메뉴 건너뛰기




Volumn 70, Issue 6, 2015, Pages 709-725

Starch-processing enzymes - Emphasis on thermostable 4-α-glucanotransferases

Author keywords

4 glucanotransferases; amylomaltases; cyclodextrin glucanotransferase; glucoamylase; glycoside hydrolases; starch processing enzymes; amylase; amylase

Indexed keywords


EID: 84938338907     PISSN: 00063088     EISSN: 13369563     Source Type: Journal    
DOI: 10.1515/biolog-2015-0087     Document Type: Review
Times cited : (13)

References (172)
  • 3
    • 52949126711 scopus 로고    scopus 로고
    • Purification and characterization of a cyclomaltodextrin glucanotransferase from Paenibacillus campinasensis strain H69-3
    • Alves-Prado H.F., Gomes E. & da Silva R. 2007. Purification and characterization of a cyclomaltodextrin glucanotransferase from Paenibacillus campinasensis strain H69-3. Appl. Biochem. Biotechnol. 140: 41-55.
    • (2007) Appl. Biochem. Biotechnol. , vol.140 , pp. 41-55
    • Alves-Prado, H.F.1    Gomes, E.2    Da Silva, R.3
  • 4
    • 84938403934 scopus 로고    scopus 로고
    • 8th Edition. Corn Refiners Association. Washington, D.C.
    • Anonymous 2006. Nutritive sweeteners from corn. 8th Edition. Corn Refiners Association. Washington, D.C.; http://www. corn.org/wp-content/uploads/2009/12/NSFC2006.pdf.
    • (2006) Nutritive Sweeteners from Corn
    • Anonymous1
  • 6
    • 58049221152 scopus 로고    scopus 로고
    • A novel thermophilic anaerobic bacteria producing cyclodextrin glycosyltransferase
    • Avci A. & Dönmez S. 2009. A novel thermophilic anaerobic bacteria producing cyclodextrin glycosyltransferase. Process Biochem. 44: 36-42.
    • (2009) Process Biochem. , vol.44 , pp. 36-42
    • Avci, A.1    Dönmez, S.2
  • 7
    • 84924027342 scopus 로고    scopus 로고
    • Purification and characterization of a thermostable cyclodextrin glycosyltransferase from Thermoanaerobacter sp. P4
    • Avci A. & Dönmez S. 2012. Purification and characterization of a thermostable cyclodextrin glycosyltransferase from Thermoanaerobacter sp. P4. Afr. J. Biotechnol. 11: 10407-10415.
    • (2012) Afr. J. Biotechnol. , vol.11 , pp. 10407-10415
    • Avci, A.1    Dönmez, S.2
  • 9
    • 34447132905 scopus 로고    scopus 로고
    • Three-way stabilization of the covalent intermediate in amylomaltase, an α-amylaselike transglycosylase
    • Barends T.R., Bultema J.B., Kaper T., van der Maarel M.J., Dijkhuizen L. & Dijkstra B.W. 2007. Three-way stabilization of the covalent intermediate in amylomaltase, an α-amylaselike transglycosylase. J. Biol. Chem. 282: 17242-17249.
    • (2007) J. Biol. Chem. , vol.282 , pp. 17242-17249
    • Barends, T.R.1    Bultema, J.B.2    Kaper, T.3    Van Der Maarel, M.J.4    Dijkhuizen, L.5    Dijkstra, B.W.6
  • 10
    • 14844332702 scopus 로고    scopus 로고
    • Bioresco, Bioresearch Management and Consulting Ltd.
    • Bär A. 2000. Trehalose produced by a novel enzymatic process. Bioresco, Bioresearch Management and Consulting Ltd., http://acnfp.food.gov.uk/sites/default/files/mnt/drupal data/sources/files/ multimedia/pdfs/0 1.pdf.
    • (2000) Trehalose Produced by A Novel Enzymatic Process
    • Bär, A.1
  • 11
    • 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.
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 151-160
    • Bertoldo, C.1    Antranikian, G.2
  • 12
    • 0037375065 scopus 로고    scopus 로고
    • A cycloamyloseforming hyperthermostable 4-α-glucanotransferase of Aquifex aeolicus expressed in Escherichia coli
    • Bhuiyan S.H., Kitaoka M. & Hayashi K. 2003. A cycloamyloseforming hyperthermostable 4-α-glucanotransferase of Aquifex aeolicus expressed in Escherichia coli. J. Mol. Catal. B Enzymatic 22: 45-53.
    • (2003) J. Mol. Catal. B Enzymatic , vol.22 , pp. 45-53
    • Bhuiyan, S.H.1    Kitaoka, M.2    Hayashi, K.3
  • 14
    • 84860839630 scopus 로고    scopus 로고
    • Sequence fingerprints of enzyme specificities from the glycoside hydrolase family GH57
    • Blesak K. & Janeček Š. 2012. Sequence fingerprints of enzyme specificities from the glycoside hydrolase family GH57. Extremophiles 16: 497-506.
    • (2012) Extremophiles , vol.16 , pp. 497-506
    • Blesak, K.1    Janeček, S.2
  • 16
    • 0035443118 scopus 로고    scopus 로고
    • Glycoside hydrolases and glycosyltransferases: Families and functional modules
    • Bourne Y. & Henrissat B. 2001. Glycoside hydrolases and glycosyltransferases: families and functional modules. Curr. Opin. Struct. Biol. 11: 593-600.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 593-600
    • Bourne, Y.1    Henrissat, B.2
  • 17
    • 0002874339 scopus 로고
    • Solution of the structure of Aspergillus Niger acid α-amylase by combined molecular replacement and multiple isomorphous replacement methods
    • Brady R., Brzozowski A., Derewenda Z., Dodson E. & Dodson G. 1991. Solution of the structure of Aspergillus Niger acid α-amylase by combined molecular replacement and multiple isomorphous replacement methods. Acta Crystallogr. B 47: 527-535.
    • (1991) Acta Crystallogr. B , vol.47 , pp. 527-535
    • Brady, R.1    Brzozowski, A.2    Derewenda, Z.3    Dodson, E.4    Dodson, G.5
  • 18
    • 0029111443 scopus 로고
    • The structure of human pancreatic α-amylase at 1.8 °a resolution and comparisons with related enzymes
    • Brayer G.D., Luo Y. & Withers S.G. 1995. The structure of human pancreatic α-amylase at 1.8 °A resolution and comparisons with related enzymes. Protein Sci. 4: 1730-1742.
    • (1995) Protein Sci. , vol.4 , pp. 1730-1742
    • Brayer, G.D.1    Luo, Y.2    Withers, S.G.3
  • 19
    • 58149200943 scopus 로고    scopus 로고
    • The Carbohydrate-Active EnZymes database (CAZy): An expert resource for glycogenomics
    • Database Issue
    • Cantarel B.L., Coutinho P.M., Rancurel C., Bernard T., Lombard V. & Henrissat B. 2009. The Carbohydrate-Active EnZymes database (CAZy): an expert resource for glycogenomics. Nucleic Acids Res. 37 (Database Issue): D233-D238.
    • (2009) Nucleic Acids Res. , vol.37 , pp. D233-D238
    • Cantarel, B.L.1    Coutinho, P.M.2    Rancurel, C.3    Bernard, T.4    Lombard, V.5    Henrissat, B.6
  • 20
    • 34249742691 scopus 로고    scopus 로고
    • Cloning and expression of cyclodextrin glycosyltransferase gene from Paenibacillus sp. T16 isolated from hot spring soil in northern Thailand
    • Charoensakdi R., Murakami S., Aoki K., Rimphanitchayakit V. & Limpaseni T. 2007. Cloning and expression of cyclodextrin glycosyltransferase gene from Paenibacillus sp. T16 isolated from hot spring soil in northern Thailand. J. Biochem. Mol. Biol. 40: 333-340.
    • (2007) J. Biochem. Mol. Biol. , vol.40 , pp. 333-340
    • Charoensakdi, R.1    Murakami, S.2    Aoki, K.3    Rimphanitchayakit, V.4    Limpaseni, T.5
  • 22
    • 0034997496 scopus 로고    scopus 로고
    • A critical role for disproportionating enzyme in starch breakdown is revealed by a knock-out mutation in Arabidopsis
    • Critchley J.H., Zeeman S.C., Takaha T., Smith A.M. & Smith S.M. 2001. A critical role for disproportionating enzyme in starch breakdown is revealed by a knock-out mutation in Arabidopsis. Plant J. 26: 89-100.
    • (2001) Plant J. , vol.26 , pp. 89-100
    • Critchley, J.H.1    Zeeman, S.C.2    Takaha, T.3    Smith, A.M.4    Smith, S.M.5
  • 23
    • 1942470488 scopus 로고    scopus 로고
    • Cyclodextrins and their uses: A review
    • Del Valle E.M. 2004. Cyclodextrins and their uses: a review. Process Biochem. 39: 1033-1046.
    • (2004) Process Biochem. , vol.39 , pp. 1033-1046
    • Del Valle, E.M.1
  • 24
    • 0025997060 scopus 로고
    • Effect of limited proteolysis in the 8th loop of the barrel and of antibodies on porcine pancreas amylase activity
    • Desseaux V., Payan F., Ajandouz E.H., Svensson B., Haser R. & Marchis-Mouren G. 1991. Effect of limited proteolysis in the 8th loop of the barrel and of antibodies on porcine pancreas amylase activity. Biochim Biophys. Acta 1080: 237-244.
    • (1991) Biochim Biophys. Acta , vol.1080 , pp. 237-244
    • Desseaux, V.1    Payan, F.2    Ajandouz, E.H.3    Svensson, B.4    Haser, R.5    Marchis-Mouren, G.6
  • 26
    • 0042628136 scopus 로고    scopus 로고
    • Isolation of Paenibacillus illinoisensis that produces cyclodextrin glucanotransferase resistant to organic solvents
    • Doukyu N., Kuwahara H. & Aono R. 2003. Isolation of Paenibacillus illinoisensis that produces cyclodextrin glucanotransferase resistant to organic solvents. Biosci. Biotechnol. Biochem. 67: 334-340.
    • (2003) Biosci. Biotechnol. Biochem. , vol.67 , pp. 334-340
    • Doukyu, N.1    Kuwahara, H.2    Aono, R.3
  • 27
    • 0032571332 scopus 로고    scopus 로고
    • Crystal structure of a catalytic-site mutant α-amylase from Bacillus subtilis complexed with maltopentaose
    • Fujimoto Z., Takase K., Doui N., Momma M., Matsumoto T. & Mizuno H. 1998. Crystal structure of a catalytic-site mutant α-amylase from Bacillus subtilis complexed with maltopentaose. J. Mol. Biol. 277: 393-407.
    • (1998) J. Mol. Biol. , vol.277 , pp. 393-407
    • Fujimoto, Z.1    Takase, K.2    Doui, N.3    Momma, M.4    Matsumoto, T.5    Mizuno, H.6
  • 28
    • 0026478671 scopus 로고
    • Cyclization characteristics of cyclodextrin glucanotransferase are conferred by the NH2-terminal region of the enzyme
    • Fujiwara S., Kakihara H., Woo K.B., Lejeune A., Kanemoto M., Sakaguchi K. & Imanaka T. 1992. Cyclization characteristics of cyclodextrin glucanotransferase are conferred by the NH2-terminal region of the enzyme. Appl. Environ. Microbiol. 58: 4016-4025.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 4016-4025
    • Fujiwara, S.1    Kakihara, H.2    Woo, K.B.3    Lejeune, A.4    Kanemoto, M.5    Sakaguchi, K.6    Imanaka, T.7
  • 29
    • 48549105103 scopus 로고    scopus 로고
    • β-Amylase4, a noncatalytic protein required for starch breakdown, acts upstream of three active β-amylases in Arabidopsis chloroplasts
    • Fulton D.C., Stettler M., Mettler T., Vaughan C.K., Li J., Francisco P., Gil M., Reinhold H., Eicke S. & Messerli G. 2008. β-Amylase4, a noncatalytic protein required for starch breakdown, acts upstream of three active β-amylases in Arabidopsis chloroplasts. Plant Cell 20: 1040-1058.
    • (2008) Plant Cell , vol.20 , pp. 1040-1058
    • Fulton, D.C.1    Stettler, M.2    Mettler, T.3    Vaughan, C.K.4    Li, J.5    Francisco, P.6    Gil, M.7    Reinhold, H.8    Eicke, S.9    Messerli, G.10
  • 30
    • 66149083223 scopus 로고    scopus 로고
    • Shelf life of packaged bakery goods - A review
    • Galic K., Curic D. & Gabric D. 2009. Shelf life of packaged bakery goods - a review. Crit. Rev. Food. Sci. 49: 405-426.
    • (2009) Crit. Rev. Food. Sci. , vol.49 , pp. 405-426
    • Galic, K.1    Curic, D.2    Gabric, D.3
  • 31
    • 0032952120 scopus 로고    scopus 로고
    • Purification and properties of a novel raw starch degrading cyclomaltodextrin glucanotransferase from Bacillus firmus
    • Gawande B.N., Goel A., Patkar A.Y. & Nene S.N. 1999. Purification and properties of a novel raw starch degrading cyclomaltodextrin glucanotransferase from Bacillus firmus. Appl. Microbiol. Biotechnol. 51: 504-509.
    • (1999) Appl. Microbiol. Biotechnol. , vol.51 , pp. 504-509
    • Gawande, B.N.1    Goel, A.2    Patkar, A.Y.3    Nene, S.N.4
  • 32
    • 0030730274 scopus 로고    scopus 로고
    • Molecular analysis of a Clostridium butyricum NCIMB 7423 gene encoding 4-α-glucanotransferase and characterization of the recombinant enzyme produced in Escherichia coli
    • Goda S.K., Eissa O., Akhtar M. & Minton N.P. 1997. Molecular analysis of a Clostridium butyricum NCIMB 7423 gene encoding 4-α-glucanotransferase and characterization of the recombinant enzyme produced in Escherichia coli. Microbiology 143: 3287-3294.
    • (1997) Microbiology , vol.143 , pp. 3287-3294
    • Goda, S.K.1    Eissa, O.2    Akhtar, M.3    Minton, N.P.4
  • 33
    • 44649096836 scopus 로고    scopus 로고
    • The unique glycoside hydrolase family 77 amylomaltase from Borrelia burgdorferi with only catalytic triad conserved
    • Godany A., Vidova B. & Janeček Š. 2008. The unique glycoside hydrolase family 77 amylomaltase from Borrelia burgdorferi with only catalytic triad conserved. FEMS Microbiol. Lett. 284: 84-91.
    • (2008) FEMS Microbiol. Lett. , vol.284 , pp. 84-91
    • Godany, A.1    Vidova, B.2    Janeček, S.3
  • 35
    • 0001148160 scopus 로고
    • Nucleotide sequence of the cyclomaltodextrin glucanotransferase (CGTase) gene from alkalophilic Bacillus sp. Strain No. 38-2
    • Hamamoto T., Kaneko T. & Horikoshi K. 1987. Nucleotide sequence of the cyclomaltodextrin glucanotransferase (CGTase) gene from alkalophilic Bacillus sp. strain No. 38-2. Agric. Biol. Chem. 51: 2019-2022.
    • (1987) Agric. Biol. Chem. , vol.51 , pp. 2019-2022
    • Hamamoto, T.1    Kaneko, T.2    Horikoshi, K.3
  • 36
    • 0030513264 scopus 로고    scopus 로고
    • X-ray structure of cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011. Comparison of two independent molecules at 1.8 °a resolution
    • Harata K., Haga K., Nakamura A., Aoyagi M. & Yamane K. 1996. X-ray structure of cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011. Comparison of two independent molecules at 1.8 °A resolution. Acta Crystallogr. D Biol. Crystallogr. 52: 1136-1145.
    • (1996) Acta Crystallogr. D Biol. Crystallogr. , vol.52 , pp. 1136-1145
    • Harata, K.1    Haga, K.2    Nakamura, A.3    Aoyagi, M.4    Yamane, K.5
  • 37
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B. 1991. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280: 309-316.
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 38
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B. & Bairoch A. 1993. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 293: 781-788.
    • (1993) Biochem. J. , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 39
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hydrolases
    • Henrissat B. & Bairoch A. 1996. Updating the sequence-based classification of glycosyl hydrolases. Biochem. J. 316: 695-696.
    • (1996) Biochem. J. , vol.316 , pp. 695-696
    • Henrissat, B.1    Bairoch, A.2
  • 40
    • 0035145163 scopus 로고    scopus 로고
    • Classification of glycoside hydrolases and glycosyltransferases from hyperthermophiles
    • Henrissat B. & Coutinho P.M. 2001. Classification of glycoside hydrolases and glycosyltransferases from hyperthermophiles. Method. Enzymol. 330: 183-201.
    • (2001) Method. Enzymol. , vol.330 , pp. 183-201
    • Henrissat, B.1    Coutinho, P.M.2
  • 41
    • 0036664543 scopus 로고    scopus 로고
    • Novel functions and applications of trehalose
    • Higashiyama T. 2002. Novel functions and applications of trehalose. Pure Appl. Chem. 74: 1263-1269.
    • (2002) Pure Appl. Chem. , vol.74 , pp. 1263-1269
    • Higashiyama, T.1
  • 43
    • 84878663941 scopus 로고    scopus 로고
    • Sweeteners from starch: Production, properties and uses
    • BeMiller J.N. & Whistler R.L. (eds), 3rd Ed., Academic Press, Elsevier, London
    • Hobbs L. 2009. Sweeteners from starch: production, properties and uses, pp.: 797-832. In: BeMiller J.N. & Whistler R.L. (eds), Starch Chemistry and Technology, 3rd Ed., Academic Press, Elsevier, London.
    • (2009) Starch Chemistry and Technology , pp. 797-832
    • Hobbs, L.1
  • 44
    • 0025239538 scopus 로고
    • Random mutagenesis used to probe the structure and function of Bacillus stearothermophilus α-amylase
    • Holm L., Koivula A.K., Lehtovaara P.M., Hemminki A. & Knowles J.K. 1990. Random mutagenesis used to probe the structure and function of Bacillus stearothermophilus α-amylase. Protein Eng. 3: 181-191.
    • (1990) Protein Eng. , vol.3 , pp. 181-191
    • Holm, L.1    Koivula, A.K.2    Lehtovaara, P.M.3    Hemminki, A.4    Knowles, J.K.5
  • 45
    • 0037423706 scopus 로고    scopus 로고
    • Three-dimensional structure and substrate binding of Bacillus stearothermophilus neopullulanase
    • Hondoh H., Kuriki T. & Matsuura Y. 2003. Three-dimensional structure and substrate binding of Bacillus stearothermophilus neopullulanase. J. Mol. Biol. 326: 177-188.
    • (2003) J. Mol. Biol. , vol.326 , pp. 177-188
    • Hondoh, H.1    Kuriki, T.2    Matsuura, Y.3
  • 46
    • 0035899987 scopus 로고    scopus 로고
    • Identification of the catalytic residue of Thermococcus litoralis 4-α-glucanotransferase through mechanism-based labeling
    • Imamura H., Fushinobu S., Jeon B.S.,Wakagi T. & Matsuzawa H. 2001. Identification of the catalytic residue of Thermococcus litoralis 4-α-glucanotransferase through mechanism-based labeling. Biochemistry 40: 12400-12406.
    • (2001) Biochemistry , vol.40 , pp. 12400-12406
    • Imamura, H.1    Fushinobu, S.2    Jeon, B.S.3    Wakagi, T.4    Matsuzawa, H.5
  • 47
    • 0038143285 scopus 로고    scopus 로고
    • Crystal structures of 4-α-glucanotransferase from Thermococcus litoralis and its complex with an inhibitor
    • Imamura H., Fushinobu S., Yamamoto M., Kumasaka T., Jeon B.S., Wakagi T. & Matsuzawa H. 2003. Crystal structures of 4-α-glucanotransferase from Thermococcus litoralis and its complex with an inhibitor. J. Biol. Chem. 278: 19378-19386.
    • (2003) J. Biol. Chem. , vol.278 , pp. 19378-19386
    • Imamura, H.1    Fushinobu, S.2    Yamamoto, M.3    Kumasaka, T.4    Jeon, B.S.5    Wakagi, T.6    Matsuzawa, H.7
  • 48
    • 0029619220 scopus 로고
    • Close evolutionary relatedness among functionally distantly related members of the (α/β)8-barrel glycosyl hydrolases suggested by the similarity of their fifth conserved sequence region
    • Janeček Š. 1995. Close evolutionary relatedness among functionally distantly related members of the (α/β)8-barrel glycosyl hydrolases suggested by the similarity of their fifth conserved sequence region. FEBS Lett. 377: 6-8.
    • (1995) FEBS Lett. , vol.377 , pp. 6-8
    • Janeček, S.1
  • 49
    • 0012286188 scopus 로고    scopus 로고
    • How many conserved sequence regions are there in the α-amylase family?
    • Janeček Š. 2002. How many conserved sequence regions are there in the α-amylase family? Biologia 57 (Suppl 11): 29-41.
    • (2002) Biologia , vol.57 , pp. 29-41
    • Janeček, S.1
  • 50
    • 33748670795 scopus 로고    scopus 로고
    • Amylolytic families of glycoside hydrolases: Focus on the family GH-57
    • Janeček Š. 2005. Amylolytic families of glycoside hydrolases: focus on the family GH-57. Biologia 60 (Suppl 16): 177-184.
    • (2005) Biologia , vol.60 , pp. 177-184
    • Janeček, S.1
  • 51
    • 77955094931 scopus 로고    scopus 로고
    • Amylolytic enzymes-focus on the α-amylases from archaea and plants
    • Janeček Š. 2009. Amylolytic enzymes-focus on the α-amylases from archaea and plants. Nova Biotechnol. 9: 5-25.
    • (2009) Nova Biotechnol. , vol.9 , pp. 5-25
    • Janeček, S.1
  • 52
    • 84866630737 scopus 로고    scopus 로고
    • In silico identification of catalytic residues and domain fold of the family GH119 sharing the catalytic machinery with the α-amylase family GH57
    • Janeček Š. & Kuchtova A. 2012. In silico identification of catalytic residues and domain fold of the family GH119 sharing the catalytic machinery with the α-amylase family GH57. FEBS Lett. 586: 3360-3366.
    • (2012) FEBS Lett. , vol.586 , pp. 3360-3366
    • Janeček, S.1    Kuchtova, A.2
  • 53
  • 54
    • 33847261709 scopus 로고    scopus 로고
    • A β-cyclodextrin glycosyltransferase from a newly isolated Paenibacillus pabuli US132 strain: Purification, properties and potential use in bread-making
    • Jemli S., Messaoud E.B., Ayadi-Zouari D., Naili B., Khemakhem B. & Bejar S. 2007. A β-cyclodextrin glycosyltransferase from a newly isolated Paenibacillus pabuli US132 strain: purification, properties and potential use in bread-making. Biochem. Eng. J. 34: 44-50.
    • (2007) Biochem. Eng. J. , vol.34 , pp. 44-50
    • Jemli, S.1    Messaoud, E.B.2    Ayadi-Zouari, D.3    Naili, B.4    Khemakhem, B.5    Bejar, S.6
  • 55
    • 0030738673 scopus 로고    scopus 로고
    • 4-α-Glucanotransferase from the hyperthermophilic archaeon Thermococcus litoralis
    • Jeon B.S., Taguchi H., Sakai H., Ohshima T., Wakagi T. & Matsuzawa H. 1997. 4-α-Glucanotransferase from the hyperthermophilic archaeon Thermococcus litoralis. Eur. J. Biochem. 248: 171-178.
    • (1997) Eur. J. Biochem. , vol.248 , pp. 171-178
    • Jeon, B.S.1    Taguchi, H.2    Sakai, H.3    Ohshima, T.4    Wakagi, T.5    Matsuzawa, H.6
  • 56
    • 0026040317 scopus 로고
    • Comparison of the domain-level organization of starch hydrolases and related enzymes
    • Jespersen H., MacGregor E.A., Sierks M. & Svensson B. 1991. Comparison of the domain-level organization of starch hydrolases and related enzymes. Biochem. J. 280: 51-55.
    • (1991) Biochem. J. , vol.280 , pp. 51-55
    • Jespersen, H.1    MacGregor, E.A.2    Sierks, M.3    Svensson, B.4
  • 57
    • 0030662111 scopus 로고    scopus 로고
    • Cloning and nucleotide sequence of a thermostable cyclodextrin glycosyltransferase gene from Thermoanaerobacter sp. ATCC 53627 and its expression in Escherichia coli
    • Jorgensen S., Tangney M., Starnes R., Amemiya K. & Jorgensen P. 1997. Cloning and nucleotide sequence of a thermostable cyclodextrin glycosyltransferase gene from Thermoanaerobacter sp. ATCC 53627 and its expression in Escherichia coli. Biotechnol. Lett. 19: 1027-1031.
    • (1997) Biotechnol. Lett. , vol.19 , pp. 1027-1031
    • Jorgensen, S.1    Tangney, M.2    Starnes, R.3    Amemiya, K.4    Jorgensen, P.5
  • 58
    • 78650789668 scopus 로고    scopus 로고
    • Structural and functional analysis of substrate recognition by the 250s loop in amylomaltase from Thermus brockianus
    • Jung J.H., Jung T.Y., Seo D.H., Yoon S.M., Choi H.C., Park B.C., Park C.S. & Woo E.J. 2011. Structural and functional analysis of substrate recognition by the 250s loop in amylomaltase from Thermus brockianus. Proteins 79: 633-644.
    • (2011) Proteins , vol.79 , pp. 633-644
    • Jung, J.H.1    Jung, T.Y.2    Seo, D.H.3    Yoon, S.M.4    Choi, H.C.5    Park, B.C.6    Park, C.S.7    Woo, E.J.8
  • 59
    • 84863239712 scopus 로고    scopus 로고
    • Association of novel domain in active site of archaic hyperthermophilic maltogenic amylase from Staphylothermus marinus
    • Jung T.Y., Li D., Park J.T., Yoon S.M., Tran P.L., Oh B.H., Janecek S., Park S.G., Woo E.J. & Park K.H. 2012. Association of novel domain in active site of archaic hyperthermophilic maltogenic amylase from Staphylothermus marinus. J. Biol. Chem. 287: 7979-7989.
    • (2012) J. Biol. Chem. , vol.287 , pp. 7979-7989
    • Jung, T.Y.1    Li, D.2    Park, J.T.3    Yoon, S.M.4    Tran, P.L.5    Oh, B.H.6    Janecek, S.7    Park, S.G.8    Woo, E.J.9    Park, K.H.10
  • 60
    • 0028229326 scopus 로고
    • Crystal and molecular structure of barley α-amylase
    • Kadziola A., Abe J.i., Svensson B. & Haser R. 1994. Crystal and molecular structure of barley α-amylase. J. Mol. Biol. 239: 104-121.
    • (1994) J. Mol. Biol. , vol.239 , pp. 104-121
    • Kadziola, A.1    Abe, J.I.2    Svensson, B.3    Haser, R.4
  • 61
    • 0036304348 scopus 로고    scopus 로고
    • Crystal structures and structural comparison of Thermoactinomyces vulgaris R-47 α-amylase 1 (TVAI) at 1.6 °a resolution and α-amylase 2 (TVAII) at 2.3 °a resolution
    • Kamitori S., Abe A., Ohtaki A., Kaji A., Tonozuka T. & Sakano Y. 2002. Crystal structures and structural comparison of Thermoactinomyces vulgaris R-47 α-amylase 1 (TVAI) at 1.6 °A resolution and α-amylase 2 (TVAII) at 2.3 °A resolution. J. Mol. Biol. 318: 443-453.
    • (2002) J. Mol. Biol. , vol.318 , pp. 443-453
    • Kamitori, S.1    Abe, A.2    Ohtaki, A.3    Kaji, A.4    Tonozuka, T.5    Sakano, Y.6
  • 62
    • 0033574502 scopus 로고    scopus 로고
    • Crystal structure of Thermoactinomyces vulgaris R-47 α-amylase II (TVAII) hydrolyzing cyclodextrins and pullulan at 2.6 °a resolution
    • Kamitori S., Kondo S., Okuyama K., Yokota T., Shimura Y., Tonozuka T. & Sakano Y. 1999. Crystal structure of Thermoactinomyces vulgaris R-47 α-amylase II (TVAII) hydrolyzing cyclodextrins and pullulan at 2.6 °A resolution. J. Mol. Biol. 287: 907-921.
    • (1999) J. Mol. Biol. , vol.287 , pp. 907-921
    • Kamitori, S.1    Kondo, S.2    Okuyama, K.3    Yokota, T.4    Shimura, Y.5    Tonozuka, T.6    Sakano, Y.7
  • 63
    • 12144255190 scopus 로고    scopus 로고
    • Identification of Pyrococcus furiosus amylopullulanase catalytic residues
    • Kang S., Vieille C. & Zeikus J. 2005. Identification of Pyrococcus furiosus amylopullulanase catalytic residues. Appl.Microbiol. Biotechnol. 66: 408-413.
    • (2005) Appl.Microbiol. Biotechnol. , vol.66 , pp. 408-413
    • Kang, S.1    Vieille, C.2    Zeikus, J.3
  • 67
    • 0032483304 scopus 로고    scopus 로고
    • Threedimensional structure of Pseudomonas isoamylase at 2.2 °a resolution
    • Katsuya Y., Mezaki Y., Kubota M. & Matsuura Y. 1998. Threedimensional structure of Pseudomonas isoamylase at 2.2 °A resolution. J. Mol. Biol. 281: 885-897.
    • (1998) J. Mol. Biol. , vol.281 , pp. 885-897
    • Katsuya, Y.1    Mezaki, Y.2    Kubota, M.3    Matsuura, Y.4
  • 68
    • 4444347048 scopus 로고    scopus 로고
    • Expression of cyclodextrinase gene from Paenibacillus sp. A11 in Escherichia coli and characterization of the purified cyclodextrinase
    • Kaulpiboon J. & Pongsawasdi P. 2004. Expression of cyclodextrinase gene from Paenibacillus sp. A11 in Escherichia coli and characterization of the purified cyclodextrinase. J. Biochem. Mol. Biol. 37: 408-415.
    • (2004) J. Biochem. Mol. Biol. , vol.37 , pp. 408-415
    • Kaulpiboon, J.1    Pongsawasdi, P.2
  • 69
    • 11144282638 scopus 로고    scopus 로고
    • Purification and characterization of cyclodextrinase from Paenibacillus sp. A11
    • Kaulpiboon J. & Pongsawasdi P. 2005. Purification and characterization of cyclodextrinase from Paenibacillus sp. A11. Enzyme Microb. Technol. 36: 168-175.
    • (2005) Enzyme Microb. Technol. , vol.36 , pp. 168-175
    • Kaulpiboon, J.1    Pongsawasdi, P.2
  • 70
    • 34848871965 scopus 로고    scopus 로고
    • Conversion of a cyclodextrin glucanotransferase into an α-amylase: Assessment of directed evolution strategies
    • Kelly R.M., Leemhuis H. & Dijkhuizen L. 2007. Conversion of a cyclodextrin glucanotransferase into an α-amylase: assessment of directed evolution strategies. Biochemistry 46: 11216-11222.
    • (2007) Biochemistry , vol.46 , pp. 11216-11222
    • Kelly, R.M.1    Leemhuis, H.2    Dijkhuizen, L.3
  • 71
    • 34247614099 scopus 로고    scopus 로고
    • Molecular cloning and biochemical characterization of the first archaeal maltogenic amylase from the hyperthermophilic archaeon Thermoplasma volcanium GSS1
    • Kim J.W., Kim Y.H., Lee H.S., Yang S.J., Kim Y.W., Lee M.H., Kim J.W., Seo N.S., Park C.S. & Park K.H. 2007. Molecular cloning and biochemical characterization of the first archaeal maltogenic amylase from the hyperthermophilic archaeon Thermoplasma volcanium GSS1. Biochim. Biophys. Acta 1774: 661-669.
    • (2007) Biochim. Biophys. Acta , vol.1774 , pp. 661-669
    • Kim, J.W.1    Kim, Y.H.2    Lee, H.S.3    Yang, S.J.4    Kim, Y.W.5    Lee, M.H.6    Kim, J.W.7    Seo, N.S.8    Park, C.S.9    Park, K.H.10
  • 72
    • 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
  • 74
    • 0024786756 scopus 로고
    • Purification and some properties of amylomaltase from Escherichia coli IFO 3806
    • Kitahata S., Murakami H. & Okada S. 1989. Purification and some properties of amylomaltase from Escherichia coli IFO 3806. Agric. Biol. Chem. 53: 2653-2659.
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 2653-2659
    • Kitahata, S.1    Murakami, H.2    Okada, S.3
  • 75
    • 0027176843 scopus 로고
    • Polypeptide folding of Bacillus cereus ATCC7064 oligo-1,6-glucosidase revealed by 3.0 °a resolution X-ray analysis
    • Kizaki H., Hata Y., Watanabe K., Katsube Y. & Suzuki Y. 1993. Polypeptide folding of Bacillus cereus ATCC7064 oligo-1,6-glucosidase revealed by 3.0 °A resolution X-ray analysis. J. Biochem. 113: 646-649.
    • (1993) J. Biochem. , vol.113 , pp. 646-649
    • Kizaki, H.1    Hata, Y.2    Watanabe, K.3    Katsube, Y.4    Suzuki, Y.5
  • 76
    • 0026744021 scopus 로고
    • Catalytic center of cyclodextrin glycosyltransferase derived from X-ray structure analysis combined with site-directed mutagenesis
    • Klein C., Hollender J., Bender H. & Schulz G.E. 1992. Catalytic center of cyclodextrin glycosyltransferase derived from X-ray structure analysis combined with site-directed mutagenesis. Biochemistry 31: 8740-8746.
    • (1992) Biochemistry , vol.31 , pp. 8740-8746
    • Klein, C.1    Hollender, J.2    Bender, H.3    Schulz, G.E.4
  • 77
    • 0026027728 scopus 로고
    • Structure of cyclodextrin glycosyltransferase refined at 2.0 °a resolution
    • Klein C. & Schulz G.E. 1991. Structure of cyclodextrin glycosyltransferase refined at 2.0 °A resolution. J. Mol. Biol. 217: 737-750.
    • (1991) J. Mol. Biol. , vol.217 , pp. 737-750
    • Klein, C.1    Schulz, G.E.2
  • 78
    • 0029979578 scopus 로고    scopus 로고
    • Crystal structure at 2.3 °a resolution and revised nucleotide sequence of the thermostable cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1
    • Knegtel R.M.A., Wind R.D., Rozeboom H.J., Kalk K.H., Buitelaar R.M., Dijkhuizen L. & Dijkstra B.W. 1996. Crystal structure at 2.3 °A resolution and revised nucleotide sequence of the thermostable cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1. J. Mol. Biol. 256: 611-622.
    • (1996) J. Mol. Biol. , vol.256 , pp. 611-622
    • Knegtel, R.M.A.1    Wind, R.D.2    Rozeboom, H.J.3    Kalk, K.H.4    Buitelaar, R.M.5    Dijkhuizen, L.6    Dijkstra, B.W.7
  • 79
    • 0028880402 scopus 로고
    • Crystallographic studies of the interaction of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 with natural substrates and products
    • Knegtel R.M., Strokopytov B., Penninga D., Faber O.G., Rozeboom H.J., Kalk K.H., Dijkhuizen L. & Dijkstra B.W. 1995. Crystallographic studies of the interaction of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 with natural substrates and products. J. Biol. Chem. 270: 29256-29264.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29256-29264
    • Knegtel, R.M.1    Strokopytov, B.2    Penninga, D.3    Faber, O.G.4    Rozeboom, H.J.5    Kalk, K.H.6    Dijkhuizen, L.7    Dijkstra, B.W.8
  • 80
    • 0001737019 scopus 로고
    • Molecular structure of Bacillus stearothermophilus cyclodextrin glucanotransferase and analysis of substrate binding site
    • Kubota M., Matsuura Y., Sakai S. & Katsube Y. 1991. Molecular structure of Bacillus stearothermophilus cyclodextrin glucanotransferase and analysis of substrate binding site. J. Jpn. Soc. Starch Sci. 38: 141-146.
    • (1991) J. Jpn. Soc. Starch Sci. , vol.38 , pp. 141-146
    • Kubota, M.1    Matsuura, Y.2    Sakai, S.3    Katsube, Y.4
  • 81
    • 0032976301 scopus 로고    scopus 로고
    • The concept of the α-amylase family: Structural similarity and common catalytic mechanism
    • Kuriki T. & Imanaka T. 1999. The concept of the α-amylase family: structural similarity and common catalytic mechanism. J. Biosci. Bioeng. 87: 557-565.
    • (1999) J. Biosci. Bioeng. , vol.87 , pp. 557-565
    • Kuriki, T.1    Imanaka, T.2
  • 82
    • 0027496724 scopus 로고
    • The purification and characterization of an extremely thermostable α-amylase from the hyperthermophilic archaebacterium Pyrococcus furiosus
    • Laderman K.A., Davis B.R., Krutzsch H., Lewis M.S., Griko Y., Privalov P.L. & Anfinsen C.B. 1993. The purification and characterization of an extremely thermostable α-amylase from the hyperthermophilic archaebacterium Pyrococcus furiosus. J. Biol. Chem. 268: 24394-24401.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24394-24401
    • Laderman, K.A.1    Davis, B.R.2    Krutzsch, H.3    Lewis, M.S.4    Griko, Y.5    Privalov, P.L.6    Anfinsen, C.B.7
  • 83
    • 0028359337 scopus 로고
    • Refined molecular structure of pig pancreatic α-amylase at 2·1 °a resolution
    • Larson S.B., Greenwood A., Cascio D., Day J. & McPherson A. 1994. Refined molecular structure of pig pancreatic α-amylase at 2·1 °A resolution. J. Mol. Biol. 235: 1560-1584.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1560-1584
    • Larson, S.B.1    Greenwood, A.2    Cascio, D.3    Day, J.4    McPherson, A.5
  • 86
    • 0037041916 scopus 로고    scopus 로고
    • Cooperative action of α-glucanotransferase and maltogenic amylase for an improved process of isomaltooligosaccharide (IMO) production
    • Lee H.S., Auh J.H., Yoon H.G., Kim M.J., Park J.H., Hong S.S., Kang M.H., Kim T.J., Moon T.W. & Kim J.W. 2002. Cooperative action of α-glucanotransferase and maltogenic amylase for an improved process of isomaltooligosaccharide (IMO) production. J. Agric. Food. Chem. 50: 2812-2817.
    • (2002) J. Agric. Food. Chem. , vol.50 , pp. 2812-2817
    • Lee, H.S.1    Auh, J.H.2    Yoon, H.G.3    Kim, M.J.4    Park, J.H.5    Hong, S.S.6    Kang, M.H.7    Kim, T.J.8    Moon, T.W.9    Kim, J.W.10
  • 88
    • 34248396315 scopus 로고    scopus 로고
    • Characterization of a thermostable cyclodextrin glucanotransferase from Pyrococcus furiosus DSM3638
    • Lee M.H., Yang S.J., Kim J.W., Lee H.S., Kim J.W. & Park K.H. 2007. Characterization of a thermostable cyclodextrin glucanotransferase from Pyrococcus furiosus DSM3638. Extremophiles 11: 537-541.
    • (2007) Extremophiles , vol.11 , pp. 537-541
    • Lee, M.H.1    Yang, S.J.2    Kim, J.W.3    Lee, H.S.4    Kim, J.W.5    Park, K.H.6
  • 89
    • 77955092809 scopus 로고    scopus 로고
    • Overexpression and characterization of an extremely thermostable maltogenic amylase, with an optimal temperature of 100°C, from the hyperthermophilic archaeon Staphylothermus marinus
    • Li D., Park J.T., Li X., Kim S., Lee S., Shim J.H., Park S.H., Cha J., Lee B.H., Kim J.W. & Park K.H. 2010a. Overexpression and characterization of an extremely thermostable maltogenic amylase, with an optimal temperature of 100°C, from the hyperthermophilic archaeon Staphylothermus marinus. N. Biotechnol. 27: 300-307.
    • (2010) N. Biotechnol. , vol.27 , pp. 300-307
    • Li, D.1    Park, J.T.2    Li, X.3    Kim, S.4    Lee, S.5    Shim, J.H.6    Park, S.H.7    Cha, J.8    Lee, B.H.9    Kim, J.W.10    Park, K.H.11
  • 90
    • 76849113944 scopus 로고    scopus 로고
    • Characterization of a recombinant amylolytic enzyme of hyperthermophilic archaeon Thermofilum pendens with extremely thermostable maltogenic amylase activity
    • Li X., Li D., Yin Y. & Park K.H. 2010b. Characterization of a recombinant amylolytic enzyme of hyperthermophilic archaeon Thermofilum pendens with extremely thermostable maltogenic amylase activity. Appl. Microbiol. Biotechnol. 85: 1821-1830.
    • (2010) Appl. Microbiol. Biotechnol. , vol.85 , pp. 1821-1830
    • Li, X.1    Li, D.2    Yin, Y.3    Park, K.H.4
  • 91
    • 0026660023 scopus 로고
    • Purification and characterization of a novel thermostable 4-α-glucanotransferase of Thermotoga maritima cloned in Escherichia coli
    • Liebl W., Feil R., Gabelsberger J., Kellermann J. & Schleifer K.H. 1992. Purification and characterization of a novel thermostable 4-α-glucanotransferase of Thermotoga maritima cloned in Escherichia coli. Eur. J. Biochem. 207: 81-88.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 81-88
    • Liebl, W.1    Feil, R.2    Gabelsberger, J.3    Kellermann, J.4    Schleifer, K.H.5
  • 92
    • 0037224042 scopus 로고    scopus 로고
    • Cloning and characterization of the glycogen branching enzyme gene existing in tandem with the glycogen debranching enzyme from Pectobacterium chrysanthemi PY35
    • Lim W.J., Park S.R., Kim M.K., An C.L., Yun H.J., Hong S.Y., Kim E.J., Shin E.C., Lee S.W., Lim Y.P. & Yun H.D. 2003. Cloning and characterization of the glycogen branching enzyme gene existing in tandem with the glycogen debranching enzyme from Pectobacterium chrysanthemi PY35. Biochem. Biophys. Res. Commun. 300: 93-101.
    • (2003) Biochem. Biophys. Res. Commun. , vol.300 , pp. 93-101
    • Lim, W.J.1    Park, S.R.2    Kim, M.K.3    An, C.L.4    Yun, H.J.5    Hong, S.Y.6    Kim, E.J.7    Shin, E.C.8    Lee, S.W.9    Lim, Y.P.10    Yun, H.D.11
  • 93
    • 0001310335 scopus 로고
    • Characterization of D-enzyme (4-α-glucanotransferase) in Arabidopsis leaf
    • Lin T.P. & Preiss J. 1988. Characterization of D-enzyme (4-α-glucanotransferase) in Arabidopsis leaf. Plant Physiol. 86: 260-265.
    • (1988) Plant Physiol. , vol.86 , pp. 260-265
    • Lin, T.P.1    Preiss, J.2
  • 96
    • 0035831255 scopus 로고    scopus 로고
    • Relationship of sequence and structure to specificity in the α-amylase family of enzymes
    • MacGregor E.A., Janeček Š. & Svensson B. 2001. Relationship of sequence and structure to specificity in the α-amylase family of enzymes. Biochim. Biophys. Acta 1546: 1-20.
    • (2001) Biochim. Biophys. Acta , vol.1546 , pp. 1-20
    • MacGregor, E.A.1    Janeček, S.2    Svensson, B.3
  • 97
    • 0029671161 scopus 로고    scopus 로고
    • A circularly permuted α-amylase-type α/β-barrel structure in glucan-synthesizing glucosyltransferases
    • MacGregor E.A., Jespersen H.M. & Svensson B. 1996. A circularly permuted α-amylase-type α/β-barrel structure in glucan-synthesizing glucosyltransferases. FEBS Lett. 378: 263-266.
    • (1996) FEBS Lett. , vol.378 , pp. 263-266
    • MacGregor, E.A.1    Jespersen, H.M.2    Svensson, B.3
  • 98
    • 0034624223 scopus 로고    scopus 로고
    • Cycloamylose as an efficient artificial chaperone for protein refolding
    • Machida S., Ogawa S., Xiaohua S., Takaha T., Fujii K. & Hayashi K. 2000. Cycloamylose as an efficient artificial chaperone for protein refolding. FEBS Lett. 486: 131-135.
    • (2000) FEBS Lett. , vol.486 , pp. 131-135
    • Machida, S.1    Ogawa, S.2    Xiaohua, S.3    Takaha, T.4    Fujii, K.5    Hayashi, K.6
  • 99
    • 0028933531 scopus 로고
    • Crystal structure of calcium-depleted Bacillus licheniformis α-amylase at 2.2 °a resolution
    • Machius M., Wiegand G. & Huber R. 1995. Crystal structure of calcium-depleted Bacillus licheniformis α-amylase at 2.2 °A resolution. J. Mol. Biol. 246: 545-559.
    • (1995) J. Mol. Biol. , vol.246 , pp. 545-559
    • Machius, M.1    Wiegand, G.2    Huber, R.3
  • 100
    • 0035013682 scopus 로고    scopus 로고
    • Characterization of cyclodextrin glycosyltransferase from Bacillus firmus strain no. 37
    • Matioli G., Zanin G.M. & De Moraes F.F. 2001. Characterization of cyclodextrin glycosyltransferase from Bacillus firmus strain no. 37. Appl. Biochem. Biotechnol. 93: 643-654.
    • (2001) Appl. Biochem. Biotechnol. , vol.93 , pp. 643-654
    • Matioli, G.1    Zanin, G.M.2    De Moraes, F.F.3
  • 101
    • 0021395910 scopus 로고
    • Structure and possible catalytic residues of Taka-amylase A
    • Matsuura Y., Kusunoki M., HaradaW. & Kakudo M. 1984. Structure and possible catalytic residues of Taka-amylase A. J. Biochem. 95: 697-702.
    • (1984) J. Biochem. , vol.95 , pp. 697-702
    • Matsuura, Y.1    Kusunoki, M.2    Harada, W.3    Kakudo, M.4
  • 103
    • 0021244259 scopus 로고
    • A radioisotope method for assays of amylomaltase and D-enzyme
    • Medda S. & Smith E.E. 1984. A radioisotope method for assays of amylomaltase and D-enzyme. Anal. Biochem. 138: 354-359.
    • (1984) Anal. Biochem. , vol.138 , pp. 354-359
    • Medda, S.1    Smith, E.E.2
  • 104
    • 0031552349 scopus 로고    scopus 로고
    • Crystal structure of a maltotetraose-forming exo-amylase from Pseudomonas stutzeri
    • Morishita Y., Hasegawa K., Matsuura Y., Katsube Y., Kubota M. & Sakai S. 1997. Crystal structure of a maltotetraose-forming exo-amylase from Pseudomonas stutzeri. J. Mol. Biol. 267: 661-672.
    • (1997) J. Mol. Biol. , vol.267 , pp. 661-672
    • Morishita, Y.1    Hasegawa, K.2    Matsuura, Y.3    Katsube, Y.4    Kubota, M.5    Sakai, S.6
  • 105
    • 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
  • 106
    • 0026567912 scopus 로고
    • Functional relationships between cyclodextrin glucanotransferase from an alkalophilic Bacillus and α-amylases. Site-directed mutagenesis of the conserved two ASP and one Glu residues
    • Nakamura A., Haga K., Ogawa S., Kuwano K., Kimura K. & Yamane K. 1992. Functional relationships between cyclodextrin glucanotransferase from an alkalophilic Bacillus and α-amylases. Site-directed mutagenesis of the conserved two Asp and one Glu residues. FEBS Lett. 296: 37-40.
    • (1992) FEBS Lett. , vol.296 , pp. 37-40
    • Nakamura, A.1    Haga, K.2    Ogawa, S.3    Kuwano, K.4    Kimura, K.5    Yamane, K.6
  • 107
    • 0033923355 scopus 로고    scopus 로고
    • High expression of glycogen-debranching enzyme inEscherichia coli and its competent purification method
    • Nakayama A., Yamamoto K. & Tabata S. 2000. High expression of glycogen-debranching enzyme inEscherichia coli and its competent purification method. Protein Expr. Purif. 19: 298-303.
    • (2000) Protein Expr. Purif. , vol.19 , pp. 298-303
    • Nakayama, A.1    Yamamoto, K.2    Tabata, S.3
  • 108
    • 0001778511 scopus 로고
    • Thermoanaerobacter sp. CGTase: Its properties and application
    • Norman B.E. & Jorgensen S.T. 1992. Thermoanaerobacter sp. CGTase: its properties and application. J. Jpn. Soc. Starch Sci. 39: 101-108.
    • (1992) J. Jpn. Soc. Starch Sci. , vol.39 , pp. 101-108
    • Norman, B.E.1    Jorgensen, S.T.2
  • 109
    • 84889448637 scopus 로고    scopus 로고
    • Carbohydrate and intense sweeteners
    • Ashurst P.R. (ed.), Blackwell Publishing Ltd., Oxford
    • O'Donnel K. 2005. Carbohydrate and intense sweeteners, pp. 68-89. In: Ashurst P.R. (ed.), Chemistry and Technology of Soft Drinks and Fruit Juices, Blackwell Publishing Ltd., Oxford.
    • (2005) Chemistry and Technology of Soft Drinks and Fruit Juices , pp. 68-89
    • O'Donnel, K.1
  • 110
    • 33646158199 scopus 로고    scopus 로고
    • Structure of a complex of Thermoactinomyces vulgaris R-47 α-amylase 2 with maltohexaose demonstrates the important role of aromatic residues at the reducing end of the substrate binding cleft
    • Ohtaki A., Mizuno M., Yoshida H., Tonozuka T., Sakano Y. & Kamitori S. 2006. Structure of a complex of Thermoactinomyces vulgaris R-47 α-amylase 2 with maltohexaose demonstrates the important role of aromatic residues at the reducing end of the substrate binding cleft. Carbohydr. Res. 341: 1041-1046.
    • (2006) Carbohydr. Res. , vol.341 , pp. 1041-1046
    • Ohtaki, A.1    Mizuno, M.2    Yoshida, H.3    Tonozuka, T.4    Sakano, Y.5    Kamitori, S.6
  • 112
    • 55949117487 scopus 로고    scopus 로고
    • Cloning, extracellular expression and characterization of a predominant β-CGTase from Bacillus sp. G1 in E. Coli
    • Ong R.M., Goh K.M., Mahadi N.M., Hassan O., Rahman R.N. & Illias R.M. 2008. Cloning, extracellular expression and characterization of a predominant β-CGTase from Bacillus sp. G1 in E. coli. J. Ind. Microbiol. Biotechnol. 35: 1705-1714.
    • (2008) J. Ind. Microbiol. Biotechnol. , vol.35 , pp. 1705-1714
    • Ong, R.M.1    Goh, K.M.2    Mahadi, N.M.3    Hassan, O.4    Rahman, R.N.5    Illias, R.M.6
  • 113
    • 0036866921 scopus 로고    scopus 로고
    • Oligo-1,6-glucosidase and neopullulanase enzyme subfamilies from the α-amylase family defined by the fifth conserved sequence region
    • Oslancova A. & Janeček Š. 2002. Oligo-1,6-glucosidase and neopullulanase enzyme subfamilies from the α-amylase family defined by the fifth conserved sequence region. Cell. Mol. Life Sci. 59: 1945-1959.
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1945-1959
    • Oslancova, A.1    Janeček, S.2
  • 114
    • 0017082211 scopus 로고
    • The action pattern of amylomaltase from Escherichia coli
    • Palmer T.N., Ryman B.E. & Whelan W.J. 1976. The action pattern of amylomaltase from Escherichia coli. Eur. J. Biochem. 69: 105-115.
    • (1976) Eur. J. Biochem. , vol.69 , pp. 105-115
    • Palmer, T.N.1    Ryman, B.E.2    Whelan, W.J.3
  • 116
    • 34347380952 scopus 로고    scopus 로고
    • TreX from Sulfolobus solfataricus ATCC 35092 displays isoamylase and 4-α-glucanotransferase activities
    • Park H.S., Park J.T., Kang H.K., Cha H., Kim D.S., Kim J.W. & Park K.H. 2007. TreX from Sulfolobus solfataricus ATCC 35092 displays isoamylase and 4-α-glucanotransferase activities. Biosci. Biotechnol. Biochem. 71: 1348-1352.
    • (2007) Biosci. Biotechnol. Biochem. , vol.71 , pp. 1348-1352
    • Park, H.S.1    Park, J.T.2    Kang, H.K.3    Cha, H.4    Kim, D.S.5    Kim, J.W.6    Park, K.H.7
  • 118
    • 84871714045 scopus 로고    scopus 로고
    • A novel domain arrangement in a monomeric cyclodextrin-hydrolyzing enzyme from the hyperthermophile Pyrococcus furiosus
    • Park J.T., Song H.N., Jung T.Y., Lee M.H., Park S.G., Woo E.J. & Park K.H. 2013. A novel domain arrangement in a monomeric cyclodextrin-hydrolyzing enzyme from the hyperthermophile Pyrococcus furiosus. Biochim. Biophys. Acta 1834: 380-386.
    • (2013) Biochim. Biophys. Acta , vol.1834 , pp. 380-386
    • Park, J.T.1    Song, H.N.2    Jung, T.Y.3    Lee, M.H.4    Park, S.G.5    Woo, E.J.6    Park, K.H.7
  • 119
    • 0034705064 scopus 로고    scopus 로고
    • Structure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the α-amylase family
    • Park K.H., Kim T.J., Cheong T.K., Kim J.W., Oh B.H. & Svensson B. 2000. Structure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the α-amylase family. Biochim. Biophys. Acta 1478: 165-185.
    • (2000) Biochim. Biophys. Acta , vol.1478 , pp. 165-185
    • Park, K.H.1    Kim, T.J.2    Cheong, T.K.3    Kim, J.W.4    Oh, B.H.5    Svensson, B.6
  • 120
    • 0014430006 scopus 로고
    • The isolation and mode of action of a bacterial glucanosyltranferase
    • Pazur J.H. & Okada S. 1968. The isolation and mode of action of a bacterial glucanosyltranferase. J. Biol. Chem. 243: 4732-4738.
    • (1968) J. Biol. Chem. , vol.243 , pp. 4732-4738
    • Pazur, J.H.1    Okada, S.2
  • 122
    • 46049106394 scopus 로고    scopus 로고
    • Characterization of cyclodextrin glucanotransferase produced by Bacillus megaterium
    • Pishtiyski I., Popova V. & Zhekova B. 2008. Characterization of cyclodextrin glucanotransferase produced by Bacillus megaterium. Appl. Biochem. Biotechnol. 144: 263-272.
    • (2008) Appl. Biochem. Biotechnol. , vol.144 , pp. 263-272
    • Pishtiyski, I.1    Popova, V.2    Zhekova, B.3
  • 124
    • 0034711947 scopus 로고    scopus 로고
    • Crystal structure of amylomaltase from Thermus aquaticus, a glycosyltransferase catalysing the production of large cyclic glucans
    • Przylas I., Tomoo K., Terada Y., Takaha T., Fujii K., Saenger W. & Sträter N. 2000b. Crystal structure of amylomaltase from Thermus aquaticus, a glycosyltransferase catalysing the production of large cyclic glucans. J. Mol. Biol. 296: 873-886.
    • (2000) J. Mol. Biol. , vol.296 , pp. 873-886
    • Przylas, I.1    Tomoo, K.2    Terada, Y.3    Takaha, T.4    Fujii, K.5    Saenger, W.6    Sträter, N.7
  • 125
    • 12744254232 scopus 로고    scopus 로고
    • Cyclodextrin glucanotransferase: From gene to applications
    • Qi Q. & Zimmermann W. 2005. Cyclodextrin glucanotransferase: from gene to applications. Appl. Microbiol. Biotechnol. 66: 475-485.
    • (2005) Appl. Microbiol. Biotechnol. , vol.66 , pp. 475-485
    • Qi, Q.1    Zimmermann, W.2
  • 126
    • 0028198814 scopus 로고
    • The active center of a mammalian α-amylase. Structure of the complex of a pancreatic α-amylase with a carbohydrate inhibitor refined to 2.2 °a resolution
    • Qian M., Haser R., Buisson G., Duee E. & Payan F. 1994. The active center of a mammalian α-amylase. Structure of the complex of a pancreatic α-amylase with a carbohydrate inhibitor refined to 2.2 °A resolution. Biochemistry 33: 6284-6294.
    • (1994) Biochemistry , vol.33 , pp. 6284-6294
    • Qian, M.1    Haser, R.2    Buisson, G.3    Duee, E.4    Payan, F.5
  • 127
    • 33748279844 scopus 로고    scopus 로고
    • Molecular cloning of a cyclodextrin glucanotransferase gene from alkalophilic Bacillus sp. TS1-1 and characterization of the recombinant enzyme
    • Rahman K., Illias R.M., Hassan O., Mahmood N.A.N. & Rashid N.A.A. 2006. Molecular cloning of a cyclodextrin glucanotransferase gene from alkalophilic Bacillus sp. TS1-1 and characterization of the recombinant enzyme. Enzyme Microb. Technol. 39: 74-84.
    • (2006) Enzyme Microb. Technol. , vol.39 , pp. 74-84
    • Rahman, K.1    Illias, R.M.2    Hassan, O.3    Mahmood, N.A.N.4    Rashid, N.A.A.5
  • 128
    • 0001631469 scopus 로고    scopus 로고
    • Structure of human salivary α-amylase at 1.6 °a resolution: Implications for its role in the oral cavity
    • Ramasubbu N., Paloth V., Luo Y., Brayer G.D. & Levine M. J. 1996. Structure of human salivary α-amylase at 1.6 °A resolution: implications for its role in the oral cavity. Acta. Crystallogr. D Biol. Crystallogr. 52: 435-446.
    • (1996) Acta. Crystallogr. D Biol. Crystallogr. , vol.52 , pp. 435-446
    • Ramasubbu, N.1    Paloth, V.2    Luo, Y.3    Brayer, G.D.4    Levine, M.J.5
  • 129
    • 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.
    • (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
  • 130
    • 84882734428 scopus 로고    scopus 로고
    • Production of long-chain isomaltooligosaccharides from maltotriose using the thermostable amylomaltase and transglucosidase enzymes
    • Rudeekulthamrong P., Sawasdee K. & Kaulpiboon J. 2013. Production of long-chain isomaltooligosaccharides from maltotriose using the thermostable amylomaltase and transglucosidase enzymes. Biotechnol. Bioprocess Eng. 18: 778-786.
    • (2013) Biotechnol. Bioprocess Eng. , vol.18 , pp. 778-786
    • Rudeekulthamrong, P.1    Sawasdee, K.2    Kaulpiboon, J.3
  • 131
    • 0036354161 scopus 로고    scopus 로고
    • Crystal structure of Thermotoga maritima 4-α-glucanotransferase and its acarbose complex: Implications for substrate specificity and catalysis
    • Roujeinikova A., Raasch C., Sedelnikova S., Liebl W. & Rice D.W. 2002. Crystal structure of Thermotoga maritima 4-α-glucanotransferase and its acarbose complex: implications for substrate specificity and catalysis. J. Mol. Biol. 321: 149-162.
    • (2002) J. Mol. Biol. , vol.321 , pp. 149-162
    • Roujeinikova, A.1    Raasch, C.2    Sedelnikova, S.3    Liebl, W.4    Rice, D.W.5
  • 132
    • 84871605381 scopus 로고    scopus 로고
    • Transglucosylation reaction of amylomaltase for the synthesis of anticariogenic oligosaccharides
    • Saehu S., Srisimarat W., Prousoontorn M.H. & Pongsawasdi P. 2013. Transglucosylation reaction of amylomaltase for the synthesis of anticariogenic oligosaccharides. J. Mol. Catal. B Enzymatic 88: 77-83.
    • (2013) J. Mol. Catal. B Enzymatic , vol.88 , pp. 77-83
    • Saehu, S.1    Srisimarat, W.2    Prousoontorn, M.H.3    Pongsawasdi, P.4
  • 133
    • 78650791313 scopus 로고    scopus 로고
    • Structural basis for branching-enzyme activity of glycoside hydrolase family 57: Structure and stability studies of a novel branching enzyme from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
    • Santos C.R., Tonoli C.C.C., Trindade D.M., Betzel C., Takata H., Kuriki T., Kanai T., Imanaka T., Arni R.K. & Murakami M.T. 2011. Structural basis for branching-enzyme activity of glycoside hydrolase family 57: structure and stability studies of a novel branching enzyme from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. Proteins 79: 547-557.
    • (2011) Proteins , vol.79 , pp. 547-557
    • Santos, C.R.1    Tonoli, C.C.C.2    Trindade, D.M.3    Betzel, C.4    Takata, H.5    Kuriki, T.6    Kanai, T.7    Imanaka, T.8    Arni, R.K.9    Murakami, M.T.10
  • 135
    • 0018316247 scopus 로고
    • Starch metabolism in Pseudomonas stutzeri. II. Purification and properties of a dextrin glycosyltransferase (D-enzyme) and amylomaltase
    • Schmidt J. & John M. 1979. Starch metabolism in Pseudomonas stutzeri. II. Purification and properties of a dextrin glycosyltransferase (D-enzyme) and amylomaltase. Biochim. Biophys. Acta 566: 100-114.
    • (1979) Biochim. Biophys. Acta , vol.566 , pp. 100-114
    • Schmidt, J.1    John, M.2
  • 138
    • 33845665889 scopus 로고    scopus 로고
    • Dividing the large glycoside hydrolase family 13 into subfamilies: Towards improved functional annotations of α-amylase-related proteins
    • Stam M.R., Danchin E.G.J., Rancurel C., Coutinho P.M. & Henrissat B. 2006. Dividing the large glycoside hydrolase family 13 into subfamilies: towards improved functional annotations of α-amylase-related proteins. Protein Eng. Des. Sel. 19: 555-562.
    • (2006) Protein Eng. Des. Sel. , vol.19 , pp. 555-562
    • Stam, M.R.1    Danchin, E.G.J.2    Rancurel, C.3    Coutinho, P.M.4    Henrissat, B.5
  • 140
    • 0028961637 scopus 로고
    • X-ray structure of cyclodextrin glycosyltransferase complexed with acarbose. Implications for the catalytic mechanism of glycosidases
    • Strokopytov B., Penninga D., Rozeboom H.J., Kalk K.H., Dijkhuizen L. & Dijkstra B.W. 1995. X-ray structure of cyclodextrin glycosyltransferase complexed with acarbose. Implications for the catalytic mechanism of glycosidases. Biochemistry 34: 2234-2240.
    • (1995) Biochemistry , vol.34 , pp. 2234-2240
    • Strokopytov, B.1    Penninga, D.2    Rozeboom, H.J.3    Kalk, K.H.4    Dijkhuizen, L.5    Dijkstra, B.W.6
  • 141
    • 0025920719 scopus 로고
    • Analysis of the characteristic action of D-enzyme from sweet potato in terms of subsite theory
    • Suganuma T., Setoguchi S., Fujimoto S. & Nagahama T. 1991. Analysis of the characteristic action of D-enzyme from sweet potato in terms of subsite theory. Carbohydr. Res. 212: 201-212.
    • (1991) Carbohydr. Res. , vol.212 , pp. 201-212
    • Suganuma, T.1    Setoguchi, S.2    Fujimoto, S.3    Nagahama, T.4
  • 142
    • 0028429952 scopus 로고
    • Protein engineering in the α-amylase family: Catalytic mechanism, substrate specificity, and stability
    • Svensson B. 1994. Protein engineering in the α-amylase family: catalytic mechanism, substrate specificity, and stability. Plant. Mol. Biol. 25: 141-157.
    • (1994) Plant. Mol. Biol. , vol.25 , pp. 141-157
    • Svensson, B.1
  • 143
    • 0024430052 scopus 로고
    • Sequence homology between putative raw-starch binding domains from different starch-degrading enzymes
    • Svensson B., Jespersen H., Sierks M. & MacGregor E.A. 1989. Sequence homology between putative raw-starch binding domains from different starch-degrading enzymes. Biochem. J. 264: 309-311.
    • (1989) Biochem. J. , vol.264 , pp. 309-311
    • Svensson, B.1    Jespersen, H.2    Sierks, M.3    MacGregor, E.A.4
  • 144
    • 0000843244 scopus 로고
    • Structure and molecular model refinement of Aspergillus oryzae (TAKA) α-amylase: An application of the simulated-annealing method
    • Swift H. J., Brady L., Derewenda Z.S., Dodson E.J., Dodson G.G., Turkenburg J.P. & Wilkinson A.J. 1991. Structure and molecular model refinement of Aspergillus oryzae (TAKA) α-amylase: an application of the simulated-annealing method. Acta Crystallogr. B 47: 535-544.
    • (1991) Acta Crystallogr. B , vol.47 , pp. 535-544
    • Swift, H.J.1    Brady, L.2    Derewenda, Z.S.3    Dodson, E.J.4    Dodson, G.G.5    Turkenburg, J.P.6    Wilkinson, A.J.7
  • 145
    • 84892345152 scopus 로고    scopus 로고
    • The use of starch processing enzymes in the food industry
    • Polaina J. & MacCabe A.P. (eds), Springer, Dordrecht
    • Synowiecki J. 2007. The use of starch processing enzymes in the food industry, pp. 19-34. In: Polaina J. & MacCabe A.P. (eds), Industrial Enzymes Structure, Function and Applications, Springer, Dordrecht.
    • (2007) Industrial Enzymes Structure, Function and Applications , pp. 19-34
    • Synowiecki, J.1
  • 146
    • 0001351992 scopus 로고
    • Electrochemical detection of reducing carbohydrates produced by the transferase action of yeast debranching enzyme on maltosaccharides
    • Tabata S. & Ide T. 1988. Electrochemical detection of reducing carbohydrates produced by the transferase action of yeast debranching enzyme on maltosaccharides. Carbohydr. Res. 176: 245-251.
    • (1988) Carbohydr. Res. , vol.176 , pp. 245-251
    • Tabata, S.1    Ide, T.2
  • 147
    • 0030808181 scopus 로고    scopus 로고
    • Cloning and expression of the 4-α-glucanotransferase gene from the hyperthermophilic archaeon Pyrococcus sp. KOD1, and characterization of the enzyme
    • 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.
    • (1997) J. Ferment. Bioeng. , vol.83 , pp. 540-548
    • Tachibana, Y.1    Fujiwara, S.2    Takagi, M.3    Imanaka, T.4
  • 148
    • 0032899816 scopus 로고    scopus 로고
    • Purification and characterization of an extremely thermostable cyclomaltodextrin glucanotransferase from a newly isolated hyperthermophilic archaeon, a Thermococcus sp
    • Tachibana Y., Kuramura A., Shirasaka N., Suzuki Y., Yamamoto T., Fujiwara S., Takagi M. & Imanaka T. 1999. Purification and characterization of an extremely thermostable cyclomaltodextrin glucanotransferase from a newly isolated hyperthermophilic archaeon, a Thermococcus sp. Appl. Environ. Microbiol. 65: 1991-1997.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 1991-1997
    • Tachibana, Y.1    Kuramura, A.2    Shirasaka, N.3    Suzuki, Y.4    Yamamoto, T.5    Fujiwara, S.6    Takagi, M.7    Imanaka, T.8
  • 149
    • 0034302052 scopus 로고    scopus 로고
    • Acceptor specificity of 4-α-glucanotransferase from Pyrococcus kodakaraensis KOD1, and synthesis of cycloamylose
    • Tachibana Y., Takaha T., Fujiwara S., Takagi M. & Imanaka T. 2000. Acceptor specificity of 4-α-glucanotransferase from Pyrococcus kodakaraensis KOD1, and synthesis of cycloamylose. J. Biosci. Bioeng. 90: 406-409.
    • (2000) J. Biosci. Bioeng. , vol.90 , pp. 406-409
    • Tachibana, Y.1    Takaha, T.2    Fujiwara, S.3    Takagi, M.4    Imanaka, T.5
  • 150
    • 0032810126 scopus 로고    scopus 로고
    • The functions of 4-α-glucanotransferases and their use for the production of cyclic glucans
    • Takaha T. & Smith S.M. 1999. The functions of 4-α-glucanotransferases and their use for the production of cyclic glucans. Biotechnol. Genet. Eng. 16: 257-280.
    • (1999) Biotechnol. Genet. Eng. , vol.16 , pp. 257-280
    • Takaha, T.1    Smith, S.M.2
  • 151
    • 0027458378 scopus 로고
    • Disproportionating enzyme (4-α-glucanotransferase; EC 2.4.1.25) of potato. Purification, molecular cloning, and potential role in starch metabolism
    • Takaha T., Yanase M., Okada S. & Smith S.M. 1993. Disproportionating enzyme (4-α-glucanotransferase; EC 2.4.1.25) of potato. Purification, molecular cloning, and potential role in starch metabolism. J. Biol. Chem. 268: 1391-1396.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1391-1396
    • Takaha, T.1    Yanase, M.2    Okada, S.3    Smith, S.M.4
  • 152
    • 0030062091 scopus 로고    scopus 로고
    • Potato D-enzyme catalyzes the cyclization of amylose to produce cycloamylose, a novel cyclic glucan
    • Takaha T., Yanase M., Takata H., Okada S. & Smith S.M. 1996. Potato D-enzyme catalyzes the cyclization of amylose to produce cycloamylose, a novel cyclic glucan. J. Biol. Chem. 271: 2902-2908.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2902-2908
    • Takaha, T.1    Yanase, M.2    Takata, H.3    Okada, S.4    Smith, S.M.5
  • 153
    • 84891826789 scopus 로고    scopus 로고
    • Expression and characterization of 4-α-glucanotransferase genes from Manihot esculenta Crantz and Arabidopsis thaliana and their use for the production of cycloamyloses
    • Tantanarat K., O'Neill E.C., Rejzek M., Field R. A. & Limpaseni T. 2014. Expression and characterization of 4-α-glucanotransferase genes from Manihot esculenta Crantz and Arabidopsis thaliana and their use for the production of cycloamyloses. Process Biochem. 49: 84-89.
    • (2014) Process Biochem. , vol.49 , pp. 84-89
    • Tantanarat, K.1    O'neill, E.C.2    Rejzek, M.3    Field, R.A.4    Limpaseni, T.5
  • 154
    • 0032985721 scopus 로고    scopus 로고
    • Thermus aquaticus ATCC 33923 amylomaltase gene cloning and expression and enzyme characterization: Production of cycloamylose
    • Terada Y., Fujii K., Takaha T. & Okada S. 1999. Thermus aquaticus ATCC 33923 amylomaltase gene cloning and expression and enzyme characterization: production of cycloamylose. Appl. Environ. Microbiol. 65: 910-915.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 910-915
    • Terada, Y.1    Fujii, K.2    Takaha, T.3    Okada, S.4
  • 156
    • 5544280269 scopus 로고    scopus 로고
    • Characterisation of a thermoalkali-stable cyclodextrin glycosyltransferase from the anaerobic thermoalkaliphilic bacterium Anaerobranca gottschalkii
    • Thiemann V., Donges C., Prowe S.G., Sterner R. & Antranikian G. 2004. Characterisation of a thermoalkali-stable cyclodextrin glycosyltransferase from the anaerobic thermoalkaliphilic bacterium Anaerobranca gottschalkii. Arch. Microbiol. 182: 226-235.
    • (2004) Arch. Microbiol. , vol.182 , pp. 226-235
    • Thiemann, V.1    Donges, C.2    Prowe, S.G.3    Sterner, R.4    Antranikian, G.5
  • 157
    • 0033520936 scopus 로고    scopus 로고
    • The cyclization mechanism of cyclodextrin glycosyltransferase (CGTase) as revealed by a γ-cyclodextrin-CGTase complex at 1.8-°A resolution
    • Uitdehaag J.C.M., Kalk K.H., van der Veen B.A., Dijkhuizen L. & Dijkstra B.W. 1999. The cyclization mechanism of cyclodextrin glycosyltransferase (CGTase) as revealed by a γ-cyclodextrin-CGTase complex at 1.8-°A resolution. J. Biol. Chem. 274: 34868-34876.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34868-34876
    • Uitdehaag, J.C.M.1    Kalk, K.H.2    Van Der Veen, B.A.3    Dijkhuizen, L.4    Dijkstra, B.W.5
  • 159
    • 84874650404 scopus 로고    scopus 로고
    • Starch modification with microbial α-glucanotransferase enzymes
    • van der Maarel M.J. & Leemhuis H. 2013. Starch modification with microbial α-glucanotransferase enzymes. Carbohyd. Polym. 93: 116-121.
    • (2013) Carbohyd. Polym. , vol.93 , pp. 116-121
    • Van Der Maarel, M.J.1    Leemhuis, H.2
  • 161
    • 0035976993 scopus 로고    scopus 로고
    • Hydrophobic amino acid residues in the acceptor binding site are main determinants for reaction mechanism and specificity of cyclodextringlycosyltransferase
    • van der Veen B.A., Leemhuis H., Kralj S., Uitdehaag J.C., Dijkstra B.W. & Dijkhuizen L. 2001. Hydrophobic amino acid residues in the acceptor binding site are main determinants for reaction mechanism and specificity of cyclodextringlycosyltransferase. J. Biol. Chem. 276: 44557-44562.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44557-44562
    • Van Der Veen, B.A.1    Leemhuis, H.2    Kralj, S.3    Uitdehaag, J.C.4    Dijkstra, B.W.5    Dijkhuizen, L.6
  • 162
    • 77958500768 scopus 로고    scopus 로고
    • Crystal structure of an essential enzyme in seed starch degradation: Barley limit dextrinase in complex with cyclodextrins
    • Vester-Christensen M.B., Abou Hachem M., Svensson B. & Henriksen A. 2010. Crystal structure of an essential enzyme in seed starch degradation: barley limit dextrinase in complex with cyclodextrins. J. Mol. Biol. 403: 739-750.
    • (2010) J. Mol. Biol. , vol.403 , pp. 739-750
    • Vester-Christensen, M.B.1    Abou Hachem, M.2    Svensson, B.3    Henriksen, A.4
  • 163
    • 0028091811 scopus 로고
    • C-terminal truncations of a thermostable Bacillus stearothermophilus α-amylase
    • Vihinen M., Peltonen T., Iitiä A., Suominen I. & Mäntsälä P. 1994. C-terminal truncations of a thermostable Bacillus stearothermophilus α-amylase. Protein Eng. 7: 1255-1259.
    • (1994) Protein Eng. , vol.7 , pp. 1255-1259
    • Vihinen, M.1    Peltonen, T.2    Iitiä, A.3    Suominen, I.4    Mäntsälä, P.5
  • 164
    • 0002051699 scopus 로고
    • Cyclomaltodextrin glucanotransferase from Bacillus circulans e 192. I. Purification and characterization of the enzyme
    • Villette J., Krzewinski F., Looten P., Sicard P. & Bouquelet S.L. 1992. Cyclomaltodextrin glucanotransferase from Bacillus circulans E 192. I. Purification and characterization of the enzyme. Biotechnol. Appl. Biochem. 16: 57-63.
    • (1992) Biotechnol. Appl. Biochem. , vol.16 , pp. 57-63
    • Villette, J.1    Krzewinski, F.2    Looten, P.3    Sicard, P.4    Bouquelet, S.L.5
  • 165
    • 0010266358 scopus 로고
    • A transglucosylase of Streptococcus bovis
    • Walker G.J. 1965. A transglucosylase of Streptococcus bovis. Biochem. J. 94: 299-308.
    • (1965) Biochem. J. , vol.94 , pp. 299-308
    • Walker, G.J.1
  • 166
    • 0010274051 scopus 로고
    • Metabolism of the reserve polysaccharide of Streptococcus mitis
    • Walker G.J. 1966. Metabolism of the reserve polysaccharide of Streptococcus mitis. Biochem. J. 101: 861-872.
    • (1966) Biochem. J. , vol.101 , pp. 861-872
    • Walker, G.J.1
  • 167
    • 33846874322 scopus 로고    scopus 로고
    • Efficient solubilization, purification of recombinant extracellular α-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 α-amylase from Pyrococcus furiosus expressed as inclusion bodies in Escherichia coli. J. Ind. Microbiol. Biotechnol. 34: 187-192.
    • (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
  • 168
    • 0031591389 scopus 로고    scopus 로고
    • The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 °a resolution: Structural characterization of proline-substitution sites for protein thermostabilization
    • Watanabe K., Hata Y., Kizaki H., Katsube Y. & Suzuki Y. 1997. The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 °A resolution: structural characterization of proline-substitution sites for protein thermostabilization. J. Mol. Biol. 269: 142-153.
    • (1997) J. Mol. Biol. , vol.269 , pp. 142-153
    • Watanabe, K.1    Hata, Y.2    Kizaki, H.3    Katsube, Y.4    Suzuki, Y.5
  • 169
    • 0032489385 scopus 로고    scopus 로고
    • Engineering of cyclodextrin product specificity and pH optima of the thermostable cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1
    • Wind R.D., Uitdehaag J.C., Buitelaar R.M., Dijkstra B.W. & Dijkhuizen L. 1998. Engineering of cyclodextrin product specificity and pH optima of the thermostable cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1. J. Biol. Chem. 273: 5771-5779.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5771-5779
    • Wind, R.D.1    Uitdehaag, J.C.2    Buitelaar, R.M.3    Dijkstra, B.W.4    Dijkhuizen, L.5
  • 170
    • 57649133949 scopus 로고    scopus 로고
    • Structural insight into the bifunctional mechanism of the glycogen-debranching enzyme TreX from the archaeon Sulfolobus solfataricus
    • Woo E.J., Lee S., Cha H., Park J.T., Yoon S.M., Song H.N. & Park K.H. 2008. Structural insight into the bifunctional mechanism of the glycogen-debranching enzyme TreX from the archaeon Sulfolobus solfataricus. J. Biol. Chem. 283: 28641-28648.
    • (2008) J. Biol. Chem. , vol.283 , pp. 28641-28648
    • Woo, E.J.1    Lee, S.2    Cha, H.3    Park, J.T.4    Yoon, S.M.5    Song, H.N.6    Park, K.H.7
  • 172
    • 3242816124 scopus 로고    scopus 로고
    • Bioinformatics of the glycoside hydrolase family 57 and identification of catalytic residues in amylopullulanase from Thermococcus hydrothermalis
    • Zona R., Chang-Pi-Hin F., O'Donohue M.J. & Janeček Š. 2004. Bioinformatics of the glycoside hydrolase family 57 and identification of catalytic residues in amylopullulanase from Thermococcus hydrothermalis. Eur. J. Biochem. 271: 2863-2872.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 2863-2872
    • Zona, R.1    Chang-Pi-Hin, F.2    O'donohue, M.J.3    Janeček, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.