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Volumn 78, Issue 15, 2012, Pages 5182-5188

Gene cloning, purification, and characterization of a novel peptidoglutaminase-asparaginase from Aspergillus sojae

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINYL; ASPERGILLUS ORYZAE; CELL SURFACES; DEAMIDATED; EXPRESSED SEQUENCE TAGS; FERMENTED FOODS; GEL-FILTRATION CHROMATOGRAPHY; GENE CLONING; GENOME SEQUENCES; GLUTAMINASE; GLUTAMINYL; L-GLUTAMATE; L-GLUTAMINE; NATIVE FORMS; OPTIMAL TEMPERATURE; OVER-EXPRESSION; SALT TOLERANT; SDS-PAGE; SODIUM PHOSPHATE BUFFER; STRUCTURAL GENE; SUBMERGED CULTURES; SUBSTRATE SPECIFICITY; UMAMI TASTE;

EID: 84866171039     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.00765-12     Document Type: Article
Times cited : (24)

References (34)
  • 1
    • 34548460363 scopus 로고    scopus 로고
    • Analysis of expressed sequence tags from the fungus Aspergillus oryzae cultured under different conditions
    • Akao T, et al. 2007. Analysis of expressed sequence tags from the fungus Aspergillus oryzae cultured under different conditions. DNA Res. 14:47-57.
    • (2007) DNA Res. , vol.14 , pp. 47-57
    • Akao, T.1
  • 2
    • 0037024085 scopus 로고    scopus 로고
    • Purification and characterization of a glutaminase from Debaryomyces spp. Int.
    • Durá AM, Flores M, Toldrá F. 2002. Purification and characterization of a glutaminase from Debaryomyces spp. Int. J. Food Microbiol. 76:117-126.
    • (2002) J. Food Microbiol. , vol.76 , pp. 117-126
    • Durá, A.M.1    Flores, M.2    Toldrá, F.3
  • 4
    • 64749116346 scopus 로고    scopus 로고
    • c-Myc suppression of miR-23a/b enhances mitochondrial glutaminase expression and glutamine metabolism
    • Gao P, et al. 2009. c-Myc suppression of miR-23a/b enhances mitochondrial glutaminase expression and glutamine metabolism. Nature 458:762-765.
    • (2009) Nature , vol.458 , pp. 762-765
    • Gao, P.1
  • 5
    • 0028250433 scopus 로고
    • Deamidation of food proteins to improve functionality
    • Hamada JS. 1994. Deamidation of food proteins to improve functionality. Crit. Rev. Food Sci. Nutr. 34:283-292.
    • (1994) Crit. Rev. Food Sci. Nutr. , vol.34 , pp. 283-292
    • Hamada, J.S.1
  • 6
    • 84985294310 scopus 로고
    • Enhancement of peptidoglutaminase deamidation of soy protein by heat treatment and/or proteolysis
    • Hamada JS, Mashall WE. 1988. Enhancement of peptidoglutaminase deamidation of soy protein by heat treatment and/or proteolysis. J. Food Sci. 53:1132-1134.
    • (1988) J. Food Sci. , vol.53 , pp. 1132-1134
    • Hamada, J.S.1    Mashall, W.E.2
  • 7
    • 0023095943 scopus 로고
    • Purification and characterization of rat liver glutaminase
    • Heini HG, Gebhardt R, Brecht A, Mecke D. 1987. Purification and characterization of rat liver glutaminase. Eur. J. Biochem. 162:541-546.
    • (1987) Eur. J. Biochem. , vol.162 , pp. 541-546
    • Heini, H.G.1    Gebhardt, R.2    Brecht, A.3    Mecke, D.4
  • 8
  • 9
    • 79960761825 scopus 로고    scopus 로고
    • Salt-tolerant and thermostable glutaminase of Cryptococcus species form a new glutaminase family
    • Ito K, Umitsuki G, Oguma T, Koyama Y. 2011. Salt-tolerant and thermostable glutaminase of Cryptococcus species form a new glutaminase family. Biosci. Biotechnol. Biochem. 75:1317-1324.
    • (2011) Biosci. Biotechnol. Biochem. , vol.75 , pp. 1317-1324
    • Ito, K.1    Umitsuki, G.2    Oguma, T.3    Koyama, Y.4
  • 10
    • 0001511576 scopus 로고
    • On the glutaminase produced by Cryptococcus albidus ATCC 20293
    • Iwasa T, Fujii S, Yokotsuka T. 1987. On the glutaminase produced by Cryptococcus albidus ATCC 20293. J. Jpn. Soy Sauce Res. Inst. 13:205-210.
    • (1987) J. Jpn. Soy Sauce Res. Inst. , vol.13 , pp. 205-210
    • Iwasa, T.1    Fujii, S.2    Yokotsuka, T.3
  • 11
    • 0015245042 scopus 로고
    • Enzyme for selective deamidation of Γ-amide of peptide-bond glutamine
    • Peptidoglutaminase
    • Kikuchi M, Hayashi H, Nakano E, Sakaguchi K. 1971. Peptidoglutaminase. Enzyme for selective deamidation of Γ-amide of peptide-bond glutamine. Biochemistry 10:1222-1229.
    • (1971) Biochemistry , vol.10 , pp. 1222-1229
    • Kikuchi, M.1    Hayashi, H.2    Nakano, E.3    Sakaguchi, K.4
  • 12
    • 0015842414 scopus 로고
    • Some enzymatic properties and substrate specidicities of peptidoglutaminase-I and II
    • Kikuchi M, Sakaguchi K. 1973. Some enzymatic properties and substrate specidicities of peptidoglutaminase-I and II. Agr. Biol. Chem. 37:1813-1821.
    • (1973) Agr. Biol. Chem. , vol.37 , pp. 1813-1821
    • Kikuchi, M.1    Sakaguchi, K.2
  • 15
    • 0041518552 scopus 로고
    • Biosynthesis and degradation of glutamic acid in microorganisms relating to the soy sauce brewing
    • Kurose E, Oyama Y, Matuo T, Sugimori T. 1969. Biosynthesis and degradation of glutamic acid in microorganisms relating to the soy sauce brewing. J. Ferment. Technol. 47:693-700.
    • (1969) J. Ferment. Technol. , vol.47 , pp. 693-700
    • Kurose, E.1    Oyama, Y.2    Matuo, T.3    Sugimori, T.4
  • 16
    • 29244442741 scopus 로고    scopus 로고
    • Genome sequencing and analysis of Aspergillus oryzae
    • Machida M, et al. 2005. Genome sequencing and analysis of Aspergillus oryzae. Nature 438:1157-1161.
    • (2005) Nature , vol.438 , pp. 1157-1161
    • Machida, M.1
  • 17
    • 8844254802 scopus 로고    scopus 로고
    • Molecular cloning, overexpression, and purification of Micrococcus luteus K-3-type glutaminase from Aspergillus oryzae RIB40
    • Masuo N, et al. 2004. Molecular cloning, overexpression, and purification of Micrococcus luteus K-3-type glutaminase from Aspergillus oryzae RIB40. Protein Expr. Purif. 38:272-278.
    • (2004) Protein Expr. Purif. , vol.38 , pp. 272-278
    • Masuo, N.1
  • 18
    • 0035010841 scopus 로고    scopus 로고
    • Pre-termination in aflR of Aspergillus sojae inhibits aflatoxin biosynthesis
    • Matsushima K, et al. 2001. Pre-termination in aflR of Aspergillus sojae inhibits aflatoxin biosynthesis. Appl. Microbiol. Biotechnol. 55:585-589.
    • (2001) Appl. Microbiol. Biotechnol. , vol.55 , pp. 585-589
    • Matsushima, K.1
  • 19
    • 0036253171 scopus 로고    scopus 로고
    • Gene cloning, overexpression and biochemical characterization of the peptide amidase from Stenotrophomonas maltophilia
    • Neumann S, Kula MR. 2002. Gene cloning, overexpression and biochemical characterization of the peptide amidase from Stenotrophomonas maltophilia. Appl. Microbiol. Biotechnol. 58:772-780.
    • (2002) Appl. Microbiol. Biotechnol. , vol.58 , pp. 772-780
    • Neumann, S.1    Kula, M.R.2
  • 20
    • 0016161117 scopus 로고
    • Isolation and characterization of acidic peptide in soy sauce
    • Oka S, Nagata K. 1973. Isolation and characterization of acidic peptide in soy sauce. Agr. Biol. Chem. 38:1195-1202.
    • (1973) Agr. Biol. Chem. , vol.38 , pp. 1195-1202
    • Oka, S.1    Nagata, K.2
  • 22
    • 0026936942 scopus 로고
    • Overproduction of an alpha-amylase/glucoamylase fusion protein in Aspergillus oryzae using a high expression vector
    • Shibuya I, Tsuchiya K, Tamura G, Ishikawa T, Hara S. 1992. Overproduction of an alpha-amylase/glucoamylase fusion protein in Aspergillus oryzae using a high expression vector. Biosci. Biotech. Biochem. 56:1674-1675.
    • (1992) Biosci. Biotech. Biochem. , vol.56 , pp. 1674-1675
    • Shibuya, I.1    Tsuchiya, K.2    Tamura, G.3    Ishikawa, T.4    Hara, S.5
  • 24
    • 0017062893 scopus 로고
    • Bacterial glutaminase in treatment of acute leukaemia
    • Spiers AS, Wade HE. 1976. Bacterial glutaminase in treatment of acute leukaemia. Br. Med. J. 1:1317-1319.
    • (1976) Br. Med. J. , vol.1 , pp. 1317-1319
    • Spiers, A.S.1    Wade, H.E.2
  • 25
    • 0029616106 scopus 로고
    • Purification and characterization of a newly screened microbial peptide amidase
    • Stelkes-Ritter U, Wyzgol K, Kula MR. 1995. Purification and characterization of a newly screened microbial peptide amidase. Appl. Microbiol. Biotechnol. 44:393-398.
    • (1995) Appl. Microbiol. Biotechnol. , vol.44 , pp. 393-398
    • Stelkes-Ritter, U.1    Wyzgol, K.2    Kula, M.R.3
  • 26
    • 80455173785 scopus 로고    scopus 로고
    • Optimization of the enzymatic deamidation of soy protein by protein-glutaminase and its effect on the functional properties of the protein
    • Suppavorasatit I, De Mejia EG, Cadwallader KR. 2011. Optimization of the enzymatic deamidation of soy protein by protein-glutaminase and its effect on the functional properties of the protein. J. Agric. Food Chem. 59:11621-11628.
    • (2011) J. Agric. Food Chem. , vol.59 , pp. 11621-11628
    • Suppavorasatit, I.1    De Mejia, E.G.2    Cadwallader, K.R.3
  • 27
    • 33646596933 scopus 로고    scopus 로고
    • Enhanced gene targeting frequency in ku70 and ku80 disruption mutants of Aspergillus sojae and Aspergillus oryzae
    • Takahashi T, Masuda T, Koyama Y. 2006. Enhanced gene targeting frequency in ku70 and ku80 disruption mutants of Aspergillus sojae and Aspergillus oryzae. Mol. Genet. Genomics 275:460-470.
    • (2006) Mol. Genet. Genomics , vol.275 , pp. 460-470
    • Takahashi, T.1    Masuda, T.2    Koyama, Y.3
  • 28
    • 8644233254 scopus 로고    scopus 로고
    • Efficient gene disruption in the koji-mold Aspergillus sojae using a novel variation of the positive-negative method
    • Takahashi T, Hatamoto T, Koyama Y, Abe K. 2004. Efficient gene disruption in the koji-mold Aspergillus sojae using a novel variation of the positive-negative method. Mol. Genet. Genomics 272:344-352.
    • (2004) Mol. Genet. Genomics , vol.272 , pp. 344-352
    • Takahashi, T.1    Hatamoto, T.2    Koyama, Y.3    Abe, K.4
  • 30
    • 77956497712 scopus 로고    scopus 로고
    • Targeting mitochondrial glutaminase activity inhibits oncogenic transformation
    • Wang JB, et al. 2010. Targeting mitochondrial glutaminase activity inhibits oncogenic transformation. Cancer Cell 18:207-219.
    • (2010) Cancer Cell , vol.18 , pp. 207-219
    • Wang, J.B.1
  • 31
    • 0000669328 scopus 로고
    • Production of glutaminase by Aspergillus sojae
    • Yamamoto S, Hirooka H. 1974. Production of glutaminase by Aspergillus sojae. J. Ferment. Technol. 52:564-569.
    • (1974) J. Ferment. Technol. , vol.52 , pp. 564-569
    • Yamamoto, S.1    Hirooka, H.2
  • 32
    • 0035079176 scopus 로고    scopus 로고
    • Protein-glutaminase from Chryseobacterium proteolyticum, an enzyme that deamidates glutaminyl residues in proteins
    • Purification, characterization and gene cloning
    • Yamaguchi S, Jeenes DJ, Archer DB. 2001. Protein-glutaminase from Chryseobacterium proteolyticum, an enzyme that deamidates glutaminyl residues in proteins. Purification, characterization and gene cloning. Eur. J. Biochem. 268:1410-1421.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1410-1421
    • Yamaguchi, S.1    Jeenes, D.J.2    Archer, D.B.3
  • 34
    • 33748437518 scopus 로고    scopus 로고
    • Effects of enzymatic deamidation by protein-glutaminase on structure and functional properties of wheat gluten
    • Yong YH, Yamaguchi S, Matsumura Y. 2006. Effects of enzymatic deamidation by protein-glutaminase on structure and functional properties of wheat gluten. J. Agric. Food Chem. 54:6034-6040.
    • (2006) J. Agric. Food Chem. , vol.54 , pp. 6034-6040
    • Yong, Y.H.1    Yamaguchi, S.2    Matsumura, Y.3


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