org/10.1007/s00018-013-1388-z.
    • (2013) Cell. Mol. Life Sci.
    • Janeček, Š.1    Svensson, B.2    MacGregor, E.A.3
  • 7
    • 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. http://dx.doi.org/10.1016/S0167-4838(00)00302-2.
    • (2001) Biochim. Biophys. Acta , vol.1546 , pp. 1-20
    • MacGregor, E.A.1    Janecek, S.2    Svensson, B.3
  • 8
    • 79958849265 scopus 로고    scopus 로고
    • Purification and characterization of pullulanase from Lactococcus lactis
    • Wasko A, Polak-Berecka M, Targonski Z. 2011. Purification and characterization of pullulanase from Lactococcus lactis. Prep. Biochem. Biotechnol. 41:252-261. http://dx.doi.org/10.1080/10826068.2011.575316.
    • (2011) Prep. Biochem. Biotechnol. , vol.41 , pp. 252-261
    • Wasko, A.1    Polak-Berecka, M.2    Targonski, Z.3
  • 9
    • 84887560848 scopus 로고    scopus 로고
    • Recombinant bacterial amylopullulanases: developments and perspectives
    • Nisha M, Satyanarayana T. 2013. Recombinant bacterial amylopullulanases: developments and perspectives. Bioengineered 4(6):300-312. http: //dx.doi.org/10.4161/bioe.24629.
    • (2013) Bioengineered , vol.4 , Issue.6 , pp. 300-312
    • Nisha, M.1    Satyanarayana, T.2
  • 10
    • 0034666611 scopus 로고    scopus 로고
    • Cloning, expression and biochemical characterisation of a unique thermostable pullulanhydrolysing enzyme from the hyperthermophilic archaeon Thermococcus aggregans
    • Niehaus F, Peters A, Groudieva T, Antranikian. 2000. Cloning, expression and biochemical characterisation of a unique thermostable pullulanhydrolysing enzyme from the hyperthermophilic archaeon Thermococcus aggregans. FEMS Microbiol. Lett. 190:223-229. http://dx.doi.org/10.1111/j.1574-6968.2000.tb09290.x.
    • (2000) FEMS Microbiol. Lett. , vol.190 , pp. 223-229
    • Niehaus, F.1    Peters, A.2    Groudieva, T.3    Antranikian4
  • 11
    • 0033760418 scopus 로고    scopus 로고
    • A new thermoactive pullulanase from Desulfurococcus mucosus: cloning, sequencing, purification, and characterization of the recombinant enzyme after expression in Bacillus subtilis
    • Duffner F, Bertoldo C, Andersen JT, Wagner K, Antranikian G. 2000. A new thermoactive pullulanase from Desulfurococcus mucosus: cloning, sequencing, purification, and characterization of the recombinant enzyme after expression in Bacillus subtilis. J. Bacteriol. 182:6331-6338. http://dx .doi.org/10.1128/JB.182.22.6331-6338.2000.
    • (2000) J. Bacteriol. , vol.182 , pp. 6331-6338
    • Duffner, F.1    Bertoldo, C.2    Andersen, J.T.3    Wagner, K.4    Antranikian, G.5
  • 13
    • 84868599824 scopus 로고    scopus 로고
    • Cloning, expression, characterization, and biocatalytic investigation of a novel bacilli thermostable type I pullulanase from Bacillus sp
    • Li Y, Zhang L, Niu D, Wang Z, Shi G. 2012. Cloning, expression, characterization, and biocatalytic investigation of a novel bacilli thermostable type I pullulanase from Bacillus sp. CICIM 263. J. Agric. Food Chem. 60:11164-11172. http://dx.doi.org/10.1021/jf303109u.
    • (2012) CICIM 263. J. Agric. Food Chem. , vol.60 , pp. 11164-11172
    • Li, Y.1    Zhang, L.2    Niu, D.3    Wang, Z.4    Shi, G.5
  • 14
    • 8444239349 scopus 로고    scopus 로고
    • Description of Thermococcus kodakaraensis sp.nov., a well studied hyperthermophilic archaeon previously reported as Pyrococcus sp.
    • Atomi H, Fukui T, Kanai T, Morikawa M, Imanaka T. 2004. Description of Thermococcus kodakaraensis sp. nov., a well studied hyperthermophilic archaeon previously reported as Pyrococcus sp. KOD1. Archaea 1:263-267. http://dx.doi.org/10.1155/2004/204953.
    • (2004) KOD1. Archaea , vol.1 , pp. 263-267
    • Atomi, H.1    Fukui, T.2    Kanai, T.3    Morikawa, M.4    Imanaka, T.5
  • 15
    • 0027946790 scopus 로고
    • Purification and characterization of a thermostable thiol protease from a newly isolated hyperthermophilic Pyrococcus sp
    • Morikawa M, Izawa Y, Rashid N, Hoaki T, Imanaka T. 1994. Purification and characterization of a thermostable thiol protease from a newly isolated hyperthermophilic Pyrococcus sp. Appl. Environ. Microbiol. 60: 4559-4566.
    • (1994) Appl. Environ. Microbiol , vol.60 , pp. 4559-4566
    • Morikawa, M.1    Izawa, Y.2    Rashid, N.3    Hoaki, T.4    Imanaka, T.5
  • 16
    • 13544250517 scopus 로고    scopus 로고
    • Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes
    • Fukui T, Atomi H, Kanai T, Matsumi R, Fujiwara S, Imanaka T. 2005. Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes. Genome Res. 15:352-363. http://dx.doi.org/10.1101/gr.3003105.
    • (2005) Genome Res. , vol.15 , pp. 352-363
    • Fukui, T.1    Atomi, H.2    Kanai, T.3    Matsumi, R.4    Fujiwara, S.5    Imanaka, T.6
  • 17
    • 84878679186 scopus 로고    scopus 로고
    • Cloning, purification and biochemical characterization of an organic solvent-, detergent-, and thermo-stable amylopullulanase from Thermococcus kodakarensis KOD1
    • Guan Q, Guo X, Han T, Wei M, Jin M, Zeng F, Liu L, Li Z, Wang Y, Cheong G-W. 2013. Cloning, purification and biochemical characterization of an organic solvent-, detergent-, and thermo-stable amylopullulanase from Thermococcus kodakarensis KOD1. Process Biochem. 48:878- 884. http://dx.doi.org/10.1016/j.procbio.2013.04.007.
    • (2013) Process Biochem. , vol.48
    • Guan, Q.1    Guo, X.2    Han, T.3    Wei, M.4    Jin, M.5    Zeng, F.6    Liu, L.7    Li, Z.8    Wang, Y.9    Cheong, G.-W.10
  • 18
    • 0036181524 scopus 로고    scopus 로고
    • Characterization of an archaeal cyclodextrin glucanotransferase with a novel C-terminal domain
    • Rashid N, Cornista J, Ezaki S, Fukui T, Atomi H, Imanaka T. 2002. Characterization of an archaeal cyclodextrin glucanotransferase with a novel C-terminal domain. J. Bacteriol. 184:777-784. http://dx.doi.org/10.1128/JB.184.3.777-784.2002.
    • (2002) J. Bacteriol. , vol.184 , pp. 777-784
    • Rashid, N.1    Cornista, J.2    Ezaki, S.3    Fukui, T.4    Atomi, H.5    Imanaka, T.6
  • 19
    • 0030808181 scopus 로고    scopus 로고
    • Cloning and expression of the 4-α-glucanotransferase gene from the hyperthermophilic archaeon Pyrococcus sp
    • Tachibana Y, Fujiwara S, Takagi M, Imanaka T. 1997. Cloning and expression of the 4-α-glucanotransferase gene from the hyperthermophilic archaeon Pyrococcus sp. KOD1, and characterization of the enzyme. J. Ferment. Bioeng. 83:540-548. http://dx.doi.org/10.1016/S0922-338X(97)81134-8.
    • (1997) KOD1, and characterization of the enzyme. J. Ferment. Bioeng. , vol.83 , pp. 540-548
    • Tachibana, Y.1    Fujiwara, S.2    Takagi, M.3    Imanaka, T.4
  • 22
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall TA. 1999. BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp. Ser. 41:95-98.
    • (1999) Nucleic Acids Symp. Ser , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 23
    • 33748037939 scopus 로고
    • Amylases, alpha and beta
    • doi.10.1016/0076-6879(55)01021-5
    • Bernfeld P. 1955. Amylases, alpha and beta. Methods Enzymol. 1:149- 158. doi.10.1016/0076-6879(55)01021-5. http://dx.doi.org/10.1016/0076-6879(55)01021-5.
    • (1955) Methods Enzymol. , vol.1
    • Bernfeld, P.1
  • 24
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • Bendtsen JD, Nielsen H, von Heijne G, Brunak S. 2004. Improved prediction of signal peptides: SignalP 3.0. J. Mol. Biol. 340:783-795. http: //dx.doi.org/10.1016/j.jmb.2004.05.028.
    • (2004) J. Mol. Biol. , vol.340 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    von Heijne, G.3    Brunak, S.4
  • 25
    • 0032908691 scopus 로고    scopus 로고
    • The type II pullulanase of Thermococcus hydrothermalis: molecular characterization of the gene and expression of the catalytic domain
    • Erra-Pujada M, Debeire P, Duchiron F, O'Donohue MJ. 1999. The type II pullulanase of Thermococcus hydrothermalis: molecular characterization of the gene and expression of the catalytic domain. J. Bacteriol. 181:3284-3287.
    • (1999) J. Bacteriol , vol.181 , pp. 3284-3287
    • Erra-Pujada, M.1    Debeire, P.2    Duchiron, F.3    O'Donohue, M.J.4
  • 26
    • 0030803307 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of the gene encoding amylopullulanase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme
    • Dong G, Vieille C, Zeikus JG. 1997. Cloning, sequencing, and expression of the gene encoding amylopullulanase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme. Appl. Environ. Microbiol. 63:3577-3584.
    • (1997) Appl. Environ. Microbiol , vol.63 , pp. 3577-3584
    • Dong, G.1    Vieille, C.2    Zeikus, J.G.3
  • 27
    • 0022670999 scopus 로고
    • Comparison of amino acid sequences of eleven different α-amylases
    • Nakajima R, Imanaka T, Aiba S. 1986. Comparison of amino acid sequences of eleven different α-amylases. Appl. Microbiol. Biotechnol. 23: 355-360.
    • (1986) Appl. Microbiol. Biotechnol , vol.23 , pp. 355-360
    • Nakajima, R.1    Imanaka, T.2    Aiba, S.3
  • 28
    • 0032942009 scopus 로고    scopus 로고
    • Modes of action of acarbose hydrolysis and transglycosylation catalyzed by a thermostable maltogenic amylase, the gene for which was cloned from a Thermus strain
    • Kim T-J, Kim M-J, Kim B-C, Kim J-C, Cheong T-K, Kim J-W, Park K-H. 1999. Modes of action of acarbose hydrolysis and transglycosylation catalyzed by a thermostable maltogenic amylase, the gene for which was cloned from a Thermus strain. Appl. Environ. Microbiol. 65:1644-1651.
    • (1999) Appl. Environ. Microbiol , vol.65 , pp. 1644-1651
    • Kim, T.-J.1    Kim, M-J.2    Kim, B.-C.3    Kim, J.-C.4    Cheong, T.-K.5    Kim, J.-W.6    Park, K.-H.7
  • 29
    • 33846874322 scopus 로고    scopus 로고
    • Efficient solubilization, purification of recombinant extracellular alpha-amylase from Pyrococcus furiosus expressed as inclusion bodies in Escherichia coli
    • Wang L, Zhou Q, Chen H, Chu Z, Lu J, Zhang Y, Yang S. 2007. Efficient solubilization, purification of recombinant extracellular alpha-amylase from Pyrococcus furiosus expressed as inclusion bodies in Escherichia coli. J. Ind. Microbiol. Biotechnol. 34:187-192. http://dx.doi .org/10.1007/s10295-006-0185-1.
    • (2007) J. Ind. Microbiol. Biotechnol. , vol.34 , pp. 187-192
    • Wang, L.1    Zhou, Q.2    Chen, H.3    Chu, Z.4    Lu, J.5    Zhang, Y.6    Yang, S.7
  • 30
    • 0023411219 scopus 로고
    • Active-site-and substrate-specificity of Thermoanaerobium Tok6-B1 pullulanase
    • Plant AR, Clemens RM, Morgan HW, Daniel RM. 1987. Active-site-and substrate-specificity of Thermoanaerobium Tok6-B1 pullulanase. Biochem. J. 246:537-541.
    • (1987) Biochem. J , vol.246 , pp. 537-541
    • Plant, A.R.1    Clemens, R.M.2    Morgan, H.W.3    Daniel, R.M.4
  • 31
    • 0025012804 scopus 로고
    • Substrate competition and specificity at the active site of amylopullulanase from Clostridium thermohydrosulfuricum
    • Mathupala S, Saha BC, Zeikus JG. 1990. Substrate competition and specificity at the active site of amylopullulanase from Clostridium thermohydrosulfuricum. Biochem. Biophys. Res. Commun. 166:126-132. http: //dx.doi.org/10.1016/0006-291X(90)91920-N.
    • (1990) Biochem. Biophys. Res. Commun. , vol.166 , pp. 126-132
    • Mathupala, S.1    Saha, B.C.2    Zeikus, J.G.3
  • 32
    • 0028814170 scopus 로고
    • Substrate specificity and detailed characterization of a bifunctional amylase-pullulanase enzyme from Bacillus circulans F-2 having two different active sites on one polypeptide
    • Kim CH, Kim YS. 1995. Substrate specificity and detailed characterization of a bifunctional amylase-pullulanase enzyme from Bacillus circulans F-2 having two different active sites on one polypeptide. Eur. J. Biochem. 227:687-693. http://dx.doi.org/10.1111/j.1432-1033.1995.tb20189.x.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 687-693
    • Kim, C.H.1    Kim, Y.S.2
  • 33
    • 0029661443 scopus 로고    scopus 로고
    • Amino acid sequence and molecular structure of an alkaline amylopullulanase from Bacillus that hydrolyzes α-1, 4 and α-1, 6 linkages in polysaccharides at different active sites
    • Hatada Y, Igarashi K, Ozaki K, Ara K, Hitomi J, Kobayashi T, Kawai S, Watabe T, Ito S. 1996. Amino acid sequence and molecular structure of an alkaline amylopullulanase from Bacillus that hydrolyzes α-1, 4 and α-1, 6 linkages in polysaccharides at different active sites. J. Biol. Chem. 271: 24075-24083. http://dx.doi.org/10.1074/jbc.271.39.24075.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24075-24083
    • Hatada, Y.1    Igarashi, K.2    Ozaki, K.3    Ara, K.4    Hitomi, J.5    Kobayashi, T.6    Kawai, S.7    Watabe, T.8    Ito, S.9
  • 34
    • 0028859745 scopus 로고
    • Isolation and characterization of a heat-stable pullulanase from the hyperthermophilic archaeon Pyrococcus woesei after cloning and expression of its gene in Escherichia coli
    • Rudiger A, Jorgensen PL, Antranikian G. 1995. Isolation and characterization of a heat-stable pullulanase from the hyperthermophilic archaeon Pyrococcus woesei after cloning and expression of its gene in Escherichia coli. Appl. Environ. Microbiol. 61:567-575.
    • (1995) Appl. Environ. Microbiol , vol.61 , pp. 567-575
    • Rudiger, A.1    Jorgensen, P.L.2    Antranikian, G.3
  • 35
    • 33748668694 scopus 로고    scopus 로고
    • A novel branching enzyme of the GH-57 family in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
    • Murakami T, Kanai T, Takata H, Kuriki T, Imanaka T. 2006. A novel branching enzyme of the GH-57 family in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J. Bacteriol. 188:5915-5924. http://dx.doi.org/10.1128/JB.00390-06.
    • (2006) J. Bacteriol. , vol.188 , pp. 5915-5924
    • Murakami, T.1    Kanai, T.2    Takata, H.3    Kuriki, T.4    Imanaka, T.5
  • 36
    • 0030805437 scopus 로고    scopus 로고
    • Domain evolution in the α-amylase family
    • Janeček Š Svensson B, Henrissat B. 1997. Domain evolution in the α-amylase family. J. Mol. Evol. 45:322-331. http://dx.doi.org/10.1007 /PL00006236.
    • (1997) J. Mol. Evol. , vol.45 , pp. 322-331
    • Janeček, Š.1    Svensson, B.2    Henrissat, B.3


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