메뉴 건너뛰기




Volumn 107, Issue 2, 2009, Pages 124-129

Characterization of the C-terminal truncated form of amylopullulanase from Lactobacillus plantarum L137

Author keywords

Amylopullulanase; Catalytic efficiency; Repeating amino acid sequence; Stability; Truncated forms

Indexed keywords

AMYLOPULLULANASE; C-TERMINAL REGIONS; CATALYTIC EFFICIENCY; ENZYME PRODUCTIONS; FERMENTED FOODS; LACTIC ACID BACTERIUM; LACTOBACILLUS PLANTARUM; PHILIPPINES; PULLULAN; REPEATING AMINO ACID SEQUENCE; REPEATING UNITS; SOLUBLE STARCHES; SPECIFIC ACTIVITIES; SUBSTRATE SPECIFICITIES; TRUNCATED FORMS; WILD TYPES;

EID: 60949105812     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2008.10.019     Document Type: Article
Times cited : (34)

References (35)
  • 1
    • 0002612033 scopus 로고
    • Recent advances in microbial amylases
    • Fogart W.M., and Kelly C.T. (Eds), Applied Science, London
    • Fogarty W.M., and Kelly C.T. Recent advances in microbial amylases. In: Fogart W.M., and Kelly C.T. (Eds). Microbial enzymes and biotechnology. 2nd edn. (1990), Applied Science, London 71-132
    • (1990) Microbial enzymes and biotechnology. 2nd edn. , pp. 71-132
    • Fogarty, W.M.1    Kelly, C.T.2
  • 2
    • 0001484876 scopus 로고
    • Pullulanase-amylase complex enzyme from Bacillus subtilis
    • Takasaki Y. Pullulanase-amylase complex enzyme from Bacillus subtilis. Agric. Biol. Chem. 51 (1987) 9-16
    • (1987) Agric. Biol. Chem. , vol.51 , pp. 9-16
    • Takasaki, Y.1
  • 3
    • 0028904973 scopus 로고
    • Purification and characterization of an alkaline amylopullulanase with both α-1,-4 and α-1,-6 hydrolytic activity from alkalophilic Bacillus sp. KSM-1378
    • Ara K., Saeki K., Igarashi K., Takaiwa M., Uemura T., Hagihara H., Kawai S., and Ito S. Purification and characterization of an alkaline amylopullulanase with both α-1,-4 and α-1,-6 hydrolytic activity from alkalophilic Bacillus sp. KSM-1378. Biochim. Biophys. Acta 1243 (1995) 315-324
    • (1995) Biochim. Biophys. Acta , vol.1243 , pp. 315-324
    • Ara, K.1    Saeki, K.2    Igarashi, K.3    Takaiwa, M.4    Uemura, T.5    Hagihara, H.6    Kawai, S.7    Ito, S.8
  • 4
    • 0023413269 scopus 로고
    • Cloning of the debranching-enzyme gene from Thermoanaerobium brockii into Escherichia coli and Bacillus subtilis
    • Coleman R.D., Yang S.S., and McAlister M.P. Cloning of the debranching-enzyme gene from Thermoanaerobium brockii into Escherichia coli and Bacillus subtilis. J. Bacteriol. 169 (1987) 4302-4307
    • (1987) J. Bacteriol. , vol.169 , pp. 4302-4307
    • Coleman, R.D.1    Yang, S.S.2    McAlister, M.P.3
  • 5
    • 0027257462 scopus 로고
    • Sequencing of the amylopullulanase (apu) gene of Thermoanaerobacter ethanolicus 39E, and identification of the active site by site-directed mutagenesis
    • Mathupala S.P., Lowe S.E., Podkovyrov S.M., and Zeikus J.G. Sequencing of the amylopullulanase (apu) gene of Thermoanaerobacter ethanolicus 39E, and identification of the active site by site-directed mutagenesis. J. Biol. Chem. 268 (1993) 16332-16344
    • (1993) J. Biol. Chem. , vol.268 , pp. 16332-16344
    • Mathupala, S.P.1    Lowe, S.E.2    Podkovyrov, S.M.3    Zeikus, J.G.4
  • 6
    • 0023411219 scopus 로고
    • Active-site- and substrate-specificity of Thermoanaerobium Tok6-B1 pullulanase
    • Plant A.R., Clemens R.M., Morgan H.W., and Daniel R.M. Active-site- and substrate-specificity of Thermoanaerobium Tok6-B1 pullulanase. Biochem. J. 246 (1987) 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
  • 7
    • 0028038927 scopus 로고
    • Cloning and sequencing of the Thermoanaerobacterium saccharolyticum B6A-RI apu gene and purification and characterization of the amylopullulase from Escherichia coli
    • Ramesh M.V., Podkovyrov S.M., Lowe S.E., and Zeikus J.G. Cloning and sequencing of the Thermoanaerobacterium saccharolyticum B6A-RI apu gene and purification and characterization of the amylopullulase from Escherichia coli. Appl. Environ. Microbiol. 60 (1994) 94-101
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 94-101
    • Ramesh, M.V.1    Podkovyrov, S.M.2    Lowe, S.E.3    Zeikus, J.G.4
  • 8
    • 0028146782 scopus 로고
    • Cloning of the aapT gene and characterization of its product, an amylase-pullulanase (AapT), from thermophilic and alkaliphilic Bacillus sp. strain XAL601
    • Lee S.P., Morikawa M., Takagi M., and Imanaka T. Cloning of the aapT gene and characterization of its product, an amylase-pullulanase (AapT), from thermophilic and alkaliphilic Bacillus sp. strain XAL601. Appl. Environ. Microbiol. 60 (1994) 3764-3773
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 3764-3773
    • Lee, S.P.1    Morikawa, M.2    Takagi, M.3    Imanaka, T.4
  • 10
    • 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 C.H., and Kim Y.S. 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 (1995) 687-693
    • (1995) Eur. J. Biochem. , vol.227 , pp. 687-693
    • Kim, C.H.1    Kim, Y.S.2
  • 11
    • 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., and Ito S. 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 (1996) 24075-24083
    • (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
  • 12
    • 0031991241 scopus 로고    scopus 로고
    • Purification and properties of an amylopullulanase, a glucoamylase and an α-glucosidase in the amylolytic enzyme system of Thermoanaerobacterium thermosaccharolyticum
    • Ganghofner D., Kellermann J., Staudenbauer W.L., and Bronnenmeier K. Purification and properties of an amylopullulanase, a glucoamylase and an α-glucosidase in the amylolytic enzyme system of Thermoanaerobacterium thermosaccharolyticum. Biosci. Biotechnol. Biochem. 62 (1998) 302-308
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 302-308
    • Ganghofner, D.1    Kellermann, J.2    Staudenbauer, W.L.3    Bronnenmeier, K.4
  • 13
    • 0029769634 scopus 로고    scopus 로고
    • Purification and properties of a 140 kDa amylopullulanase from the thermophilic and alkaliphilic Bacillus sp. strain TS-23
    • Lin L.-L., Tsau M.-R., and Chu W.-S. Purification and properties of a 140 kDa amylopullulanase from the thermophilic and alkaliphilic Bacillus sp. strain TS-23. Biotechnol. Appl. Biochem. 24 (1996) 101-107
    • (1996) Biotechnol. Appl. Biochem. , vol.24 , pp. 101-107
    • Lin, L.-L.1    Tsau, M.-R.2    Chu, W.-S.3
  • 14
    • 0028321448 scopus 로고
    • Pullulanase of Thermoanaerobacterium thermosulfurigenes EM1 (Clostridium thermosulfurogenes): molecular analysis of the gene, composite structure of the enzyme, and a common model for its attachment to the cell surface
    • Matuschek M., Burchhardt G., Sahm K., and Balh H. Pullulanase of Thermoanaerobacterium thermosulfurigenes EM1 (Clostridium thermosulfurogenes): molecular analysis of the gene, composite structure of the enzyme, and a common model for its attachment to the cell surface. J. Bacteriol. 176 (1994) 3295-3302
    • (1994) J. Bacteriol. , vol.176 , pp. 3295-3302
    • Matuschek, M.1    Burchhardt, G.2    Sahm, K.3    Balh, H.4
  • 15
    • 28844470263 scopus 로고    scopus 로고
    • Amylopullulanase-A novel enzyme of Lactobacillus amylophilus GV6 in direct fermentation of starch to L(+) lactic acid
    • Vishnu C., Naveena B.J., Altaf M.d., Venkateshwar M., and Reddy G. Amylopullulanase-A novel enzyme of Lactobacillus amylophilus GV6 in direct fermentation of starch to L(+) lactic acid. Enzyme Microb. Technol. 38 (2006) 545-550
    • (2006) Enzyme Microb. Technol. , vol.38 , pp. 545-550
    • Vishnu, C.1    Naveena, B.J.2    Altaf, M.d.3    Venkateshwar, M.4    Reddy, G.5
  • 16
    • 33747360729 scopus 로고    scopus 로고
    • Screening for and identification of starch-, amylopectin-, and pullulan-degrading activities in bifidobacterial strains
    • Ryan S.M., Fitzgerald G.F., and van Sinderen D. Screening for and identification of starch-, amylopectin-, and pullulan-degrading activities in bifidobacterial strains. Appl. Environ. Microbiol. 72 (2006) 5289-5296
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 5289-5296
    • Ryan, S.M.1    Fitzgerald, G.F.2    van Sinderen, D.3
  • 17
    • 57849098719 scopus 로고    scopus 로고
    • Characterization of gene encoding amylopullulanase from plant-originated lactic acid bacterium, Lactobacillus plantarum L137
    • Kim J.H., Sunako M., Ono H., Murooka Y., Fukusaki E., and Yamashita M. Characterization of gene encoding amylopullulanase from plant-originated lactic acid bacterium, Lactobacillus plantarum L137. J. Biosci. Bioeng. 106 (2008) 449-459
    • (2008) J. Biosci. Bioeng. , vol.106 , pp. 449-459
    • Kim, J.H.1    Sunako, M.2    Ono, H.3    Murooka, Y.4    Fukusaki, E.5    Yamashita, M.6
  • 18
    • 0026507005 scopus 로고
    • Lactic acid bacteria in a fermented fishery product, "burong bangus"
    • Olympia M., Ono H., Shinmyo A., and Takano M. Lactic acid bacteria in a fermented fishery product, "burong bangus". J. Ferment. Bioeng. 73 (1992) 193-197
    • (1992) J. Ferment. Bioeng. , vol.73 , pp. 193-197
    • Olympia, M.1    Ono, H.2    Shinmyo, A.3    Takano, M.4
  • 19
    • 0029131119 scopus 로고
    • Characterization of starch-hydrolyzing lactic acid bacteria isolated from a fermented fish and rice food, "burong bangus", and its amylolytic enzyme
    • Olympia M., Fukuda H., Ono H., Kaneko Y., and Takano M. Characterization of starch-hydrolyzing lactic acid bacteria isolated from a fermented fish and rice food, "burong bangus", and its amylolytic enzyme. J. Ferment. Bioeng. 80 (1995) 124-130
    • (1995) J. Ferment. Bioeng. , vol.80 , pp. 124-130
    • Olympia, M.1    Fukuda, H.2    Ono, H.3    Kaneko, Y.4    Takano, M.5
  • 21
    • 0020593886 scopus 로고
    • Simple and Rapid method for isolating large plasmid DNA from lactic streptococci
    • Anderson D.G., and McKay L.L. Simple and Rapid method for isolating large plasmid DNA from lactic streptococci. Appl. Environ. Microbiol. 46 (1983) 549-552
    • (1983) Appl. Environ. Microbiol. , vol.46 , pp. 549-552
    • Anderson, D.G.1    McKay, L.L.2
  • 22
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmid
    • Hanahan D. Studies on transformation of Escherichia coli with plasmid. J. Mol. Biol. 166 (1983) 577-580
    • (1983) J. Mol. Biol. , vol.166 , pp. 577-580
    • Hanahan, D.1
  • 23
    • 0033969932 scopus 로고    scopus 로고
    • Development of a host-vector system for Lactobacillus plantarum L137 isolated from a traditional fermented food produced in Philippines
    • Kaneko Y., Kobayashi H., Kiatpapan P., Nishimoto T., Napitupulu R., Ono H., and Murooka Y. Development of a host-vector system for Lactobacillus plantarum L137 isolated from a traditional fermented food produced in Philippines. J. Biosci. Bioeng. 89 (2000) 62-67
    • (2000) J. Biosci. Bioeng. , vol.89 , pp. 62-67
    • Kaneko, Y.1    Kobayashi, H.2    Kiatpapan, P.3    Nishimoto, T.4    Napitupulu, R.5    Ono, H.6    Murooka, Y.7
  • 24
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller G.L. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Ann. Biochem. 31 (1959) 426-428
    • (1959) Ann. Biochem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 25
    • 0001465376 scopus 로고
    • Studies on plant amylases: the effect of starch concentration upon the velocity of hydrolysis by the amylase of germinated barley
    • Hanes C.S. Studies on plant amylases: the effect of starch concentration upon the velocity of hydrolysis by the amylase of germinated barley. Biochem. J. 26 (1932) 1406-1421
    • (1932) Biochem. J. , vol.26 , pp. 1406-1421
    • Hanes, C.S.1
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0036183142 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of thermostable region of amylopullulanase gene from Thermoanaerobacter ethanolicus 39E
    • Lin F.-P., and Leu K.-L. Cloning, expression, and characterization of thermostable region of amylopullulanase gene from Thermoanaerobacter ethanolicus 39E. Appl. Biochem. Biotechnol. 97 (2002) 33-44
    • (2002) Appl. Biochem. Biotechnol. , vol.97 , pp. 33-44
    • Lin, F.-P.1    Leu, K.-L.2
  • 29
    • 0024430052 scopus 로고
    • Sequence homology between putative raw-starch binding domains from different starch-degrading enzymes
    • Svensson B., Jespersen H., Sierks M.R., and MacGregor E.A. Sequence homology between putative raw-starch binding domains from different starch-degrading enzymes. Biochem. J. 264 (1989) 309-311
    • (1989) Biochem. J. , vol.264 , pp. 309-311
    • Svensson, B.1    Jespersen, H.2    Sierks, M.R.3    MacGregor, E.A.4
  • 30
    • 0036315808 scopus 로고    scopus 로고
    • Deletion analysis of the C-terminal region of the α-amylase of Bacillus sp. strain TS-23
    • Lo H.F., Lin L.L., Chiang W.Y., Chie M.C., Hsu W.H., and Chang C.T. Deletion analysis of the C-terminal region of the α-amylase of Bacillus sp. strain TS-23. Arch. Microbiol. 178 (2002) 115-123
    • (2002) Arch. Microbiol. , vol.178 , pp. 115-123
    • Lo, H.F.1    Lin, L.L.2    Chiang, W.Y.3    Chie, M.C.4    Hsu, W.H.5    Chang, C.T.6
  • 31
    • 0034876882 scopus 로고    scopus 로고
    • Purification and properties of the catalytic domain of the thermostable pullulanase type II from Thermococcus hydrothermalis
    • Erra-Pujada M., Chang-Pi-Hin F., Debeire P., Duchiron F., and O'Donohue M.J. Purification and properties of the catalytic domain of the thermostable pullulanase type II from Thermococcus hydrothermalis. Biotechnol. Lett. 23 (2001) 1273-1277
    • (2001) Biotechnol. Lett. , vol.23 , pp. 1273-1277
    • Erra-Pujada, M.1    Chang-Pi-Hin, F.2    Debeire, P.3    Duchiron, F.4    O'Donohue, M.J.5
  • 32
    • 50649108593 scopus 로고    scopus 로고
    • Biochemical characterization of engineered amylopullulanase from Thermoanaerobacter ethanolicus 39E-implicating the non-necessity of its 100 C-terminal amino acid residues
    • Lin H.Y., Chuang H.H., and Lin F.P. Biochemical characterization of engineered amylopullulanase from Thermoanaerobacter ethanolicus 39E-implicating the non-necessity of its 100 C-terminal amino acid residues. Extremophiles 12 (2008) 641-650
    • (2008) Extremophiles , vol.12 , pp. 641-650
    • Lin, H.Y.1    Chuang, H.H.2    Lin, F.P.3
  • 33
    • 0028091811 scopus 로고
    • C-terminal truncations of thermostable Bacillus stearothermophilus α-amylase
    • Vihinen M., Peltonen T., Litia A., Suominen I., and Mantsala P. C-terminal truncations of thermostable Bacillus stearothermophilus α-amylase. Protein Eng. 7 (1994) 1255-1259
    • (1994) Protein Eng. , vol.7 , pp. 1255-1259
    • Vihinen, M.1    Peltonen, T.2    Litia, A.3    Suominen, I.4    Mantsala, P.5
  • 35
    • 0033856840 scopus 로고    scopus 로고
    • Comparative characterization of complete and truncated forms of Lactobacillus amylovorus-amylase and role of the C-terminal direct repeats in raw-starch binding
    • Rodriguez Sanoja R., Morlon-Guyot J., Jore J., Pintado J., Juge N., and Guyot J.P. Comparative characterization of complete and truncated forms of Lactobacillus amylovorus-amylase and role of the C-terminal direct repeats in raw-starch binding. Appl. Environ. Microbiol. 66 (2000) 3350-3356
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 3350-3356
    • Rodriguez Sanoja, R.1    Morlon-Guyot, J.2    Jore, J.3    Pintado, J.4    Juge, N.5    Guyot, J.P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.