메뉴 건너뛰기




Volumn 19, Issue 3, 2003, Pages 936-944

Purification and kinetics of a raw starch-hydrolyzing, thermostable, and neutral glucoamylase of the thermophilic mold Thermomucor indicae-seudaticae

Author keywords

[No Author keywords available]

Indexed keywords

RESPONSE SURFACE METHODOLOGY (RSM);

EID: 0038119653     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp034012a     Document Type: Article
Times cited : (62)

References (54)
  • 1
    • 0027071862 scopus 로고
    • cDNA clone and expression of a Talaromyces emersonii amylase encoding genetic determinant in E. coli
    • Bunni, L.; Coleman, D. C.; McHale, L.; Hackett, T. J.; McHale, A. P. cDNA clone and expression of a Talaromyces emersonii amylase encoding genetic determinant in E. coli. Biotechnol. Lett. 1992, 14, 1109-1114.
    • (1992) Biotechnol. Lett. , vol.14 , pp. 1109-1114
    • Bunni, L.1    Coleman, D.C.2    McHale, L.3    Hackett, T.J.4    McHale, A.P.5
  • 2
    • 85006938760 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of granular starch directly to glucose. European Patent Application 0171218, 1985
    • Jackson, L. E.; Seidman, M. Enzymatic hydrolysis of granular starch directly to glucose. European Patent Application 0171218, 1985.
    • Jackson, L.E.1    Seidman, M.2
  • 3
    • 0029010497 scopus 로고
    • Purification and characterization of a glucoamylase from Humicola grisea
    • Campos, L.; Felix, C. R. Purification and characterization of a glucoamylase from Humicola grisea. Appl. Environ. Microbiol. 1995, 2436-2438.
    • (1995) Appl. Environ. Microbiol. , pp. 2436-2438
    • Campos, L.1    Felix, C.R.2
  • 4
    • 0034647075 scopus 로고    scopus 로고
    • Evidence that the glucoamylase and α-amylase secreted by Aspergilus niger are proteolytically processed products of a precursor enzyme
    • Dubey, A. K.; Suresh, C.; Kavitha, R.; Karnath, S.; Kumar, U. Evidence that the glucoamylase and α-amylase secreted by Aspergilus niger are proteolytically processed products of a precursor enzyme. FEBS Lett. 2000, 471, 251-255.
    • (2000) FEBS Lett. , vol.471 , pp. 251-255
    • Dubey, A.K.1    Suresh, C.2    Kavitha, R.3    Karnath, S.4    Kumar, U.5
  • 5
    • 0028919386 scopus 로고
    • Characterization, subsite mapping and partial amino acid sequence of glucoamylase from the filamentous fungus Trichoderma reesei
    • Fagerstrom, R.; Kalkkinen. Characterization, subsite mapping and partial amino acid sequence of glucoamylase from the filamentous fungus Trichoderma reesei. Biotechnol. Appl. Biochem. 1995, 21, 223-231.
    • (1995) Biotechnol. Appl. Biochem. , vol.21 , pp. 223-231
    • Fagerstrom, R.1    Kalkkinen2
  • 6
    • 0001051874 scopus 로고
    • Amylases of the thermophilic fungus Thermomyces lanuginosus: Their purification, properties, action on starch and response to heat
    • Mishra, R.; Maheshwari, R. Amylases of the thermophilic fungus Thermomyces lanuginosus: their purification, properties, action on starch and response to heat. J. Biosci. 1995, 21(5), 653-672.
    • (1995) J. Biosci. , vol.21 , Issue.5 , pp. 653-672
    • Mishra, R.1    Maheshwari, R.2
  • 7
    • 0019482653 scopus 로고
    • Purification and characterization of a thermostable glucoamylase from thermophilic fungus Thermomyces lanuginosus
    • Rao, B. V.; Sastri, N. V. S. Rao Subba, P. V. Purification and characterization of a thermostable glucoamylase from thermophilic fungus Thermomyces lanuginosus. Biochem. J. 1981, 193, 379-387.
    • (1981) Biochem. J. , vol.193 , pp. 379-387
    • Rao, B.V.1    Sastri, N.V.S.2    Rao Subba, P.V.3
  • 8
    • 0027448702 scopus 로고
    • Purification and characterization of an extracellular glucoamylase from thermophilic fungus Humicola grisea var. thermoidea
    • Tosi, L. R. O.; Terenzi, H. F.; Jorge, J. A. Purification and characterization of an extracellular glucoamylase from thermophilic fungus Humicola grisea var. thermoidea. Can. J. Microbiol. 1993, 39, 846-852.
    • (1993) Can. J. Microbiol. , vol.39 , pp. 846-852
    • Tosi, L.R.O.1    Terenzi, H.F.2    Jorge, J.A.3
  • 9
    • 0001832594 scopus 로고
    • Microbial degradation of starch
    • Winkelmann, G. Ed.; VCH: Weinheim, Germany
    • Antranikian, G. Microbial degradation of starch. In Microbial Degradation of Natural Products; Winkelmann, G. Ed.; VCH: Weinheim, Germany, 1992; pp 27-51.
    • (1992) Microbial Degradation of Natural Products , pp. 27-51
    • Antranikian, G.1
  • 10
    • 0008592352 scopus 로고    scopus 로고
    • Amylases and their industrial potential
    • Johri, B. N., Satyanarayana, T., Olsen, J., Eds. Kluwer Academic Publishers: The Netherlands, 1999
    • Jensen, B.; Olsen, J. 1999. Amylases and their industrial potential. In Thermophilic Molds in Biotechnology; Johri, B. N., Satyanarayana, T., Olsen, J., Eds. Kluwer Academic Publishers: The Netherlands, 1999; pp 115-137.
    • (1999) Thermophilic Molds in Biotechnology , pp. 115-137
    • Jensen, B.1    Olsen, J.2
  • 12
    • 0000120116 scopus 로고    scopus 로고
    • Protein engineering of glucoamylase to improve industrial properties. A review
    • Reilly, P. J. Protein engineering of glucoamylase to improve industrial properties. A Review. Starch 1999, 51, 269-274.
    • (1999) Starch , vol.51 , pp. 269-274
    • Reilly, P.J.1
  • 13
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: Sources, uses and molecular mechanism for thermostability
    • Vieille, C.; Zeikus, G. J. Hyperthermophilic enzymes: sources, uses and molecular mechanism for thermostability. Microbiol. Mol. Biol. Rev. 2001, 65(1), 1-43.
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , Issue.1 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 14
    • 0002790580 scopus 로고    scopus 로고
    • Introduction to industrial enzymology
    • Godfrey, T., West, S. I., Eds.; Macmillan Press Ltd.: U.K.
    • Godfrey, T.; West, S. I. Introduction to industrial Enzymology. In Industrial Enzymology, 2nd ed., Godfrey, T., West, S. I., Eds.; Macmillan Press Ltd.: U.K., 1996; pp 1-8.
    • (1996) Industrial Enzymology, 2nd Ed. , pp. 1-8
    • Godfrey, T.1    West, S.I.2
  • 15
    • 33644518645 scopus 로고    scopus 로고
    • Industrial enzymes, an introduction
    • Walsh, G., Ed.; John Wiley & Sons Ltd.: New York
    • Walsh, G. Industrial enzymes, an Introduction. In Biochemistry and Biotechnology; Walsh, G., Ed.; John Wiley & Sons Ltd.: New York, 2002; pp 393-454.
    • (2002) Biochemistry and Biotechnology , pp. 393-454
    • Walsh, G.1
  • 16
    • 0037023912 scopus 로고    scopus 로고
    • Kinetic constant determination for an alkaline protease from Bacillus mojvensis using response surface methodology
    • Beg, Q. K.; Saxena, R. K.; Gupta, R. Kinetic constant determination for an alkaline protease from Bacillus mojvensis using response surface methodology. Biotechnol. Bioeng. 2002, 78(3), 289-295.
    • (2002) Biotechnol. Bioeng. , vol.78 , Issue.3 , pp. 289-295
    • Beg, Q.K.1    Saxena, R.K.2    Gupta, R.3
  • 17
    • 0036275211 scopus 로고    scopus 로고
    • Purification of lipase from Cunnighamella verticillata and optimization of enzyme activity using response surface methodology
    • Gopinath, S. C. B.; Hilda, A.; Lakshmipriya, T.; Annadurai, G. Purification of lipase from Cunnighamella verticillata and optimization of enzyme activity using response surface methodology. World J. Microbiol. Biotechnol. 2002, 18, 449-458.
    • (2002) World J. Microbiol. Biotechnol. , vol.18 , pp. 449-458
    • Gopinath, S.C.B.1    Hilda, A.2    Lakshmipriya, T.3    Annadurai, G.4
  • 18
    • 0035139574 scopus 로고    scopus 로고
    • Purification and some properties of a novel raw starch-digesting amylase from Aspergillus carbonarius
    • Okolo, B. N.; Francis, S. I.; Ezeogu, L. I.; Anyanwu, C. U.; Odibo, J. C. Purification and some properties of a novel raw starch-digesting amylase from Aspergillus carbonarius. J. Sci. Food Agric. 2000, 81, 329-336.
    • (2000) J. Sci. Food Agric. , vol.81 , pp. 329-336
    • Okolo, B.N.1    Francis, S.I.2    Ezeogu, L.I.3    Anyanwu, C.U.4    Odibo, J.C.5
  • 20
    • 0001796193 scopus 로고
    • An experimental study of life cycle and taxonomies of Allomyces
    • Emerson, R. An experimental study of life cycle and taxonomies of Allomyces. Lloydia 1941, 4, 77-144.
    • (1941) Lloydia , vol.4 , pp. 77-144
    • Emerson, R.1
  • 21
    • 0037580099 scopus 로고    scopus 로고
    • Partial purification and characterization of glucoamylase of thermophilic mold Thermomucor indicae-seudaticae
    • Kaur, P.; Satyanarayana, T. Partial purification and characterization of glucoamylase of thermophilic mold Thermomucor indicae-seudaticae. Indian J. Microbiol. 2001, 41, 195-199.
    • (2001) Indian J. Microbiol. , vol.41 , pp. 195-199
    • Kaur, P.1    Satyanarayana, T.2
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 277, 680-685.
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0031838675 scopus 로고    scopus 로고
    • Use of Box-Behnken design experiments for the adsorption of verofix red using biopolymer
    • Annadurai, G.; Sheeja, R. Y. Use of Box-Behnken design experiments for the adsorption of verofix red using biopolymer. Bioprocess Eng. 1998, 18, 463-466.
    • (1998) Bioprocess Eng. , vol.18 , pp. 463-466
    • Annadurai, G.1    Sheeja, R.Y.2
  • 25
    • 62249137520 scopus 로고
    • The estimation of carbohydrates in plant extracts by anthrone
    • Yemm, E. W.; Willis, A. J. The estimation of carbohydrates in plant extracts by anthrone. Biochem. J. 1954, 57, 508-514.
    • (1954) Biochem. J. , vol.57 , pp. 508-514
    • Yemm, E.W.1    Willis, A.J.2
  • 26
    • 33748037939 scopus 로고
    • Amylases, α and β
    • Bernfield, P. Amylases, α and β. Methods Enzymol. 1955, 1, 149-158.
    • (1955) Methods Enzymol. , vol.1 , pp. 149-158
    • Bernfield, P.1
  • 27
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • Dubois, M.; Gilles, K. A.; Hamilton, J. K.; Rebers, P. A.; Smith, F. Colorimetric method for determination of sugars and related substances. Anal. Chem. 1956, 28, 350-356.
    • (1956) Anal. Chem. , vol.28 , pp. 350-356
    • Dubois, M.1    Gilles, K.A.2    Hamilton, J.K.3    Rebers, P.A.4    Smith, F.5
  • 28
    • 0345912536 scopus 로고    scopus 로고
    • Purification and characterization of a thermostable glucoamylase from Aspergillus fumigatus
    • DaSilva, W. B.; Peralta, R. M. Purification and characterization of a thermostable glucoamylase from Aspergillus fumigatus. Can. J. Microbiol. 1998, 44, 493-497.
    • (1998) Can. J. Microbiol. , vol.44 , pp. 493-497
    • DaSilva, W.B.1    Peralta, R.M.2
  • 29
    • 0031670504 scopus 로고    scopus 로고
    • Purification and properties of the raw starch digesting glucoamylases from Corticium rolfsii
    • Nagasaka, Y.; Kurosawa, K.; Yokota, A.; Tomita, F. Purification and properties of the raw starch digesting glucoamylases from Corticium rolfsii. Appl. Microbiol. Biotechnol. 1998, 50, 323-330.
    • (1998) Appl. Microbiol. Biotechnol. , vol.50 , pp. 323-330
    • Nagasaka, Y.1    Kurosawa, K.2    Yokota, A.3    Tomita, F.4
  • 30
    • 12444332322 scopus 로고
    • Production of xylanolytic enzymes by Aspergillus fumigatus
    • Flannigan, B.; Sellars, P. N. Production of xylanolytic enzymes by Aspergillus fumigatus. Trans Brit. Mycol. Soc. 1978, 71, 353-358.
    • (1978) Trans Brit. Mycol. Soc. , vol.71 , pp. 353-358
    • Flannigan, B.1    Sellars, P.N.2
  • 32
    • 0021706633 scopus 로고
    • Isolation and characterization of glucoamylase from Saccharomyces diastaticus
    • Tucker, M.; Grohman, K.; Himmel, M. Isolation and characterization of glucoamylase from Saccharomyces diastaticus. Biotechnol. Bioeng. Symp. 1984, 14, 279.
    • (1984) Biotechnol. Bioeng. Symp. , vol.14 , pp. 279
    • Tucker, M.1    Grohman, K.2    Himmel, M.3
  • 33
    • 0040685650 scopus 로고
    • Glucoamylase: Microbial sources, industrial applications and molecular biology-A review
    • James, J. A.; Lee, B. H. Glucoamylase: Microbial sources, industrial applications and molecular biology-A review. J. Food Biochem. 1987, 21, 1-52.
    • (1987) J. Food Biochem. , vol.21 , pp. 1-52
    • James, J.A.1    Lee, B.H.2
  • 34
    • 0025916813 scopus 로고
    • Purification and properties of thermoactive glucoamylase from Clostridium thermosaccharolyticum
    • Specka, U.; Mayer, F.; Antranikian, G. Purification and properties of thermoactive glucoamylase from Clostridium thermosaccharolyticum. Appl. Environ. Microbiol. 1991, 57(8), 2317-2323.
    • (1991) Appl. Environ. Microbiol. , vol.57 , Issue.8 , pp. 2317-2323
    • Specka, U.1    Mayer, F.2    Antranikian, G.3
  • 35
    • 0029450515 scopus 로고
    • Studies on glucoamylase produced from Aspergillus awamori (NRRL-3112) and their effect on saccharification of potato starch
    • Soni, S. K.; Rao, M. V.; Das, D. Studies on glucoamylase produced from Aspergillus awamori (NRRL-3112) and their effect on saccharification of potato starch. Indian J. Exp. Biol. 1995, 33, 957-961.
    • (1995) Indian J. Exp. Biol. , vol.33 , pp. 957-961
    • Soni, S.K.1    Rao, M.V.2    Das, D.3
  • 36
    • 0036228026 scopus 로고    scopus 로고
    • Purification and characterization of a glucoamylase secreted by the plant pathogen Sclerotinia sclerotiorum
    • Martel, M. B.; Penhoat, C. H. D.; Letoublon, R.; Fever, M. Purification and characterization of a glucoamylase secreted by the plant pathogen Sclerotinia sclerotiorum. Can. J. Microbiol. 2002, 48, 212-218.
    • (2002) Can. J. Microbiol. , vol.48 , pp. 212-218
    • Martel, M.B.1    Penhoat, C.H.D.2    Letoublon, R.3    Fever, M.4
  • 37
    • 0030472492 scopus 로고    scopus 로고
    • Purification and characterization of glucoamylase produced by Aspergilus niger in solid-state fermentation
    • Selvakumar, P.; Ashakumari, L.; Helen, A.; Pandey, A. Purification and characterization of glucoamylase produced by Aspergilus niger in solid-state fermentation. Lett. App. Microbiol. 1996, 23, 403-406.
    • (1996) Lett. App. Microbiol. , vol.23 , pp. 403-406
    • Selvakumar, P.1    Ashakumari, L.2    Helen, A.3    Pandey, A.4
  • 38
    • 0025035931 scopus 로고
    • Thermostable amylolytic enzymes from a cellulolytic fungus Myceliophthora thermophila D14 (ATCC 48104)
    • Sadhukhan, R. K.; Manna, S.; Roy, S. K.; Chakraborty, S. L. Thermostable amylolytic enzymes from a cellulolytic fungus Myceliophthora thermophila D14 (ATCC 48104). App. Microbiol. Biotechnol. 1990, 33, 692-696.
    • (1990) App. Microbiol. Biotechnol. , vol.33 , pp. 692-696
    • Sadhukhan, R.K.1    Manna, S.2    Roy, S.K.3    Chakraborty, S.L.4
  • 39
    • 85004685302 scopus 로고
    • Formation of active derivatives of glucoamylaseI during the digestion with fungal acidic protease and α-mannosidase
    • Hyashida, S.; Yoshino, E. Formation of active derivatives of glucoamylaseI during the digestion with fungal acidic protease and α-mannosidase. Agric. Biol. Chem. 1978, 42, 927.
    • (1978) Agric. Biol. Chem. , vol.42 , pp. 927
    • Hyashida, S.1    Yoshino, E.2
  • 40
    • 0021073149 scopus 로고
    • Purification and properties of a thermophilic amyloglucosidase from Aspergillus niger
    • Fogarty, W. M. Benson, C. P. Purification and properties of a thermophilic amyloglucosidase from Aspergillus niger. Appl. Microbiol. Biotechnol. 1983, 18, 271-278.
    • (1983) Appl. Microbiol. Biotechnol. , vol.18 , pp. 271-278
    • Fogarty, W.M.1    Benson, C.P.2
  • 41
    • 14744285620 scopus 로고
    • Extraordinary stability of enzyme dried in trehalose: Simplified molecular biology
    • Colaco, C.; Sen, S.; Thangavelu, M.; Pinder, S.; Roser, B. Extraordinary stability of enzyme dried in trehalose: simplified molecular biology. Biotechnology 1992, 10(9), 1007-1011.
    • (1992) Biotechnology , vol.10 , Issue.9 , pp. 1007-1011
    • Colaco, C.1    Sen, S.2    Thangavelu, M.3    Pinder, S.4    Roser, B.5
  • 42
    • 0031715787 scopus 로고    scopus 로고
    • Stabilizing crude and ultrafiltrated α-amylase and α-glucosidase from Aspergillus oryzae by trehalose
    • Terebiznik, M. R.; Zylberman, V.; Buera, M. P.; Pilosof, A. M. R. Stabilizing crude and ultrafiltrated α-amylase and α-glucosidase from Aspergillus oryzae by trehalose. Biotechnol. Tech. 1998, 12(9), 683-687.
    • (1998) Biotechnol. Tech. , vol.12 , Issue.9 , pp. 683-687
    • Terebiznik, M.R.1    Zylberman, V.2    Buera, M.P.3    Pilosof, A.M.R.4
  • 43
    • 0016585033 scopus 로고
    • Studies on the inhibition and molecular properties of crystalline Pseudomonas amylodermosa isoamylase
    • Kitagawa, H.; Imamura, A.; Harada, T. Studies on the inhibition and molecular properties of crystalline Pseudomonas amylodermosa isoamylase. Agric. Biol. Chem. 1975, 39, 989-1975.
    • (1975) Agric. Biol. Chem. , vol.39 , pp. 989-1975
    • Kitagawa, H.1    Imamura, A.2    Harada, T.3
  • 44
    • 0037580100 scopus 로고
    • Effects of additives on the thermostability of Bacillus stearothermophilus α-amylase
    • Brumn, P. J.; Teague, W. M. Effects of additives on the thermostability of Bacillus stearothermophilus α-amylase. Biotechnol. Lett. 1989, 11, 541-544.
    • (1989) Biotechnol. Lett. , vol.11 , pp. 541-544
    • Brumn, P.J.1    Teague, W.M.2
  • 45
    • 0023505188 scopus 로고
    • Thermal stability of proteins in the presence of poly(ethylene glycol)
    • Lee, L. L. Y.; Lee, J. C. Thermal stability of proteins in the presence of poly(ethylene glycol). Biochemistry 1987, 26, 7813-7819.
    • (1987) Biochemistry , vol.26 , pp. 7813-7819
    • Lee, L.L.Y.1    Lee, J.C.2
  • 46
    • 0002676861 scopus 로고
    • Purification of membrane proteins
    • Harria, E. L. V., Angal, S., Eds.; IRL Press, Oxford Univerity Press: Oxford
    • Findlay, J. B. C. Purification of membrane proteins. In Protein Purification Application A Practical Approach; Harria, E. L. V., Angal, S., Eds.; IRL Press, Oxford Univerity Press: Oxford, 1990; pp. 59-82.
    • (1990) Protein Purification Application A Practical Approach , pp. 59-82
    • Findlay, J.B.C.1
  • 47
    • 0001477783 scopus 로고
    • The role of tryptophanyl residue in the function of Aspergillus niger glucoamylase G1 and G2
    • Clarke, A. J.; Svensson, B. The role of tryptophanyl residue in the function of Aspergillus niger glucoamylase G1 and G2. Carlsberg Res. Commun. 1984, 49, 111-122.
    • (1984) Carlsberg Res. Commun. , vol.49 , pp. 111-122
    • Clarke, A.J.1    Svensson, B.2
  • 48
    • 0020687024 scopus 로고
    • Subsite structure and ligand mechanism of glucoamylase
    • Hiromi, K.; Ohnishi, M.; Tanaka, A. Subsite structure and ligand mechanism of glucoamylase. Mol. Cell. Biochem. 1983, 51, 79-95.
    • (1983) Mol. Cell. Biochem. , vol.51 , pp. 79-95
    • Hiromi, K.1    Ohnishi, M.2    Tanaka, A.3
  • 49
    • 0031574082 scopus 로고    scopus 로고
    • Some details of the reaction mechanism of glucoamylase from Aspergillus niger; kinetic and structural studies on Trp52 → Phe and Trp317 → Phe mutants
    • Christensen, T.; Stoffer, B.; Svensson, B.; Christensen, U. Some details of the reaction mechanism of glucoamylase from Aspergillus niger; kinetic and structural studies on Trp52 → Phe and Trp317 → Phe mutants. Eur. J. Biochem. 1997, 250, 638-645.
    • (1997) Eur. J. Biochem. , vol.250 , pp. 638-645
    • Christensen, T.1    Stoffer, B.2    Svensson, B.3    Christensen, U.4
  • 50
    • 0027429148 scopus 로고
    • Reaction mechanism of Trp120 → Phe and wild-type glucoamylase from Aspergillus niger: Intercations with maltooligodextrins and acarbose
    • Olsen, K.; Christensen, U.; Sierks, M. R.; Svensson, B. Reaction mechanism of Trp120 → Phe and wild-type glucoamylase from Aspergillus niger: Intercations with maltooligodextrins and acarbose. Biochemistry 1993, 32, 9686-9693.
    • (1993) Biochemistry , vol.32 , pp. 9686-9693
    • Olsen, K.1    Christensen, U.2    Sierks, M.R.3    Svensson, B.4
  • 51
    • 0024972502 scopus 로고
    • Substantial increase of protein stability by multiple disulphide bonds
    • Matsumura, M.; Signor, G.; Mathew, B. W. Substantial increase of protein stability by multiple disulphide bonds. Nature 1989, 342, 291-293.
    • (1989) Nature , vol.342 , pp. 291-293
    • Matsumura, M.1    Signor, G.2    Mathew, B.W.3
  • 52
    • 0033534477 scopus 로고    scopus 로고
    • Extremely thermostable serine type protease from Aquifex pyrophilus: Molecular cloning, expression and characterization
    • Choi, I. G.; Bang, W. G.; Kim, S. H. Yu, Y. G. Extremely thermostable serine type protease from Aquifex pyrophilus: molecular cloning, expression and characterization. J. Biol. Chem. 1999, 274, 881-888.
    • (1999) J. Biol. Chem. , vol.274 , pp. 881-888
    • Choi, I.G.1    Bang, W.G.2    Kim, S.H.3    Yu, Y.G.4
  • 54
    • 0033152019 scopus 로고
    • Heterologous expression of 5′-methylthioadenosine phosphorylase from the archaeon Sulfolobus sulfatricus: Characterization of recombinant protein and involvement of disulphide bond in thermophilicity and thermostability
    • Caccipuoti, G.; Poracelli, M.; Bertaoldo, C.; DeRose, M.; Zappia, V. Heterologous expression of 5′-methylthioadenosine phosphorylase from the archaeon Sulfolobus sulfatricus: characterization of recombinant protein and involvement of disulphide bond in thermophilicity and thermostability. Protein Expression Purif. 1994, 16, 125-135.
    • (1994) Protein Expression Purif. , vol.16 , pp. 125-135
    • Caccipuoti, G.1    Poracelli, M.2    Bertaoldo, C.3    DeRose, M.4    Zappia, V.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.