메뉴 건너뛰기




Volumn 99, Issue 13, 2015, Pages 5461-5474

The role of N1 domain on the activity, stability, substrate specificity and raw starch binding of amylopullulanase of the extreme thermophile Geobacillus thermoleovorans

Author keywords

Amylopullulanase; Geobacillus thermoleovorans; Raw starch binding; Thermostable; Truncation; X25 domain

Indexed keywords

BACTERIA; ESCHERICHIA COLI; STABILITY;

EID: 84930766492     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-014-6345-8     Document Type: Article
Times cited : (34)

References (58)
  • 1
    • 28244442802 scopus 로고    scopus 로고
    • Complexes of Thermoactinomyces vulgaris R-47 a-amylase 1 and pullulan model oligossacharides provide new insight into the mechanism for recognizing substrates with α-(1,6) glycosidic linkages
    • COI: 1:CAS:528:DC%2BD2MXhtlSqsbfI, PID: 16302977
    • Abe A, Yoshida H, Tonozuka T, Sakano Y, Kamitori S (2005) Complexes of Thermoactinomyces vulgaris R-47 a-amylase 1 and pullulan model oligossacharides provide new insight into the mechanism for recognizing substrates with α-(1,6) glycosidic linkages. FEBS J 272:6145–6153
    • (2005) FEBS J , vol.272 , pp. 6145-6153
    • Abe, A.1    Yoshida, H.2    Tonozuka, T.3    Sakano, Y.4    Kamitori, S.5
  • 2
    • 0030999008 scopus 로고    scopus 로고
    • Molecular cloning and heterologous expression of the isopullulanase gene from Aspergillus niger A.T.C.C. 9642
    • COI: 1:CAS:528:DyaK2sXjtFGltbg%3D, PID: 9169610
    • Aoki H, Yopi, Sakano Y (1997) Molecular cloning and heterologous expression of the isopullulanase gene from Aspergillus niger A.T.C.C. 9642. Biochem J 323:757–764
    • (1997) Biochem J , vol.323 , pp. 757-764
    • Aoki, H.1    Yopi2    Sakano, Y.3
  • 3
    • 85007778637 scopus 로고
    • An alkaline amylopullulanase from alkaliphilic Bacillus sp. KSM-1378; kinetic evidence for two independent active sites for the α-1,4 and α-1,6 hydrolytic reactions
    • COI: 1:CAS:528:DyaK2MXlsVSmtLY%3D
    • Ara K, Igarashi K, Saeki K, Ito S (1995) An alkaline amylopullulanase from alkaliphilic Bacillus sp. KSM-1378; kinetic evidence for two independent active sites for the α-1,4 and α-1,6 hydrolytic reactions. Biosci Biotechnol Biochem 59:662–665
    • (1995) Biosci Biotechnol Biochem , vol.59 , pp. 662-665
    • Ara, K.1    Igarashi, K.2    Saeki, K.3    Ito, S.4
  • 5
    • 2942621927 scopus 로고    scopus 로고
    • Cloning, sequencing, and characterization of a heat- and alkali-stable type I pullulanase from Anaerobranca gottschalkii
    • Bertoldo C, Armbrecht M, Becker F, Schafer T, Antranikian G, Liebl W (2004) Cloning, sequencing, and characterization of a heat- and alkali-stable type I pullulanase from Anaerobranca gottschalkii. Appl Environ Microbial 70(6):3407–3416
    • (2004) Appl Environ Microbial , vol.70 , Issue.6 , pp. 3407-3416
    • Bertoldo, C.1    Armbrecht, M.2    Becker, F.3    Schafer, T.4    Antranikian, G.5    Liebl, W.6
  • 6
    • 34748886064 scopus 로고    scopus 로고
    • The ‘pair of sugar tongs’ site on the non-catalytic domain C of barley-amylase participates in substrate binding and activity
    • COI: 1:CAS:528:DC%2BD2sXhtFeks77K, PID: 17803687
    • Bozonnet S, Jensen MT, Nielsen MM, Aghajari N, Jensen MH, Kramhoft B, Willemoes M, Tranier S, Haser R, Svensson B (2007) The ‘pair of sugar tongs’ site on the non-catalytic domain C of barley-amylase participates in substrate binding and activity. FEBS J 274:5055–5067
    • (2007) FEBS J , vol.274 , pp. 5055-5067
    • Bozonnet, S.1    Jensen, M.T.2    Nielsen, M.M.3    Aghajari, N.4    Jensen, M.H.5    Kramhoft, B.6    Willemoes, M.7    Tranier, S.8    Haser, R.9    Svensson, B.10
  • 7
    • 0032989826 scopus 로고    scopus 로고
    • The amylopullulanase of Bacillus sp. DSM 405
    • COI: 1:CAS:528:DyaK1MXitVSrurw%3D, PID: 10091322
    • Brunswick JM, Kelly CT, Fogarty WM (1999) The amylopullulanase of Bacillus sp. DSM 405. Appl Microbiol Biotechnol 51:170–175
    • (1999) Appl Microbiol Biotechnol , vol.51 , pp. 170-175
    • Brunswick, J.M.1    Kelly, C.T.2    Fogarty, W.M.3
  • 8
    • 58149200943 scopus 로고    scopus 로고
    • The carbohydrate-active enzymes database (CAZy): an expert resource for glycogenomics
    • COI: 1:CAS:528:DC%2BD1cXhsFejtL7K, PID: 18838391
    • Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, Henrissat B (2009) The carbohydrate-active enzymes database (CAZy): an expert resource for glycogenomics. Nucleic Acids Res 37:D233–D238. doi:10.1093/nar/gkn663
    • (2009) Nucleic Acids Res , vol.37 , pp. 233-238
    • Cantarel, B.L.1    Coutinho, P.M.2    Rancurel, C.3    Bernard, T.4    Lombard, V.5    Henrissat, B.6
  • 9
    • 69449083006 scopus 로고    scopus 로고
    • The carbohydrate-binding module family 20—diversity, structure, and function
    • COI: 1:CAS:528:DC%2BD1MXhtFChtrjN, PID: 19682075
    • Christiansen C, Abou Hachem M, Janecek S, Vikso-Nielsen A, Blennow A, Svensson B (2009) The carbohydrate-binding module family 20—diversity, structure, and function. FEBS J 276:5006–5029
    • (2009) FEBS J , vol.276 , pp. 5006-5029
    • Christiansen, C.1    Abou Hachem, M.2    Janecek, S.3    Vikso-Nielsen, A.4    Blennow, A.5    Svensson, B.6
  • 10
    • 77449094593 scopus 로고    scopus 로고
    • Structural features of the Nostoc punctiforme debranching enzyme reveal the basis of its mechanism and substrate specificity
    • COI: 1:CAS:528:DC%2BD1MXhsFGjsr%2FE, PID: 19768689
    • Dumbrepatil AB, Choi JH, Park JT, Kim MJ, Kim TJ, Woo EJ, Park KH (2010) Structural features of the Nostoc punctiforme debranching enzyme reveal the basis of its mechanism and substrate specificity. Proteins 78:348–356
    • (2010) Proteins , vol.78 , pp. 348-356
    • Dumbrepatil, A.B.1    Choi, J.H.2    Park, J.T.3    Kim, M.J.4    Kim, T.J.5    Woo, E.J.6    Park, K.H.7
  • 11
    • 0032908691 scopus 로고    scopus 로고
    • The type II pullulanase of Thermococcus hydrothermalis: molecular characterization of the gene and expression of the catalytic domain
    • COI: 1:CAS:528:DyaK1MXjt1yrtr8%3D, PID: 10322035
    • Erra-Pujada M, Debeire P, Duchiron F, O’Donohue MJ (1999) The type II pullulanase of Thermococcus hydrothermalis: molecular characterization of the gene and expression of the catalytic domain. J Bacteriol 181:3284–3287
    • (1999) J Bacteriol , vol.181 , pp. 3284-3287
    • Erra-Pujada, M.1    Debeire, P.2    Duchiron, F.3    O’Donohue, M.J.4
  • 12
    • 0029070171 scopus 로고
    • Omega loops: nonregular secondary structures significant in protein function and stability
    • COI: 1:CAS:528:DyaK2MXmvFCltb8%3D, PID: 7601335
    • Fetrow JS (1995) Omega loops: nonregular secondary structures significant in protein function and stability. FASEB J 9:708–717
    • (1995) FASEB J , vol.9 , pp. 708-717
    • Fetrow, J.S.1
  • 13
    • 84898463754 scopus 로고    scopus 로고
    • Enhanced thermal stability and hydrolytic ability of Bacillus subtilis aminopeptidase by removing the thermal sensitive domain in the non-catalytic region
    • Gao X, Liu Z, Cui W, Zhou L, Tian Y, Zhou Z (2014) Enhanced thermal stability and hydrolytic ability of Bacillus subtilis aminopeptidase by removing the thermal sensitive domain in the non-catalytic region. PLoS One. doi:10.1371/journal.pone.0092357
    • (2014) PLoS One
    • Gao, X.1    Liu, Z.2    Cui, W.3    Zhou, L.4    Tian, Y.5    Zhou, Z.6
  • 15
    • 0013488464 scopus 로고
    • Pore- and solid diffusion kinetics in fixed-bed adsorption under constant-pattern conditions
    • COI: 1:CAS:528:DyaF28XktVajurk%3D
    • Hall KR, Eagleton LC, Acrivos A, Vermeulen T (1966) Pore- and solid diffusion kinetics in fixed-bed adsorption under constant-pattern conditions. Ind Eng Chem Fundam 5:212–223
    • (1966) Ind Eng Chem Fundam , vol.5 , pp. 212-223
    • Hall, K.R.1    Eagleton, L.C.2    Acrivos, A.3    Vermeulen, T.4
  • 16
    • 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
    • COI: 1:CAS:528:DyaK28XlvFSqt7g%3D, PID: 8798645
    • Hatada Y, Igarashi K, Ozaki K, Ara K, Hitomi J, Kobayashi T, Kawai S, Watabe T, Ito S (1996) Amino acid sequence and molecular structure of an alkaline amylopullulanase from Bacillus that hydrolyzes α-1,4 and α-1,6 linkages in polysaccharides at different active sites. J Biol Chem 271:24075–24083
    • (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
  • 17
    • 0037423706 scopus 로고    scopus 로고
    • Three-dimensional structure and substrate binding of Bacillus stearothermophilus Neopullulanase
    • COI: 1:CAS:528:DC%2BD3sXlt12gtg%3D%3D, PID: 12547200
    • 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
  • 18
    • 0031888533 scopus 로고    scopus 로고
    • Conversion of neopullulanase α-amylase from Thermoactinomyces vulgaris R-47 into an amylopullulanase type enzyme
    • COI: 1:CAS:528:DyaK1cXit1GlsLc%3D, PID: 9538203
    • Ibuka A, Tonozuka T, Matsuzawa H, Sakai H (1998) Conversion of neopullulanase α-amylase from Thermoactinomyces vulgaris R-47 into an amylopullulanase type enzyme. J Biochem 123:275–282
    • (1998) J Biochem , vol.123 , pp. 275-282
    • Ibuka, A.1    Tonozuka, T.2    Matsuzawa, H.3    Sakai, H.4
  • 19
    • 33748670795 scopus 로고    scopus 로고
    • Amylolytic families of glycoside hydrolases: focus on the family GH-57
    • COI: 1:CAS:528:DC%2BD28XhvVCrt7c%3D
    • Janecek S (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
    • Janecek, S.1
  • 20
    • 80054683038 scopus 로고    scopus 로고
    • Structural and evolutionary aspects of two families of non-catalytic domains present in starch and glycogen binding proteins from microbes, plants and animals
    • COI: 1:CAS:528:DC%2BC3MXhtlejsr3M
    • Janecek S, Svensson B, MacGregor EA (2011) Structural and evolutionary aspects of two families of non-catalytic domains present in starch and glycogen binding proteins from microbes, plants and animals. Enzym Microb Technol 49:429–440
    • (2011) Enzym Microb Technol , vol.49 , pp. 429-440
    • Janecek, S.1    Svensson, B.2    MacGregor, E.A.3
  • 21
    • 84863239712 scopus 로고    scopus 로고
    • Association of novel domain in active site of archaic hyperthermophilic maltogenic amylase from Staphylothermus marinus
    • COI: 1:CAS:528:DC%2BC38XjsFCkurs%3D, PID: 22223643
    • Jung TY, Li D, Park JT, Yoon SM, Tran PL, Oh BH, Janeček Š, Park SG, Woo EJ, Park KH (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    Janeček, Š.7    Park, S.G.8    Woo, E.J.9    Park, K.H.10
  • 22
    • 84878425381 scopus 로고    scopus 로고
    • A high molecular-mass Anoxybacillus sp. SK3-4 amylopullulanase: characterization and its relationship in carbohydrate utilization
    • PID: 23759984
    • Kahar UM, Chan K-G, Salleh MM, Hii SM, Goh KM (2013) A high molecular-mass Anoxybacillus sp. SK3-4 amylopullulanase: characterization and its relationship in carbohydrate utilization. Int J Mol Sci 14:11302–11318
    • (2013) Int J Mol Sci , vol.14 , pp. 11302-11318
    • Kahar, U.M.1    Chan, K.-G.2    Salleh, M.M.3    Hii, S.M.4    Goh, K.M.5
  • 23
    • 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
    • COI: 1:CAS:528:DyaK1MXis1Kksbc%3D, PID: 10222200
    • 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
  • 24
    • 0032483304 scopus 로고    scopus 로고
    • Three-dimensional structure of Pseudomonas isoamylase at 2.2 A° resolution
    • COI: 1:CAS:528:DyaK1cXmtVygsrc%3D, PID: 9719642
    • Katsuya Y, Mezaki Y, Kubota M, Matsuura Y (1998) Three-dimensional 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
  • 25
    • 84989094287 scopus 로고
    • Purification and characterization of a pullulan-hydrolyzing glucoamylase from Sclerotium rolfsii
    • COI: 1:CAS:528:DyaK2cXhtVSjtrk%3D
    • Kelkar HS, Deshpande MV (1993) Purification and characterization of a pullulan-hydrolyzing glucoamylase from Sclerotium rolfsii. Starch 45(10):361–368
    • (1993) Starch , vol.45 , Issue.10 , pp. 361-368
    • Kelkar, H.S.1    Deshpande, M.V.2
  • 26
    • 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
    • COI: 1:CAS:528:DyaK2MXktV2msLw%3D, PID: 7532585
    • Kim C-H, Kim YS (1995) Substrate specificity and detailed characterization of a bifunctional amylase-pullulanase enzyme from Bacillus circulans F-2 having two different active sites on one polypeptide. Eur J Biochem 227:687–693
    • (1995) Eur J Biochem , vol.227 , pp. 687-693
    • Kim, C.-H.1    Kim, Y.S.2
  • 27
    • 57849098719 scopus 로고    scopus 로고
    • Characterization of gene encoding amylopullulanase from plant-originated lactic acid bacterium, Lactobacillus plantarum L137
    • COI: 1:CAS:528:DC%2BD1MXhvVymsrg%3D, PID: 19111640
    • Kim JH, Sunako M, Ono H, Murooka Y, Fukusaki E, Yamashita M (2008) Characterization of gene encoding amylopullulanase from plant-originated lactic acid bacterium, Lactobacillus plantarum L137. J Biosci Bioeng 106:449–459
    • (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
  • 28
    • 60949105812 scopus 로고    scopus 로고
    • Characterization of the C-terminal truncated form of amylopullulanase from Lactobacillus plantarum L137
    • COI: 1:CAS:528:DC%2BD1MXkvFGltrc%3D, PID: 19217549
    • Kim JH, Sunako M, Ono H, Murooka Y, Fukusaki E, Yamashita M (2009) Characterization of the C-terminal truncated form of amylopullulanase from Lactobacillus plantarum L137. J Biosci Bioeng 107:124–129
    • (2009) J Biosci Bioeng , vol.107 , pp. 124-129
    • Kim, J.H.1    Sunako, M.2    Ono, H.3    Murooka, Y.4    Fukusaki, E.5    Yamashita, M.6
  • 29
    • 41149148236 scopus 로고    scopus 로고
    • Combining the polymerase incomplete primer extension method for cloning and mutagenesis with microscreening to accelerate structural genomics efforts
    • Klock HE, Koesema EJ, Knuth MW, Lesley SA (2008) Combining the polymerase incomplete primer extension method for cloning and mutagenesis with microscreening to accelerate structural genomics efforts. Proteins 71:982–994
    • (2008) Proteins , vol.71 , pp. 982-994
    • Klock, H.E.1    Koesema, E.J.2    Knuth, M.W.3    Lesley, S.A.4
  • 30
    • 0025122755 scopus 로고
    • The normally periplasmic enzyme p-lactamase is specifically and efficiently translocated through the Escherichia coli outer membrane when it is fused to the cell surface enzyme pullulanase
    • COI: 1:CAS:528:DyaK3cXmtVyjt7Y%3D, PID: 2233249
    • Kornacker MG, Pugsley AP (1990) The normally periplasmic enzyme p-lactamase is specifically and efficiently translocated through the Escherichia coli outer membrane when it is fused to the cell surface enzyme pullulanase. Mol Microbiol 4:1101–1109
    • (1990) Mol Microbiol , vol.4 , pp. 1101-1109
    • Kornacker, M.G.1    Pugsley, A.P.2
  • 31
    • 84869203411 scopus 로고    scopus 로고
    • Identification of the sequence motif of glycoside hydrolase 13 family members
    • PID: 21544166
    • Kumar V (2011) Identification of the sequence motif of glycoside hydrolase 13 family members. Bioinformation 6:61–63
    • (2011) Bioinformation , vol.6 , pp. 61-63
    • Kumar, V.1
  • 32
    • 0023988701 scopus 로고
    • New type of pullulanase from Bacillus stearothermophilus and molecular cloning and expression of the gene in Bacillus subtilis
    • COI: 1:CAS:528:DyaL1cXhvVWnsr0%3D, PID: 3127377
    • Kuriki T, Okada S, Imanaka T (1988) New type of pullulanase from Bacillus stearothermophilus and molecular cloning and expression of the gene in Bacillus subtilis. J Bacteriol 170:1554–1559
    • (1988) J Bacteriol , vol.170 , pp. 1554-1559
    • Kuriki, T.1    Okada, S.2    Imanaka, T.3
  • 33
    • 0030016344 scopus 로고    scopus 로고
    • Controlling substrate preference and transglycosylation activity of neopullulanase by manipulating steric constraint and hydrophobicity in active center
    • COI: 1:CAS:528:DyaK28XksFamtLw%3D, PID: 8663322
    • Kuriki T, Kaneko H, Yanase M, Takata H, Shimada J, Handa S, Takada T, Umeyama H, Okada S (1996) Controlling substrate preference and transglycosylation activity of neopullulanase by manipulating steric constraint and hydrophobicity in active center. J Biol Chem 271:17321–17329
    • (1996) J Biol Chem , vol.271 , pp. 17321-17329
    • Kuriki, T.1    Kaneko, H.2    Yanase, M.3    Takata, H.4    Shimada, J.5    Handa, S.6    Takada, T.7    Umeyama, H.8    Okada, S.9
  • 34
    • 0028146782 scopus 로고
    • Gene cloning and characterization of α-amylase-pullulanase (AapT) from thermophilic and alkaliphilic Bacillus sp. XAL601
    • COI: 1:CAS:528:DyaK2MXhtFahu74%3D, PID: 7986049
    • Lee S-P, Morikawa M, Takagi M, Imanaka T (1994) Gene cloning and characterization of α-amylase-pullulanase (AapT) from thermophilic and alkaliphilic Bacillus sp. XAL601. Appl Environ Microbiol 60:3764–3773
    • (1994) Appl Environ Microbiol , vol.60 , pp. 3764-3773
    • Lee, S.-P.1    Morikawa, M.2    Takagi, M.3    Imanaka, T.4
  • 36
    • 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
    • COI: 1:CAS:528:DC%2BD1cXhtVekt7bM, PID: 18500431
    • Lin HY, Chuang HH, Lin FP (2008) Biochemical characterization of engineered amylopullulanase from Thermoanaerobacter ethanolicus 39E-implicating the non-necessity of its 100 C-terminal amino acid residues. Extremophiles 12:641–650
    • (2008) Extremophiles , vol.12 , pp. 641-650
    • Lin, H.Y.1    Chuang, H.H.2    Lin, F.P.3
  • 37
    • 81355147636 scopus 로고    scopus 로고
    • Biochemical characterization of two truncated forms of amylopullulanase from Thermoanaerobacterium saccharolyticum NTOU1 to identify its enzymatically active region
    • COI: 1:CAS:528:DC%2BC3MXhsVars7rO, PID: 21750992
    • Lin FP, Ma HY, Lin HJ, Liu SM, Tzou WS (2011) Biochemical characterization of two truncated forms of amylopullulanase from Thermoanaerobacterium saccharolyticum NTOU1 to identify its enzymatically active region. Appl Biochem Biotechnol 165:1047–1056
    • (2011) Appl Biochem Biotechnol , vol.165 , pp. 1047-1056
    • Lin, F.P.1    Ma, H.Y.2    Lin, H.J.3    Liu, S.M.4    Tzou, W.S.5
  • 38
    • 71849104860 scopus 로고
    • Protein measurement with the Folin phenol reagent
    • COI: 1:CAS:528:DyaG38XhsVyrsw%3D%3D, PID: 14907713
    • Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265–275
    • (1951) J Biol Chem , vol.193 , pp. 265-275
    • Lowry, O.H.1    Rosebrough, N.J.2    Farr, A.L.3    Randall, R.J.4
  • 39
    • 84894338490 scopus 로고    scopus 로고
    • Enhanced thermal stability of Pseudomonas aeruginosa lipoxygenase through modification of two highly flexible regions
    • COI: 1:CAS:528:DC%2BC2cXitFyisb4%3D, PID: 23793260
    • Lu X, Liu S, Feng Y, Rao S, Zhou X, Wang M, Du G, Chen J (2014) Enhanced thermal stability of Pseudomonas aeruginosa lipoxygenase through modification of two highly flexible regions. Appl Microbiol Biotechnol 98:1663–1669
    • (2014) Appl Microbiol Biotechnol , vol.98 , pp. 1663-1669
    • Lu, X.1    Liu, S.2    Feng, Y.3    Rao, S.4    Zhou, X.5    Wang, M.6    Du, G.7    Chen, J.8
  • 40
    • 0035831255 scopus 로고    scopus 로고
    • Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes
    • COI: 1:CAS:528:DC%2BD3MXhvVagtLk%3D, PID: 11257505
    • MacGregor EA, Janecek S, Svensson B (2001) Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes. Biochim Biophys Acta 1546:1–20
    • (2001) Biochim Biophys Acta , vol.1546
    • MacGregor, E.A.1    Janecek, S.2    Svensson, B.3
  • 41
    • 0031779918 scopus 로고    scopus 로고
    • Design, structure and stability of a hyperthermophilic protein variant
    • COI: 1:CAS:528:DyaK1cXjslCktb4%3D
    • Malakauskas SM, Mayo SL (1998) Design, structure and stability of a hyperthermophilic protein variant. Nat Struct Mol Biol 5:470–475
    • (1998) Nat Struct Mol Biol , vol.5 , pp. 470-475
    • Malakauskas, S.M.1    Mayo, S.L.2
  • 42
    • 0024287178 scopus 로고
    • Purification and some properties of the extracellular α-amylase pullulanase produced by Clostridium thermohydrosulfuricum
    • COI: 1:CAS:528:DyaL1cXhs1ekurs%3D, PID: 3260488
    • Melasniemi H (1988) Purification and some properties of the extracellular α-amylase pullulanase produced by Clostridium thermohydrosulfuricum. Biochem J 250:813–8
    • (1988) Biochem J , vol.250 , pp. 813-818
    • Melasniemi, H.1
  • 43
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • COI: 1:CAS:528:DyaG1MXmtFKiuw%3D%3D
    • Miller GL (1959) Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal Chem 31:426–428
    • (1959) Anal Chem , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 44
    • 84879842967 scopus 로고    scopus 로고
    • Characterization of recombinant amylopullulanase (gt-apu) and truncated amylopullulanase (gt-apuT) of the extreme thermophile Geobacillus thermoleovorans NP33 and their action in starch saccharification
    • COI: 1:CAS:528:DC%2BC3sXhtVCrt73J, PID: 23132347
    • Nisha M, Satyanarayana T (2013a) Characterization of recombinant amylopullulanase (gt-apu) and truncated amylopullulanase (gt-apuT) of the extreme thermophile Geobacillus thermoleovorans NP33 and their action in starch saccharification. Appl Microbiol Biotechnol 97:6279–6292
    • (2013) Appl Microbiol Biotechnol , vol.97 , pp. 6279-6292
    • Nisha, M.1    Satyanarayana, T.2
  • 45
    • 84887560848 scopus 로고    scopus 로고
    • Recombinant bacterial amylopullulanases: developments and perspectives
    • Nisha M, Satyanarayana T (2013b) Recombinant bacterial amylopullulanases: developments and perspectives. Bioengineered 4:1–13
    • (2013) Bioengineered , vol.4
    • Nisha, M.1    Satyanarayana, T.2
  • 46
    • 84897060453 scopus 로고    scopus 로고
    • A starch-binding domain identified in α-amylase (AmyP) represents a new family of carbohydrate-binding modules that contribute to enzymatic hydrolysis of soluble starch
    • COI: 1:CAS:528:DC%2BC2cXktlWjtL0%3D, PID: 24613924
    • Peng H, Zheng Y, Chen M, Wang Y, Xiao Y, Gao Y (2014) A starch-binding domain identified in α-amylase (AmyP) represents a new family of carbohydrate-binding modules that contribute to enzymatic hydrolysis of soluble starch. FEBS Lett 588:1161–1167
    • (2014) FEBS Lett , vol.588 , pp. 1161-1167
    • Peng, H.1    Zheng, Y.2    Chen, M.3    Wang, Y.4    Xiao, Y.5    Gao, Y.6
  • 47
    • 0026629976 scopus 로고
    • Macroamylases: differences in activity against various-sized substrates
    • COI: 1:CAS:528:DyaK38Xmt1yku7Y%3D, PID: 1381999
    • Rosenblum JL, Hortin GL, Smith CH, Pashos GE, Landt M (1992) Macroamylases: differences in activity against various-sized substrates. Clin Chem 38:1725–1729
    • (1992) Clin Chem , vol.38 , pp. 1725-1729
    • Rosenblum, J.L.1    Hortin, G.L.2    Smith, C.H.3    Pashos, G.E.4    Landt, M.5
  • 48
    • 2342584768 scopus 로고    scopus 로고
    • Development of an ideal starch saccharification process using amylolytic enzymes from thermophiles
    • COI: 1:CAS:528:DC%2BD2cXjtVSgtbc%3D, PID: 15046588
    • Satyanarayana T, Noorwez SM, Kumar S, Rao JL, Ezhilvannan M, Kaur P (2004) Development of an ideal starch saccharification process using amylolytic enzymes from thermophiles. Biochem Soc Trans 32:276–278
    • (2004) Biochem Soc Trans , vol.32 , pp. 276-278
    • Satyanarayana, T.1    Noorwez, S.M.2    Kumar, S.3    Rao, J.L.4    Ezhilvannan, M.5    Kaur, P.6
  • 49
    • 33845665889 scopus 로고    scopus 로고
    • Dividing the large glycoside hydrolase family 13 into subfamilies: towards improved functional annotations of α-amylase-related proteins
    • COI: 1:CAS:528:DC%2BD28Xht1Ohu7rJ, PID: 17085431
    • Stam MR, Danchin EG, Rancurel C, Coutinho PM, 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.2    Rancurel, C.3    Coutinho, P.M.4    Henrissat, B.5
  • 51
    • 41949118483 scopus 로고    scopus 로고
    • Crystal structure of the polyextremophilic α-amylase AmyB from Halothermothrix orenii: details of a productive enzyme-substrate complex and an N domain with a role in binding raw starch
    • PID: 18387632
    • Tan TC, Mijts BN, Swaminathan K, Patel BKC, Divne C (2008) Crystal structure of the polyextremophilic α-amylase AmyB from Halothermothrix orenii: details of a productive enzyme-substrate complex and an N domain with a role in binding raw starch. J Mol Biol 378:852–870
    • (2008) J Mol Biol , vol.378 , pp. 852-870
    • Tan, T.C.1    Mijts, B.N.2    Swaminathan, K.3    Patel, B.K.C.4    Divne, C.5
  • 52
    • 0029089389 scopus 로고
    • Comparison of primary structures and substrate specificities of two pullulan-hydrolyzing α-amylases, TVA I and TVA II, from Thermoactinomyces vulgaris R-47
    • PID: 7548164
    • Tonozuka T, Mogi S, Shimura Y, Ibuka A, Sakai H, Matsuzawa H, Sakano Y, Ohta T (1995) Comparison of primary structures and substrate specificities of two pullulan-hydrolyzing α-amylases, TVA I and TVA II, from Thermoactinomyces vulgaris R-47. Biochim Biophys Acta 1252:35–42
    • (1995) Biochim Biophys Acta , vol.1252 , pp. 35-42
    • Tonozuka, T.1    Mogi, S.2    Shimura, Y.3    Ibuka, A.4    Sakai, H.5    Matsuzawa, H.6    Sakano, Y.7    Ohta, T.8
  • 55
    • 0031471066 scopus 로고    scopus 로고
    • Amino acid residues specific for the catalytic action towards α-1,6-glucosidic linkages in Klebsiella pullulanase
    • COI: 1:CAS:528:DyaK2sXntlyjt78%3D
    • Yamashita M, Matsumoto D, Murooka Y (1997) Amino acid residues specific for the catalytic action towards α-1,6-glucosidic linkages in Klebsiella pullulanase. J Ferment Bioeng 84:283–290
    • (1997) J Ferment Bioeng , vol.84 , pp. 283-290
    • Yamashita, M.1    Matsumoto, D.2    Murooka, Y.3
  • 56
    • 0008107233 scopus 로고    scopus 로고
    • Upregulation of cytosolic chaperonin CCT subunits during recovery from chemical stress that causes accumulation of unfolded proteins
    • COI: 1:CAS:528:DC%2BD3cXit1ars7c%3D, PID: 10712596
    • Yokota SI, Yanagi H, Yura T, Kubota H (2000) Upregulation of cytosolic chaperonin CCT subunits during recovery from chemical stress that causes accumulation of unfolded proteins. Eur J Biochem 267:1658–1664
    • (2000) Eur J Biochem , vol.267 , pp. 1658-1664
    • Yokota, S.I.1    Yanagi, H.2    Yura, T.3    Kubota, H.4
  • 57
    • 71249091193 scopus 로고    scopus 로고
    • Purification and characterization of a novel amylopullulanase that converts pullulan to glucose, maltose, and maltotriose and starch to glucose and maltose
    • COI: 1:CAS:528:DC%2BD1MXhsFGgs73J
    • Zareian S, Khajeh K, Ranjbar B, Dabirmanesh B, Ghollasi M, Mollania N (2010) Purification and characterization of a novel amylopullulanase that converts pullulan to glucose, maltose, and maltotriose and starch to glucose and maltose. Enzym Microb Technol 46:57–63
    • (2010) Enzym Microb Technol , vol.46 , pp. 57-63
    • Zareian, S.1    Khajeh, K.2    Ranjbar, B.3    Dabirmanesh, B.4    Ghollasi, M.5    Mollania, N.6
  • 58
    • 77953117957 scopus 로고    scopus 로고
    • Enhancing the thermostability of α-glucosidase from Thermoanaerobacter tengcongensis MB4 by single proline substitution
    • COI: 1:CAS:528:DC%2BC3cXhtF2lsrvM, PID: 20541109
    • Zhou C, Xue Y, Ma Y (2010) Enhancing the thermostability of α-glucosidase from Thermoanaerobacter tengcongensis MB4 by single proline substitution. J Biosci Bioeng 110:12–17
    • (2010) J Biosci Bioeng , vol.110 , pp. 12-17
    • Zhou, C.1    Xue, Y.2    Ma, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.