메뉴 건너뛰기




Volumn 81, Issue 6, 2015, Pages 1977-1987

AmyM, a novel maltohexaose-forming α-amylase from Corallococcus sp. strain EGB

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY CHROMATOGRAPHY; AMINO ACIDS; CLONING; ESCHERICHIA COLI; MASS SPECTROMETRY; PEPTIDES; POLYACRYLATES; PURIFICATION; SOAPS (DETERGENTS); STARCH;

EID: 84924690340     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.03934-14     Document Type: Article
Times cited : (53)

References (57)
  • 1
    • 84876681193 scopus 로고    scopus 로고
    • A highly thermoactive and salt-tolerant α-amylase isolated from a pilot-plant biogas reactor
    • Jabbour D, Sorger A, Sahm K, Antranikian G. 2013. A highly thermoactive and salt-tolerant α-amylase isolated from a pilot-plant biogas reactor. Appl Microbiol Biotechnol 97:2971-2978. http://dx.doi.org/10.1007/s00253-012-4194-x.
    • (2013) Appl Microbiol Biotechnol , vol.97 , pp. 2971-2978
    • Jabbour, D.1    Sorger, A.2    Sahm, K.3    Antranikian, G.4
  • 2
    • 37449020231 scopus 로고    scopus 로고
    • Production of surfactant and detergentstable, halophilic, and alkalitolerant alpha-amylase by a moderately halophilic Bacillus sp. strain TSCVKK
    • Kiran KK, Chandra T. 2008. Production of surfactant and detergentstable, halophilic, and alkalitolerant alpha-amylase by a moderately halophilic Bacillus sp. strain TSCVKK. Appl Microbiol Biotechnol 77:1023-1031. http://dx.doi.org/10.1007/s00253-007-1250-z.
    • (2008) Appl Microbiol Biotechnol , vol.77 , pp. 1023-1031
    • Kiran, K.K.1    Chandra, T.2
  • 3
    • 0037187437 scopus 로고    scopus 로고
    • Properties and applications of starch-converting enzymes of the α-amylase family
    • Van Der Maarel MJ, Van Der Veen B, Uitdehaag J, Leemhuis H, Dijkhuizen L. 2002. Properties and applications of starch-converting enzymes of the α-amylase family. J Biotechnol 94:137-155. http://dx.doi.org/10.1016/S0168-1656(01)00407-2.
    • (2002) J Biotechnol , vol.94 , pp. 137-155
    • Van Der Maarel, M.J.1    Van Der Veen, B.2    Uitdehaag, J.3    Leemhuis, H.4    Dijkhuizen, L.5
  • 4
    • 84899863334 scopus 로고    scopus 로고
    • α-Amylase: an enzyme specificity found in various families of glycoside hydrolases
    • Janeček Š, Svensson B, MacGregor EA. 2014. α-Amylase: an enzyme specificity found in various families of glycoside hydrolases. Cell Mol Life Sci 71:1149-1170. http://dx.doi.org/10.1007/s00018-013-1388-z.
    • (2014) Cell Mol Life Sci , vol.71 , pp. 1149-1170
    • Janeček, Š.1    Svensson, B.2    MacGregor, E.A.3
  • 5
    • 77952879225 scopus 로고    scopus 로고
    • Molecular cloning and characterization of amylase from soil metagenomic library derived from Northwestern Himalayas
    • Sharma S, Khan FG, Qazi GN. 2010. Molecular cloning and characterization of amylase from soil metagenomic library derived from Northwestern Himalayas. Appl Microbiol Biotechnol 86:1821-1828. http://dx.doi.org/10.1007/s00253-009-2404-y.
    • (2010) Appl Microbiol Biotechnol , vol.86 , pp. 1821-1828
    • Sharma, S.1    Khan, F.G.2    Qazi, G.N.3
  • 6
    • 0035318737 scopus 로고    scopus 로고
    • Novel α-amylase that is highly resistant to chelating reagents and chemical oxidants from the alkaliphilic Bacillus isolate KSM-K38
    • Hagihara H, Igarashi K, Hayashi Y, Endo K, Ikawa-Kitayama K, Ozaki K, Kawai S, Ito S. 2001. Novel α-amylase that is highly resistant to chelating reagents and chemical oxidants from the alkaliphilic Bacillus isolate KSM-K38. Appl Environ Microbiol 67:1744-1750. http://dx.doi.org/10.1128/AEM.67.4.1744-1750.2001.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 1744-1750
    • Hagihara, H.1    Igarashi, K.2    Hayashi, Y.3    Endo, K.4    Ikawa-Kitayama, K.5    Ozaki, K.6    Kawai, S.7    Ito, S.8
  • 7
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability
    • Vieille C, Zeikus GJ. 2001. Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol Mol Biol Rev 65:1-43. http://dx.doi.org/10.1128/MMBR.65.1.1-43.2001.
    • (2001) Microbiol Mol Biol Rev , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 8
    • 33750157980 scopus 로고    scopus 로고
    • A thermostable α-amylase from a moderately thermophilic Bacillus subtilis strain for starch processing
    • Asgher M, Asad MJ, Rahman S, Legge R. 2007. A thermostable α-amylase from a moderately thermophilic Bacillus subtilis strain for starch processing. J Food Eng 79:950-955. http://dx.doi.org/10.1016/j.jfoodeng.2005.12.053.
    • (2007) J Food Eng , vol.79 , pp. 950-955
    • Asgher, M.1    Asad, M.J.2    Rahman, S.3    Legge, R.4
  • 9
    • 84861715330 scopus 로고    scopus 로고
    • Salt-independent thermophilic α-amylase from Bacillus megaterium VUMB109: an efficacy testing for preparation of maltooligosaccharides
    • Jana M, Maity C, Samanta S, Pati BR, Islam SS, Mohapatra PKD, Mondal KC. 2013. Salt-independent thermophilic α-amylase from Bacillus megaterium VUMB109: an efficacy testing for preparation of maltooligosaccharides. Ind Crops Prod 41:386-391. http://dx.doi.org/10.1016/j.indcrop.2012.04.048.
    • (2013) Ind Crops Prod , vol.41 , pp. 386-391
    • Jana, M.1    Maity, C.2    Samanta, S.3    Pati, B.R.4    Islam, S.S.5    Mohapatra, P.K.D.6    Mondal, K.C.7
  • 10
    • 33845672228 scopus 로고    scopus 로고
    • Enhancement of acid amylase production by an isolated Aspergillus awamori
    • Prakasham R, Subba Rao C, Sreenivas Rao R, Sarma P. 2007. Enhancement of acid amylase production by an isolated Aspergillus awamori. J Appl Microbiol 102:204-211. http://dx.doi.org/10.1111/j.1365-2672.2006.03058.x.
    • (2007) J Appl Microbiol , vol.102 , pp. 204-211
    • Prakasham, R.1    Subba Rao, C.2    Sreenivas Rao, R.3    Sarma, P.4
  • 11
    • 78649327448 scopus 로고    scopus 로고
    • Characterization and stability studies on surfactant, detergent and oxidant stable α-amylase from marine haloalkaliphilic Saccharopolyspora sp. A9
    • Chakraborty S, Khopade A, Biao R, Jian W, Liu XY, Mahadik K, Chopade B, Zhang L, Kokare C. 2011. Characterization and stability studies on surfactant, detergent and oxidant stable α-amylase from marine haloalkaliphilic Saccharopolyspora sp. A9. J Mol Catal B Enzym 68: 52-58. http://dx.doi.org/10.1016/j.molcatb.2010.09.009.
    • (2011) J Mol Catal B Enzym , vol.68 , pp. 52-58
    • Chakraborty, S.1    Khopade, A.2    Biao, R.3    Jian, W.4    Liu, X.Y.5    Mahadik, K.6    Chopade, B.7    Zhang, L.8    Kokare, C.9
  • 12
    • 79951674162 scopus 로고    scopus 로고
    • Purification and characterization of an organic-solvent-tolerant halophilic α-amylase from the moderately halophilic Nesterenkonia sp. strain F
    • Shafiei M, Ziaee AA, Amoozegar MA. 2011. Purification and characterization of an organic-solvent-tolerant halophilic α-amylase from the moderately halophilic Nesterenkonia sp. strain F. J Ind Microbiol Biotechnol 38:275-281. http://dx.doi.org/10.1007/s10295-010-0770-1.
    • (2011) J Ind Microbiol Biotechnol , vol.38 , pp. 275-281
    • Shafiei, M.1    Ziaee, A.A.2    Amoozegar, M.A.3
  • 13
    • 33748784641 scopus 로고    scopus 로고
    • Production of oligosaccharides as promising new food additive generation
    • Barreteau H, Delattre C, Michaud P. 2006. Production of oligosaccharides as promising new food additive generation. Food Technol Biotechnol 44:323-333.
    • (2006) Food Technol Biotechnol , vol.44 , pp. 323-333
    • Barreteau, H.1    Delattre, C.2    Michaud, P.3
  • 14
    • 0028171101 scopus 로고
    • A constitutive maltotetraose-producing amylase from Pseudomonas sp. IMD 353
    • Fogarty W, Bourke A, Kelly C, Doyle E. 1994. A constitutive maltotetraose-producing amylase from Pseudomonas sp. IMD 353. Appl Microbiol Biotechnol 42:198-203.
    • (1994) Appl Microbiol Biotechnol , vol.42 , pp. 198-203
    • Fogarty, W.1    Bourke, A.2    Kelly, C.3    Doyle, E.4
  • 15
    • 0026480142 scopus 로고
    • Cloning and nucleotide sequence of the maltopentaose-forming amylase gene from Pseudomonas sp. KO-8940
    • Shida O, Takano T, Takagi H, Kadowaki K, Kobayashi S. 1992. Cloning and nucleotide sequence of the maltopentaose-forming amylase gene from Pseudomonas sp. KO-8940. Biosci Biotechnol Biochem 56:76-80.
    • (1992) Biosci Biotechnol Biochem , vol.56 , pp. 76-80
    • Shida, O.1    Takano, T.2    Takagi, H.3    Kadowaki, K.4    Kobayashi, S.5
  • 16
    • 0024380583 scopus 로고
    • Structurally similar but functionally distinct factors, IRF-1 and IRF-2, bind to the same regulatory elements of IFN and IFN-inducible genes
    • Harada H, Fujita T, Miyamoto M, Kimura Y, Maruyama M, Furia A, Miyata T, Taniguchi T. 1989. Structurally similar but functionally distinct factors, IRF-1 and IRF-2, bind to the same regulatory elements of IFN and IFN-inducible genes. Cell 58:729-739. http://dx.doi.org/10.1016/0092-8674(89)90107-4.
    • (1989) Cell , vol.58 , pp. 729-739
    • Harada, H.1    Fujita, T.2    Miyamoto, M.3    Kimura, Y.4    Maruyama, M.5    Furia, A.6    Miyata, T.7    Taniguchi, T.8
  • 17
    • 0015405864 scopus 로고
    • Isolation and action pattern of maltohexaose producing amylase from Aerobacter aerogenes
    • Kainuma K, Kobayashi S, Ito T, Suzuki S. 1972. Isolation and action pattern of maltohexaose producing amylase from Aerobacter aerogenes. FEBS Lett 26:281-285. http://dx.doi.org/10.1016/0014-5793(72)80593-3.
    • (1972) FEBS Lett , vol.26 , pp. 281-285
    • Kainuma, K.1    Kobayashi, S.2    Ito, T.3    Suzuki, S.4
  • 18
    • 0030295006 scopus 로고    scopus 로고
    • Production, properties and applications of food-grade oligosaccharides
    • Crittenden R, Playne MJ. 1996. Production, properties and applications of food-grade oligosaccharides. Trends Food Sci Technol 7:353-361. http://dx.doi.org/10.1016/S0924-2244(96)10038-8.
    • (1996) Trends Food Sci Technol , vol.7 , pp. 353-361
    • Crittenden, R.1    Playne, M.J.2
  • 19
    • 80052026472 scopus 로고    scopus 로고
    • Digestibility and physicochemical properties of rice (Oryza sativa) flours and starches differing in amylose content
    • Zhu LJ, Liu QQ, Wilson JD, Gu MH, Shi YC. 2011. Digestibility and physicochemical properties of rice (Oryza sativa) flours and starches differing in amylose content. Carbohydr Polym 86:1751-1759. http://dx.doi.org/10.1016/j.carbpol.2011.07.017.
    • (2011) Carbohydr Polym , vol.86 , pp. 1751-1759
    • Zhu, L.J.1    Liu, Q.Q.2    Wilson, J.D.3    Gu, M.H.4    Shi, Y.C.5
  • 20
    • 0033068941 scopus 로고    scopus 로고
    • The ecology of the myxobacteria
    • Reichenbach H. 1999. The ecology of the myxobacteria. Environ Microbiol 1:15-21. http://dx.doi.org/10.1046/j.1462-2920.1999.00016.x.
    • (1999) Environ Microbiol , vol.1 , pp. 15-21
    • Reichenbach, H.1
  • 22
    • 0017837871 scopus 로고
    • Purification and properties of an extracellular protease from Myxococcus virescens
    • Gnosspelius G. 1978. Purification and properties of an extracellular protease from Myxococcus virescens. J Bacteriol 133:17-25.
    • (1978) J Bacteriol , vol.133 , pp. 17-25
    • Gnosspelius, G.1
  • 24
    • 0028171279 scopus 로고
    • Purification and characterization of an endo-N-acetyl-beta-D-glucosaminidase from the culture medium of Stigmatella aurantiaca DW4
    • Bourgerie S, Karamanos Y, Grard T, Julien R. 1994. Purification and characterization of an endo-N-acetyl-beta-D-glucosaminidase from the culture medium of Stigmatella aurantiaca DW4. J Bacteriol 176:6170-6174.
    • (1994) J Bacteriol , vol.176 , pp. 6170-6174
    • Bourgerie, S.1    Karamanos, Y.2    Grard, T.3    Julien, R.4
  • 25
    • 80055062488 scopus 로고    scopus 로고
    • A novel cold-adapted lipase from Sorangium cellulosum strain So0157-2: gene cloning, expression, and enzymatic characterization
    • Cheng YY, Qian YK, Li ZF, Wu ZH, Liu H, Li YZ. 2011. A novel cold-adapted lipase from Sorangium cellulosum strain So0157-2: gene cloning, expression, and enzymatic characterization. Int J Mol Sci 12: 6765-6780. http://dx.doi.org/10.3390/ijms12106765.
    • (2011) Int J Mol Sci , vol.12 , pp. 6765-6780
    • Cheng, Y.Y.1    Qian, Y.K.2    Li, Z.F.3    Wu, Z.H.4    Liu, H.5    Li, Y.Z.6
  • 26
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller GL. 1959. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal Chem 31:426-428. http://dx.doi.org/10.1021/ac60147a030.
    • (1959) Anal Chem , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 27
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254. http://dx.doi.org/10.1016/0003-2697(76)90527-3.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 28
    • 0001757520 scopus 로고
    • The glycogen-amylase complex as a means of obtaining highly purified α-amylases
    • Loyter A, Schramm M. 1962. The glycogen-amylase complex as a means of obtaining highly purified α-amylases. Biochim Biophys Acta 65:200-206.
    • (1962) Biochim Biophys Acta , vol.65 , pp. 200-206
    • Loyter, A.1    Schramm, M.2
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685. http://dx.doi.org/10.1038/227680a0.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 79954424004 scopus 로고    scopus 로고
    • Purification and characterization of novel α-amylase from Bacillus subtilis KIBGE HAS
    • Bano S, Qader SAU, Aman A, Syed MN, Azhar A. 2011. Purification and characterization of novel α-amylase from Bacillus subtilis KIBGE HAS. AAPS Pharmscitech 12:255-261. http://dx.doi.org/10.1208/s12249-011-9586-1.
    • (2011) AAPS Pharmscitech , vol.12 , pp. 255-261
    • Bano, S.1    Qader, S.A.U.2    Aman, A.3    Syed, M.N.4    Azhar, A.5
  • 31
    • 0037213678 scopus 로고    scopus 로고
    • Gene cloning, sequencing, and characterization of a family 9 endoglucanase (CelA) with an unusual pattern of activity from the thermoacidophile Alicyclobacillus acidocaldarius ATCC27009
    • Eckert K, Zielinski F, Leggio LL, Schneider E. 2002. Gene cloning, sequencing, and characterization of a family 9 endoglucanase (CelA) with an unusual pattern of activity from the thermoacidophile Alicyclobacillus acidocaldarius ATCC27009. Appl Microbiol Biotechnol 60:428-436. http://dx.doi.org/10.1007/s00253-002-1131-4.
    • (2002) Appl Microbiol Biotechnol , vol.60 , pp. 428-436
    • Eckert, K.1    Zielinski, F.2    Leggio, L.L.3    Schneider, E.4
  • 32
    • 41549139096 scopus 로고    scopus 로고
    • Purification and biochemical characterization of a novel α-amylase from Bacillus licheniformis NH1: cloning, nucleotide sequence and expression of amyN gene in Escherichia coli
    • Hmidet N, Bayoudh A, Berrin JG, Kanoun S, Juge N, Nasri M. 2008. Purification and biochemical characterization of a novel α-amylase from Bacillus licheniformis NH1: cloning, nucleotide sequence and expression of amyN gene in Escherichia coli. Process Biochem 43:499-510. http://dx.doi.org/10.1016/j.procbio.2008.01.017.
    • (2008) Process Biochem , vol.43 , pp. 499-510
    • Hmidet, N.1    Bayoudh, A.2    Berrin, J.G.3    Kanoun, S.4    Juge, N.5    Nasri, M.6
  • 33
    • 0020607566 scopus 로고
    • In situ transposon replacement and isolation of a spontaneous tandem genetic duplication
    • Avery L, Kaiser D. 1983. In situ transposon replacement and isolation of a spontaneous tandem genetic duplication. Mol Gen Genet 191:99-109.
    • (1983) Mol Gen Genet , vol.191 , pp. 99-109
    • Avery, L.1    Kaiser, D.2
  • 34
    • 84864004325 scopus 로고    scopus 로고
    • Complete genome sequence of the fruiting myxobacterium Corallococcus coralloides DSM 2259
    • Huntley S, Zhang Y, Treuner-Lange A, Kneip S, Sensen CW, Søgaard-Andersen L. 2012. Complete genome sequence of the fruiting myxobacterium Corallococcus coralloides DSM 2259. J Bacteriol 194:3012-3013. http://dx.doi.org/10.1128/JB.00397-12.
    • (2012) J Bacteriol , vol.194 , pp. 3012-3013
    • Huntley, S.1    Zhang, Y.2    Treuner-Lange, A.3    Kneip, S.4    Sensen, C.W.5    Søgaard-Andersen, L.6
  • 35
    • 0025946803 scopus 로고
    • Rapid and efficient purification of native histidine-tagged protein expressed by recombinant vaccinia virus
    • Janknecht R, de Martynoff G, Lou J, Hipskind RA, Nordheim A, Stunnenberg HG. 1991. Rapid and efficient purification of native histidine-tagged protein expressed by recombinant vaccinia virus. Proc Natl Acad Sci USA 88:8972-8976. http://dx.doi.org/10.1073/pnas.88.20.8972.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8972-8976
    • Janknecht, R.1    de Martynoff, G.2    Lou, J.3    Hipskind, R.A.4    Nordheim, A.5    Stunnenberg, H.G.6
  • 36
    • 84896699717 scopus 로고    scopus 로고
    • Production, purification, and characterization of α-amylase from solventogenic Clostridium sp. BOH3
    • Rajagopalan G, He J, Yang KL. 2014. Production, purification, and characterization of α-amylase from solventogenic Clostridium sp. BOH3. Bioenergy Res 7:132-141. http://dx.doi.org/10.1007/s12155-013-9356-x.
    • (2014) Bioenergy Res , vol.7 , pp. 132-141
    • Rajagopalan, G.1    He, J.2    Yang, K.L.3
  • 37
    • 33646883028 scopus 로고    scopus 로고
    • Reaction pattern of a novel thermostable a-amylase
    • Napaporn A, Jaylin J, Geoffrey H. 2006. Reaction pattern of a novel thermostable a-amylase. Carbohydr Polym 64:582-588. http://dx.doi.org/10.1016/j.carbpol.2005.11.014.
    • (2006) Carbohydr Polym , vol.64 , pp. 582-588
    • Napaporn, A.1    Jaylin, J.2    Geoffrey, H.3
  • 38
    • 0037102815 scopus 로고    scopus 로고
    • Molecular weights and gyration radii of amylopectins determined by high-performance size-exclusion chromatography equipped with multi-angel laser-light scattering and refractive index detectors
    • Sang HY, Jaylin J. 2002. Molecular weights and gyration radii of amylopectins determined by high-performance size-exclusion chromatography equipped with multi-angel laser-light scattering and refractive index detectors. Carbohydr Polym 49:307-314. http://dx.doi.org/10.1016/S0144-8617(01)00339-3.
    • (2002) Carbohydr Polym , vol.49 , pp. 307-314
    • Sang, H.Y.1    Jaylin, J.2
  • 42
    • 13844296633 scopus 로고    scopus 로고
    • Yersinia pestis outer membrane type III secretion protein YscC: expression, purification, characterization, and induction of specific antiserum
    • Goodin JL, Raab RW, McKown RL, Coffman GL, Powell BS, Enama JT, Ligon JA, Andrews GP. 2005. Yersinia pestis outer membrane type III secretion protein YscC: expression, purification, characterization, and induction of specific antiserum. Protein Expr Purif 40:152-163. http://dx.doi.org/10.1016/j.pep.2004.11.001.
    • (2005) Protein Expr Purif , vol.40 , pp. 152-163
    • Goodin, J.L.1    Raab, R.W.2    McKown, R.L.3    Coffman, G.L.4    Powell, B.S.5    Enama, J.T.6    Ligon, J.A.7    Andrews, G.P.8
  • 46
  • 47
    • 0023810007 scopus 로고
    • Cloning of a gene for maltohexaose producing amylase of an alkalophilic Bacillus and hyper-production of the enzyme in Bacillus subtilis cells
    • Kimura K, Tsukamoto A, Ishii Y, Takano T, Yamane K. 1988. Cloning of a gene for maltohexaose producing amylase of an alkalophilic Bacillus and hyper-production of the enzyme in Bacillus subtilis cells. Appl Microbiol Biotechnol 27:372-377.
    • (1988) Appl Microbiol Biotechnol , vol.27 , pp. 372-377
    • Kimura, K.1    Tsukamoto, A.2    Ishii, Y.3    Takano, T.4    Yamane, K.5
  • 49
    • 0032896156 scopus 로고    scopus 로고
    • A thermostable α-amylase producing maltohexaose from a new isolated Bacillus sp. US100: study of activity and molecular cloning of the corresponding gene
    • Ali MB, Mezghani M, Bejar S. 1999. A thermostable α-amylase producing maltohexaose from a new isolated Bacillus sp. US100: study of activity and molecular cloning of the corresponding gene. Enzyme Microb Technol 24:584-589.
    • (1999) Enzyme Microb Technol , vol.24 , pp. 584-589
    • Ali, M.B.1    Mezghani, M.2    Bejar, S.3
  • 51
    • 0038301861 scopus 로고    scopus 로고
    • Microbial α-amylases: a biotechnological perspective
    • Gupta R, Gigras P, Mohapatra H, Goswami VK, Chauhan B. 2003. Microbial α-amylases: a biotechnological perspective. Process Biochem 38:1599-1616. http://dx.doi.org/10.1016/S0032-9592(03)00053-0.
    • (2003) Process Biochem , vol.38 , pp. 1599-1616
    • Gupta, R.1    Gigras, P.2    Mohapatra, H.3    Goswami, V.K.4    Chauhan, B.5
  • 53
    • 0034693313 scopus 로고    scopus 로고
    • Purification and characterisation of a malto-oligosaccharide-forming amylase active at high pH from Bacillus clausii BT-21
    • Duedahl-Olesen L, Kragh KM, Zimmermann W. 2000. Purification and characterisation of a malto-oligosaccharide-forming amylase active at high pH from Bacillus clausii BT-21. Carbohydr Res 329:97-107. http://dx.doi.org/10.1016/S0008-6215(00)00153-1.
    • (2000) Carbohydr Res , vol.329 , pp. 97-107
    • Duedahl-Olesen, L.1    Kragh, K.M.2    Zimmermann, W.3
  • 54
    • 35748961088 scopus 로고    scopus 로고
    • Purification and characterization of a maltooligosaccharide-forming amylase that improves product selectivity in water-miscible organic solvents, from dimethylsulfoxide-tolerant Brachybacterium sp. strain LB25
    • Doukyu N, Yamagishi W, Kuwahara H, Ogino H, Furuki N. 2007. Purification and characterization of a maltooligosaccharide-forming amylase that improves product selectivity in water-miscible organic solvents, from dimethylsulfoxide-tolerant Brachybacterium sp. strain LB25. Extremophiles 11:781-788. http://dx.doi.org/10.1007/s00792-007-0096-8.
    • (2007) Extremophiles , vol.11 , pp. 781-788
    • Doukyu, N.1    Yamagishi, W.2    Kuwahara, H.3    Ogino, H.4    Furuki, N.5
  • 55
    • 84861659828 scopus 로고    scopus 로고
    • Purification and characterization of maltooligosaccharide-forming α-amylase from moderately halophilic Marinobacter sp. EMB8
    • Kumar S, Khare S. 2012. Purification and characterization of maltooligosaccharide-forming α-amylase from moderately halophilic Marinobacter sp. EMB8. Bioresour Technol 116:247-251. http://dx.doi.org/10.1016/j.biortech.2011.11.109.
    • (2012) Bioresour Technol , vol.116 , pp. 247-251
    • Kumar, S.1    Khare, S.2
  • 56
    • 0021881219 scopus 로고
    • An unusual pattern of carbohydrate utilization in Corallococcus (Myxococcus) coralloides (Myxobacterales)
    • Irschik H, Reichenbach H. 1985. An unusual pattern of carbohydrate utilization in Corallococcus (Myxococcus) coralloides (Myxobacterales). Arch Microbiol 142:40-44. http://dx.doi.org/10.1007/BF00409234.
    • (1985) Arch Microbiol , vol.142 , pp. 40-44
    • Irschik, H.1    Reichenbach, H.2
  • 57
    • 0142164488 scopus 로고    scopus 로고
    • Myxobacteria: proficient producers of novel natural products with various biological activities-past and future biotechnological aspects with the focus on the genus Sorangium
    • Gerth K, Pradella S, Perlova O, Beyer S, Müller R. 2003. Myxobacteria: proficient producers of novel natural products with various biological activities-past and future biotechnological aspects with the focus on the genus Sorangium. J Biotechnol 106:233-253. http://dx.doi.org/10.1016/j.jbiotec.2003.07.015.
    • (2003) J Biotechnol , vol.106 , pp. 233-253
    • Gerth, K.1    Pradella, S.2    Perlova, O.3    Beyer, S.4    Müller, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.