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Volumn 79, Issue 13, 2013, Pages 4072-4077

Improving the thermostability and catalytic efficiency of Bacillus deramificans pullulanase by site-directed mutagenesis

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC EFFICIENCIES; ENHANCED PROPERTIES; OPTIMAL TEMPERATURE; OPTIMUM TEMPERATURE; SITE DIRECTED MUTAGENESIS; STARCH HYDROLYSIS; STARCH INDUSTRY; WILD-TYPE ENZYMES;

EID: 84879816037     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.00457-13     Document Type: Article
Times cited : (102)

References (38)
  • 1
    • 3242696208 scopus 로고    scopus 로고
    • Starch structure and digestibility enzyme-substrate relationship
    • Tester R, Karkalas J, Qi X. 2004. Starch structure and digestibility enzyme-substrate relationship. World Poultry Sci. J. 60:186-195.
    • (2004) World Poultry Sci. J. , vol.60 , pp. 186-195
    • Tester, R.1    Karkalas, J.2    Qi, X.3
  • 2
    • 0014004642 scopus 로고
    • Pullulanase from Aerobacter aerogenes: production in a cell-bound state
    • Wallenfels K, Bender H, Rached J. 1966. Pullulanase from Aerobacter aerogenes: production in a cell-bound state. Biochem. Biophys. Res. Commun. 22:254-261.
    • (1966) Biochem. Biophys. Res. Commun. , vol.22 , pp. 254-261
    • Wallenfels, K.1    Bender, H.2    Rached, J.3
  • 3
    • 0032923123 scopus 로고    scopus 로고
    • A new pullulanase from a hyperthermophilic archaeon for starch hydrolysis
    • Gantelet H, Duchiron F. 1999. A new pullulanase from a hyperthermophilic archaeon for starch hydrolysis. Biotechnol. Lett. 21:71-75.
    • (1999) Biotechnol. Lett. , vol.21 , pp. 71-75
    • Gantelet, H.1    Duchiron, F.2
  • 4
    • 0036844135 scopus 로고    scopus 로고
    • Thermostable pullulanase type I from new isolated Bacillus thermoleovorans US105: cloning, sequencing and expression of the gene in E
    • Ben Messaoud E, Ben Ammar Y, Mellouli L, Bejar S. 2002. Thermostable pullulanase type I from new isolated Bacillus thermoleovorans US105: cloning, sequencing and expression of the gene in E. coli. Enzyme Microb. Technol. 31:827-832.
    • (2002) coli. Enzyme Microb. Technol. , vol.31 , pp. 827-832
    • Ben Messaoud, E.1    Ben Ammar, Y.2    Mellouli, L.3    Bejar, S.4
  • 5
    • 0043170899 scopus 로고    scopus 로고
    • Highly thermostable amylase and pullulanase of the extreme thermophilic eubacterium Rhodothermus marinus: production and partial characterization
    • Gomes I, Gomes J, Steiner W. 2003. Highly thermostable amylase and pullulanase of the extreme thermophilic eubacterium Rhodothermus marinus: production and partial characterization. Bioresource Technol. 90: 207-214.
    • (2003) Bioresource Technol. , vol.90 , pp. 207-214
    • Gomes, I.1    Gomes, J.2    Steiner, W.3
  • 6
    • 0033066459 scopus 로고    scopus 로고
    • Enhanced production of thermostable-amylase and pullulanase in the presence of surfactants by Clostridium thermosulfurogenes SV2
    • Reddy RM, Reddy PG, Seenayya G. 1999. Enhanced production of thermostable-amylase and pullulanase in the presence of surfactants by Clostridium thermosulfurogenes SV2. Process Biochem. 34:87-92.
    • (1999) Process Biochem. , vol.34 , pp. 87-92
    • Reddy, R.M.1    Reddy, P.G.2    Seenayya, G.3
  • 7
    • 2942621927 scopus 로고    scopus 로고
    • Cloning, sequencing, and characterization of a heat-and alkalistable type I pullulanase from Anaerobranca gottschalkii
    • Bertoldo C, Armbrecht M, Becker F, Schäfer T, Antranikian G, Liebl W. 2004. Cloning, sequencing, and characterization of a heat-and alkalistable type I pullulanase from Anaerobranca gottschalkii. Appl. Environ. Microbiol. 70:3407-3416.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 3407-3416
    • Bertoldo, C.1    Armbrecht, M.2    Becker, F.3    Schäfer, T.4    Antranikian, G.5    Liebl, W.6
  • 9
    • 79551472575 scopus 로고    scopus 로고
    • Molecular cloning and biochemical characterization of a heat-stable type I pullulanase from Thermotoga neapolitana
    • Kang J, Park KM, Choi KH, Park CS, Kim GE, Kim D, Cha J. 2011. Molecular cloning and biochemical characterization of a heat-stable type I pullulanase from Thermotoga neapolitana. Enzyme Microb. Technol. 48:260-266.
    • (2011) Enzyme Microb. Technol. , vol.48 , pp. 260-266
    • Kang, J.1    Park, K.M.2    Choi, K.H.3    Park, C.S.4    Kim, G.E.5    Kim, D.6    Cha, J.7
  • 10
    • 33645795717 scopus 로고    scopus 로고
    • Overexpression, purification and preliminary X-ray analysis of pullulanase from Bacillus subtilis strain 168
    • Malle D, Itoh T, Hashimoto W, Murata K, Utsumi S, Mikami B. 2006. Overexpression, purification and preliminary X-ray analysis of pullulanase from Bacillus subtilis strain 168. Acta Crystallogr. F 62:381-384.
    • (2006) Acta Crystallogr. , vol.62 F , pp. 381-384
    • Malle, D.1    Itoh, T.2    Hashimoto, W.3    Murata, K.4    Utsumi, S.5    Mikami, B.6
  • 13
    • 0344234325 scopus 로고    scopus 로고
    • Hydrolysis of starch by a mixture of glucoamylase and pullulanase entrapped individually in calcium alginate beads
    • Roy I, Gupta MN. 2004. Hydrolysis of starch by a mixture of glucoamylase and pullulanase entrapped individually in calcium alginate beads. Enzyme Microb. Technol. 34:26-32.
    • (2004) Enzyme Microb. Technol. , vol.34 , pp. 26-32
    • Roy, I.1    Gupta, M.N.2
  • 14
    • 0033151659 scopus 로고    scopus 로고
    • Commodity scale production of sugars from starches
    • Crabb WD, Shetty JK. 1999. Commodity scale production of sugars from starches. Curr. Opin. Microbiol. 2:252-256.
    • (1999) Curr. Opin. Microbiol. , vol.2 , pp. 252-256
    • Crabb, W.D.1    Shetty, J.K.2
  • 15
    • 84879809820 scopus 로고
    • Pullulanase, micro-organisms producing the same, method for preparation thereof aswell as its use
    • December, Europe patent 0,605,040 A1
    • Philippe D, Antoine A, December 1993. Pullulanase, micro-organisms producing the same, method for preparation thereof as well as its use. Europe patent 0,605,040 A1.
    • (1993)
    • Philippe, D.1    Antoine, A.2
  • 16
    • 38849157945 scopus 로고    scopus 로고
    • Development of a thermostable glucose dehydrogenase by a structure-guided consensus concept
    • Vázquez-Figueroa E, Chaparro-Riggers J, Bommarius AS. 2007. Development of a thermostable glucose dehydrogenase by a structure-guided consensus concept. Chembiochem 8:2295-2301.
    • (2007) Chembiochem , vol.8 , pp. 2295-2301
    • Vázquez-Figueroa, E.1    Chaparro-Riggers, J.2    Bommarius, A.S.3
  • 17
    • 78650678219 scopus 로고    scopus 로고
    • Thermostabilization of Bacillus circulans xylanase: computational optimization of unstable residues based on thermal fluctuation analysis
    • Joo JC, Pack SP, Kim YH, Yoo YJ. 2011. Thermostabilization of Bacillus circulans xylanase: computational optimization of unstable residues based on thermal fluctuation analysis. J. Bacteriol. 151:56-65.
    • (2011) J. Bacteriol. , vol.151 , pp. 56-65
    • Joo, J.C.1    Pack, S.P.2    Kim, Y.H.3    Yoo, Y.J.4
  • 19
    • 43049123356 scopus 로고    scopus 로고
    • Advances in laboratory evolution of enzymes
    • Bershtein S, Tawfik DS. 2008. Advances in laboratory evolution of enzymes. Curr. Opin. Chem. Biol. 12:151-158.
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 151-158
    • Bershtein, S.1    Tawfik, D.S.2
  • 20
    • 23444450226 scopus 로고    scopus 로고
    • Semi-rational approaches to engineering enzyme activity: combining the benefits of directed evolution and rational design
    • Chica RA, Doucet N, Pelletier JN. 2005. Semi-rational approaches to engineering enzyme activity: combining the benefits of directed evolution and rational design. Curr. Opin. Biotechnol. 16:378-384.
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 378-384
    • Chica, R.A.1    Doucet, N.2    Pelletier, J.N.3
  • 21
    • 58449130510 scopus 로고    scopus 로고
    • Improving thermostability and catalytic activity of pyranose 2-oxidase from Trametes multicolor by rational and semi-rational design
    • Spadiut O, Leitner C, Salaheddin C, Varga B, Vertessy BG, Tan TC, Divne C, Haltrich D. 2008. Improving thermostability and catalytic activity of pyranose 2-oxidase from Trametes multicolor by rational and semi-rational design. FEBS J. 276:776-792.
    • (2008) FEBS J. , vol.276 , pp. 776-792
    • Spadiut, O.1    Leitner, C.2    Salaheddin, C.3    Varga, B.4    Vertessy, B.G.5    Tan, T.C.6    Divne, C.7    Haltrich, D.8
  • 22
    • 84861149123 scopus 로고    scopus 로고
    • Improved thermostability of Clostridium thermocellum endoglucanase Cel8A by using consensus-guided mutagenesis
    • Anbar M, Gul O, Lamed R, Sezerman UO, Bayer EA. 2012. Improved thermostability of Clostridium thermocellum endoglucanase Cel8A by using consensus-guided mutagenesis. Appl. Environ. Microbiol. 78:3458-3464.
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 3458-3464
    • Anbar, M.1    Gul, O.2    Lamed, R.3    Sezerman, U.O.4    Bayer, E.A.5
  • 25
    • 84864073832 scopus 로고    scopus 로고
    • Improved thermostability of AEH by combining B-FIT analysis and structure-guided consensus method
    • Blum JK, Ricketts MD, Bommarius AS. 2012. Improved thermostability of AEH by combining B-FIT analysis and structure-guided consensus method. J. Biotechnol. 160:214-221.
    • (2012) J. Biotechnol. , vol.160 , pp. 214-221
    • Blum, J.K.1    Ricketts, M.D.2    Bommarius, A.S.3
  • 27
    • 67349085160 scopus 로고    scopus 로고
    • Mutations at subsite 3 in cyclodextrin glycosyltransferase from Paenibacillus macerans enhancing alpha-cyclodextrin specificity
    • Li Z, Zhang J, Wang M, Gu Z, Du G, Li J, Wu J, Chen J. 2009. Mutations at subsite 3 in cyclodextrin glycosyltransferase from Paenibacillus macerans enhancing alpha-cyclodextrin specificity. Appl. Microbiol. Biotechnol. 83:483-490.
    • (2009) Appl. Microbiol. Biotechnol. , vol.83 , pp. 483-490
    • Li, Z.1    Zhang, J.2    Wang, M.3    Gu, Z.4    Du, G.5    Li, J.6    Wu, J.7    Chen, J.8
  • 28
    • 74149088230 scopus 로고    scopus 로고
    • Delayed supplementation of glycine enhances extracellular secretion of the recombinant alpha-cyclodextrin glycosyltransferase in Escherichia coli
    • Li Z, Gu Z, Wang M, Du G, Wu J, Chen J. 2010. Delayed supplementation of glycine enhances extracellular secretion of the recombinant alpha-cyclodextrin glycosyltransferase in Escherichia coli. Appl. Microbiol. Biotechnol. 85:553-561.
    • (2010) Appl. Microbiol. Biotechnol. , vol.85 , pp. 553-561
    • Li, Z.1    Gu, Z.2    Wang, M.3    Du, G.4    Wu, J.5    Chen, J.6
  • 29
    • 0031809735 scopus 로고    scopus 로고
    • Purification and properties of a thermoactive and thermostable pullulanase from Thermococcus hydrothermalis, a hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent
    • Gantelet H, Duchiron F. 1998. Purification and properties of a thermoactive and thermostable pullulanase from Thermococcus hydrothermalis, a hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent. Appl. Microbiol. Biotechnol. 49:770-777.
    • (1998) Appl. Microbiol. Biotechnol. , vol.49 , pp. 770-777
    • Gantelet, H.1    Duchiron, F.2
  • 30
    • 0034736404 scopus 로고    scopus 로고
    • Kinetics of glucose isomerization to fructose by immobilized glucose isomerase: anomeric reactivity of D-glucose in kinetic model
    • Lee HS, Hong J. 2001. Kinetics of glucose isomerization to fructose by immobilized glucose isomerase: anomeric reactivity of D-glucose in kinetic model. J. Biotechnol. 84:145-153.
    • (2001) J. Biotechnol. , vol.84 , pp. 145-153
    • Lee, H.S.1    Hong, J.2
  • 31
    • 0040228649 scopus 로고
    • Improvement and estimation of enzymic starch saccharification process
    • Linko YY, Wu XY. 1993. Improvement and estimation of enzymic starch saccharification process. Biotechnol. Techniques 7:551-556.
    • (1993) Biotechnol. Techniques , vol.7 , pp. 551-556
    • Linko, Y.Y.1    Wu, X.Y.2
  • 32
    • 20744437001 scopus 로고    scopus 로고
    • RONN: the biobasis function neural network technique applied to the detection of natively disordered regions in proteins
    • Yang ZR, Thomson R, McNeil P, Esnouf RM. 2005. RONN: the biobasis function neural network technique applied to the detection of natively disordered regions in proteins. Bioinformatics 21:3369-3376.
    • (2005) Bioinformatics , vol.21 , pp. 3369-3376
    • Yang, Z.R.1    Thomson, R.2    McNeil, P.3    Esnouf, R.M.4
  • 33
    • 85004485028 scopus 로고
    • Purification and properties of Bacillus acidopullulyticus pullulanase (biological chemistry)
    • Kusano S, Nagahata N, Takahashi SI, Fujimoto D, Sakano Y. 1988. Purification and properties of Bacillus acidopullulyticus pullulanase (biological chemistry). Agric. Biol. Chem. 52:2293-2298.
    • (1988) Agric. Biol. Chem. , vol.52 , pp. 2293-2298
    • Kusano, S.1    Nagahata, N.2    Takahashi, S.I.3    Fujimoto, D.4    Sakano, Y.5
  • 34
    • 0021647321 scopus 로고
    • Characterization of a new class of thermophilic pullulanases from Bacillus acidopullulyticus
    • Schülein M, Højer-Pedersen B. 1984. Characterization of a new class of thermophilic pullulanases from Bacillus acidopullulyticus. Ann. N. Y. Acad. Sci. 434:271-274.
    • (1984) Ann. N. Y. Acad. Sci. , vol.434 , pp. 271-274
    • Schülein, M.1    Højer-Pedersen, B.2
  • 35
    • 0031568248 scopus 로고    scopus 로고
    • Intracellular and extracellular forms of alkaline pullulanase from an alkaliphilic Bacillus sp
    • Lee MJ, Lee YC, Kim CH. 1997. Intracellular and extracellular forms of alkaline pullulanase from an alkaliphilic Bacillus sp. S-1. Arch. Biochem. Biophys. 337:308-316.
    • (1997) S-1. Arch. Biochem. Biophys. , vol.337 , pp. 308-316
    • Lee, M.J.1    Lee, Y.C.2    Kim, C.H.3
  • 36
    • 0041379426 scopus 로고    scopus 로고
    • Isolation and purification of an acidic pullulanase type II from newly isolated Bacillus sp
    • Roy A, Messaoud EB, Bejar S. 2003. Isolation and purification of an acidic pullulanase type II from newly isolated Bacillus sp. US149. Enzyme Microb. Technol. 33:720-724.
    • (2003) US149. Enzyme Microb. Technol. , vol.33 , pp. 720-724
    • Roy, A.1    Messaoud, E.B.2    Bejar, S.3
  • 37
    • 0031580199 scopus 로고    scopus 로고
    • Protein thermal stability, hydrogen bonds, and ion pairs
    • Vogt G, Woell S, Argos P. 1997. Protein thermal stability, hydrogen bonds, and ion pairs. J. Mol. Biol. 269:631-643.
    • (1997) J. Mol. Biol. , vol.269 , pp. 631-643
    • Vogt, G.1    Woell, S.2    Argos, P.3
  • 38
    • 34248192717 scopus 로고    scopus 로고
    • Adopting selected hydrogen bonding and ionic interactions from Aspergillus fumigatus phytase structure improves the thermostability of Aspergillus niger PhyA phytase
    • Zhang W, Mullaney EJ, Lei XG. 2007. Adopting selected hydrogen bonding and ionic interactions from Aspergillus fumigatus phytase structure improves the thermostability of Aspergillus niger PhyA phytase. Appl. Environ. Microbiol. 73:3069-3076.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 3069-3076
    • Zhang, W.1    Mullaney, E.J.2    Lei, X.G.3


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