메뉴 건너뛰기




Volumn 104, Issue 5, 2007, Pages 353-362

Some Distinguishable Properties between Acid-Stable and Neutral Types of α-Amylases from Acid-Producing Koji

Author keywords

acid stable amylase; Aspergillus kawachii; Aspergillus usamii; citric acid; kojimold; shochu

Indexed keywords

ASPERGILLUS KAWACHII; ASPERGILLUS USAMII; SHOCHU; SOUTHERN KYUSHU;

EID: 37049019042     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1263/jbb.104.353     Document Type: Article
Times cited : (54)

References (57)
  • 1
    • 37049022158 scopus 로고
    • Study on industrial production of citric acid
    • (in Japanese)
    • Kawahara H. Study on industrial production of citric acid. Kagoshima-ken Kogyo-shikenjou Gyomu-hokokusho 1953 (1953) 23-24 (in Japanese)
    • (1953) Kagoshima-ken Kogyo-shikenjou Gyomu-hokokusho , vol.1953 , pp. 23-24
    • Kawahara, H.1
  • 3
    • 37048999735 scopus 로고    scopus 로고
    • Do not produce enzymes involved in aflatoxin biosynthesis
    • (in Japanese)
    • Matushima K. Do not produce enzymes involved in aflatoxin biosynthesis. J. Brew. Soc. Jpn. 97 (2002) 559-566 (in Japanese)
    • (2002) J. Brew. Soc. Jpn. , vol.97 , pp. 559-566
    • Matushima, K.1
  • 4
    • 2142803387 scopus 로고
    • Activity of α-glucosidase in sake koji and its role during sake brewing
    • Morimoto Y., Kitamoto K., Fujita Y., Gomi K., and Kumagai C. Activity of α-glucosidase in sake koji and its role during sake brewing. Seibutsu-kogaku 73 (1995) 97-104
    • (1995) Seibutsu-kogaku , vol.73 , pp. 97-104
    • Morimoto, Y.1    Kitamoto, K.2    Fujita, Y.3    Gomi, K.4    Kumagai, C.5
  • 5
    • 0037272612 scopus 로고    scopus 로고
    • Purification and characterization of rice α-glucosidase, a key enzyme for alcohol fermentation of rice polish
    • Iwata H., Suzuki T., and Aramaki I. Purification and characterization of rice α-glucosidase, a key enzyme for alcohol fermentation of rice polish. J. Ferment. Bioeng. 95 (2003) 106-108
    • (2003) J. Ferment. Bioeng. , vol.95 , pp. 106-108
    • Iwata, H.1    Suzuki, T.2    Aramaki, I.3
  • 7
    • 0142060309 scopus 로고
    • Isolation of crystalline Taka-amylase A from "Takadiastase sankyo"
    • Akabori S., Ikenaka T., and Hagihara B. Isolation of crystalline Taka-amylase A from "Takadiastase sankyo". J. Biochem. 41 (1954) 577-582
    • (1954) J. Biochem. , vol.41 , pp. 577-582
    • Akabori, S.1    Ikenaka, T.2    Hagihara, B.3
  • 8
    • 0015025635 scopus 로고
    • Influence of molecular structures of substrates and analogues on Taka-amylase A catalyzed hydrolyses. I. Effect of chain length of linear substrates
    • Nitta Y., Mizushima M., Hiromi K., and Ono S. Influence of molecular structures of substrates and analogues on Taka-amylase A catalyzed hydrolyses. I. Effect of chain length of linear substrates. J. Biochem. (Tokyo) 69 (1971) 567-576
    • (1971) J. Biochem. (Tokyo) , vol.69 , pp. 567-576
    • Nitta, Y.1    Mizushima, M.2    Hiromi, K.3    Ono, S.4
  • 9
    • 0018175456 scopus 로고
    • A study of the mechanism of action of Taka-amylase A on linear oligosaccharides by product analysis and computer simulation
    • Suganuma T., Matsuno R., Ohnishi M., and Hiromi K. A study of the mechanism of action of Taka-amylase A on linear oligosaccharides by product analysis and computer simulation. J. Biochem. (Tokyo) 84 (1978) 293-316
    • (1978) J. Biochem. (Tokyo) , vol.84 , pp. 293-316
    • Suganuma, T.1    Matsuno, R.2    Ohnishi, M.3    Hiromi, K.4
  • 10
    • 84989131370 scopus 로고
    • The Complete amino acid sequence of Taka-amylase A
    • Toda H., Kondo K., and Narita K. The Complete amino acid sequence of Taka-amylase A. Proc. Jpn. Acad. 58B (1982) 208-212
    • (1982) Proc. Jpn. Acad. , vol.58 B , pp. 208-212
    • Toda, H.1    Kondo, K.2    Narita, K.3
  • 11
  • 12
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrrisat B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280 (1991) 309-316
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrrisat, B.1
  • 13
    • 0032976301 scopus 로고    scopus 로고
    • The concept of the α-amylase family: structural similarity and common catalytic mechanism
    • Kuriki T., and Imanaka T. The concept of the α-amylase family: structural similarity and common catalytic mechanism. J. Biosci. Bioeng. 87 (1999) 557-565
    • (1999) J. Biosci. Bioeng. , vol.87 , pp. 557-565
    • Kuriki, T.1    Imanaka, T.2
  • 14
    • 0024809051 scopus 로고
    • Isolation of a cDNA encoding Aspergillus oryzae Taka-amylase A: evidence for multiple related genes
    • Tsukagoshi N., Furukawa M., Nagaba H., Kirita N., Tsuboi A., and Udaka S. Isolation of a cDNA encoding Aspergillus oryzae Taka-amylase A: evidence for multiple related genes. Gene 84 (1989) 319-327
    • (1989) Gene , vol.84 , pp. 319-327
    • Tsukagoshi, N.1    Furukawa, M.2    Nagaba, H.3    Kirita, N.4    Tsuboi, A.5    Udaka, S.6
  • 15
    • 0343091497 scopus 로고
    • Cloning and nucleotide sequence of the genomic Taka-amylase A gene of Aspergillus oryzae
    • Tada S., Iimura Y., Gomi K., Takahashi K., Hara S., and Yoshizawa K. Cloning and nucleotide sequence of the genomic Taka-amylase A gene of Aspergillus oryzae. Agric. Biol. Chem. 53 (1989) 593-599
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 593-599
    • Tada, S.1    Iimura, Y.2    Gomi, K.3    Takahashi, K.4    Hara, S.5    Yoshizawa, K.6
  • 16
    • 0024315839 scopus 로고
    • Aspergillus oryzae has two nearly identical Taka-amylase genes, each containing eight introns
    • Gines M.J., Dove M.J., and Seligy V.L. Aspergillus oryzae has two nearly identical Taka-amylase genes, each containing eight introns. Gene 79 (1989) 107-117
    • (1989) Gene , vol.79 , pp. 107-117
    • Gines, M.J.1    Dove, M.J.2    Seligy, V.L.3
  • 17
    • 0024489684 scopus 로고
    • Three α-amylase genes of Aspergillus oryzae exhibit identical intron-exon organization
    • Wirsel S., Lachmund A., Wildhardt G., and Ruttkowski E. Three α-amylase genes of Aspergillus oryzae exhibit identical intron-exon organization. Mol. Microbiol. 3 (1989) 3-14
    • (1989) Mol. Microbiol. , vol.3 , pp. 3-14
    • Wirsel, S.1    Lachmund, A.2    Wildhardt, G.3    Ruttkowski, E.4
  • 18
    • 0030293163 scopus 로고    scopus 로고
    • Sequence-specific binding sites in the Taka-amylase A G2 promoter for the CreA repressor mediating carbon catabolite repression
    • Kato M., Sekine K., and Tsukagoshi N. Sequence-specific binding sites in the Taka-amylase A G2 promoter for the CreA repressor mediating carbon catabolite repression. Biosci. Biotechnol. Biochem. 60 (1996) 1776-1779
    • (1996) Biosci. Biotechnol. Biochem. , vol.60 , pp. 1776-1779
    • Kato, M.1    Sekine, K.2    Tsukagoshi, N.3
  • 19
    • 0033381253 scopus 로고    scopus 로고
    • A new transcriptional activator for amylase genes in Aspergillus
    • Petersen K.L., Lehmbeck J., and Christensen T. A new transcriptional activator for amylase genes in Aspergillus. Mol. Gen. Genet. 262 (1999) 668-676
    • (1999) Mol. Gen. Genet. , vol.262 , pp. 668-676
    • Petersen, K.L.1    Lehmbeck, J.2    Christensen, T.3
  • 20
    • 0033796839 scopus 로고    scopus 로고
    • A novel nuclear factor, SREB, binds to a cis-acting element, SRE, required for inducible expression of the Aspergillus oryzae Taka-amylase A gene in A. nidulans
    • Tani S., Kawaguchi T., Kato M., Kobayashi T., and Tsukagoshi N. A novel nuclear factor, SREB, binds to a cis-acting element, SRE, required for inducible expression of the Aspergillus oryzae Taka-amylase A gene in A. nidulans. Mol. Gen. Genet. 263 (2000) 232-238
    • (2000) Mol. Gen. Genet. , vol.263 , pp. 232-238
    • Tani, S.1    Kawaguchi, T.2    Kato, M.3    Kobayashi, T.4    Tsukagoshi, N.5
  • 21
    • 0034168774 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a transcriptional activator gene, amyR, involved in the amylolytic gene expression in Aspergillus oryzae
    • Gomi K., Akeno T., Minetoki T., Ozeki K., Kumagai C., Okazaki N., and Iimura Y. Molecular cloning and characterization of a transcriptional activator gene, amyR, involved in the amylolytic gene expression in Aspergillus oryzae. Biosci. Biotechnol. Biochem. 64 (2000) 816-827
    • (2000) Biosci. Biotechnol. Biochem. , vol.64 , pp. 816-827
    • Gomi, K.1    Akeno, T.2    Minetoki, T.3    Ozeki, K.4    Kumagai, C.5    Okazaki, N.6    Iimura, Y.7
  • 22
    • 0036968875 scopus 로고    scopus 로고
    • Recent studies of protein secretion by filamentous fungi
    • Iwashita K. Recent studies of protein secretion by filamentous fungi. J. Biosci. Bioeng. 94 (2002) 530-535
    • (2002) J. Biosci. Bioeng. , vol.94 , pp. 530-535
    • Iwashita, K.1
  • 26
    • 85007767228 scopus 로고
    • High level secretion of calf chymosin using a glucoamylase-prochymosin fusion gene in Aspergillus oryzae
    • Tsuchiya K., Gomi K., Kitamoto K., Kumagai C., and Tamura G. High level secretion of calf chymosin using a glucoamylase-prochymosin fusion gene in Aspergillus oryzae. Biosci. Biotechnol. Biochem. 58 (1994) 895-899
    • (1994) Biosci. Biotechnol. Biochem. , vol.58 , pp. 895-899
    • Tsuchiya, K.1    Gomi, K.2    Kitamoto, K.3    Kumagai, C.4    Tamura, G.5
  • 27
    • 0031342633 scopus 로고    scopus 로고
    • Comparison of two glucoamylases produced by Aspergillus oryzae in solid-state culture (koji) and in submerged culture
    • Hata Y., Ishida H., Kojima Y., Ichikawa E., Kawato A., Suginami K., and Imayasu S. Comparison of two glucoamylases produced by Aspergillus oryzae in solid-state culture (koji) and in submerged culture. J. Ferment. Bioeng. 84 (1997) 532-537
    • (1997) J. Ferment. Bioeng. , vol.84 , pp. 532-537
    • Hata, Y.1    Ishida, H.2    Kojima, Y.3    Ichikawa, E.4    Kawato, A.5    Suginami, K.6    Imayasu, S.7
  • 28
    • 0032579434 scopus 로고    scopus 로고
    • Nucleotide sequence of an alternative glucoamylase-encoding gene (glaB) expressed in solid-state culture of Aspergillus oryzae
    • Hata Y., Ishida H., Ichikawa E., Kawato A., Suginami K., and Imayasu S. Nucleotide sequence of an alternative glucoamylase-encoding gene (glaB) expressed in solid-state culture of Aspergillus oryzae. Gene 207 (1998) 127-134
    • (1998) Gene , vol.207 , pp. 127-134
    • Hata, Y.1    Ishida, H.2    Ichikawa, E.3    Kawato, A.4    Suginami, K.5    Imayasu, S.6
  • 29
    • 0031710490 scopus 로고    scopus 로고
    • Regulation of the glucoamylase-encoding gene (glaB) expressed in solid-state culture (koji) of Aspergillus oryzae
    • Ishida H., Hata Y., Ichikawa E., Kawato A., Suginami K., and Imayasu S. Regulation of the glucoamylase-encoding gene (glaB) expressed in solid-state culture (koji) of Aspergillus oryzae. J. Ferment. Bioeng. 86 (1998) 301-307
    • (1998) J. Ferment. Bioeng. , vol.86 , pp. 301-307
    • Ishida, H.1    Hata, Y.2    Ichikawa, E.3    Kawato, A.4    Suginami, K.5    Imayasu, S.6
  • 30
    • 0034130410 scopus 로고    scopus 로고
    • Identification of functional elements that regulate the glucoamylase-encoding gene (glaB) expressed in solid-state culture of Aspergillus oryzae
    • Ishida H., Hata Y., Ichikawa E., Kawato A., Abe Y., Suginami K., and Imayasu S. Identification of functional elements that regulate the glucoamylase-encoding gene (glaB) expressed in solid-state culture of Aspergillus oryzae. Curr. Genet. 37 (2000) 373-379
    • (2000) Curr. Genet. , vol.37 , pp. 373-379
    • Ishida, H.1    Hata, Y.2    Ichikawa, E.3    Kawato, A.4    Abe, Y.5    Suginami, K.6    Imayasu, S.7
  • 32
    • 28444454600 scopus 로고
    • Acid-stable α-amylase of black Aspergilli part I. Detection and purification of acid-stable dextrinizing amylase
    • Minoda Y., and Yamada K. Acid-stable α-amylase of black Aspergilli part I. Detection and purification of acid-stable dextrinizing amylase. Agric. Biol. Chem. 27 (1963) 806-811
    • (1963) Agric. Biol. Chem. , vol.27 , pp. 806-811
    • Minoda, Y.1    Yamada, K.2
  • 33
    • 4544386874 scopus 로고    scopus 로고
    • Simple measurement of α-amylase activity I rice koji
    • (in Japanese)
    • Shirokane Y., Tokutake S., Tobe K., and Suzuki M. Simple measurement of α-amylase activity I rice koji. J. Brew. Soc. Jpn. 91 (1996) 889-894 (in Japanese)
    • (1996) J. Brew. Soc. Jpn. , vol.91 , pp. 889-894
    • Shirokane, Y.1    Tokutake, S.2    Tobe, K.3    Suzuki, M.4
  • 35
    • 0642371853 scopus 로고    scopus 로고
    • Distiguishable action between acid-stable and neutral α-amylases from shochu koji (Aspergillus kawachii)
    • Suganuma T., Noda N., Honbo H., and Kitahara K. Distiguishable action between acid-stable and neutral α-amylases from shochu koji (Aspergillus kawachii). Biosci. Biotechnol. Biochem. 61 (1997) 1617-1619
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 1617-1619
    • Suganuma, T.1    Noda, N.2    Honbo, H.3    Kitahara, K.4
  • 36
    • 85007984954 scopus 로고
    • Acid-stable α-amylase of black Aspergilli part III. Separation of acid-stable α-amylase and acid-unstable α-amylase from the same mold amylase preparation
    • Minoda Y., Arai M., Torigoe Y., and Yamada K. Acid-stable α-amylase of black Aspergilli part III. Separation of acid-stable α-amylase and acid-unstable α-amylase from the same mold amylase preparation. Agric. Biol. Chem. 32 (1968) 110-113
    • (1968) Agric. Biol. Chem. , vol.32 , pp. 110-113
    • Minoda, Y.1    Arai, M.2    Torigoe, Y.3    Yamada, K.4
  • 38
    • 85004654592 scopus 로고
    • Purification and some properties of acid-stable α-amylases from shochu koji (Aspergilli kawachii)
    • Mikami S., Iwano K., Shiinoki S., and Shimada T. Purification and some properties of acid-stable α-amylases from shochu koji (Aspergilli kawachii). Agric. Biol. Chem. 51 (1987) 2495-2501
    • (1987) Agric. Biol. Chem. , vol.51 , pp. 2495-2501
    • Mikami, S.1    Iwano, K.2    Shiinoki, S.3    Shimada, T.4
  • 39
    • 0019036695 scopus 로고
    • Studies of the action pattern of an α-amylase from Streptomyces praecox NA-273
    • Suganuma T., Mizukami T., Moori K., Ohnishi M., and Hiromi K. Studies of the action pattern of an α-amylase from Streptomyces praecox NA-273. J. Biochem. (Tokyo) 88 (1980) 131-138
    • (1980) J. Biochem. (Tokyo) , vol.88 , pp. 131-138
    • Suganuma, T.1    Mizukami, T.2    Moori, K.3    Ohnishi, M.4    Hiromi, K.5
  • 41
    • 0026813059 scopus 로고
    • Cloning of the α-amylase cDNA of Aspergillus shirousamii and its expression in Saccharomyces cerevisiae
    • Shibuya I., Tamura G., Ishikawa T., and Hara S. Cloning of the α-amylase cDNA of Aspergillus shirousamii and its expression in Saccharomyces cerevisiae. Biosci. Biotechnol. Biochem. 56 (1992) 174-179
    • (1992) Biosci. Biotechnol. Biochem. , vol.56 , pp. 174-179
    • Shibuya, I.1    Tamura, G.2    Ishikawa, T.3    Hara, S.4
  • 42
    • 0029885397 scopus 로고    scopus 로고
    • Molecular cloning and determination of the nucleotide sequence of a gene encoding an acid-stable α-amylase from Aspergillus kawachii
    • Kaneko A., Sudo S., Takayasu-Sakamoto Y., Tamura G., Ishikawa T., and Oba T. Molecular cloning and determination of the nucleotide sequence of a gene encoding an acid-stable α-amylase from Aspergillus kawachii. J. Ferment. Bioeng. 81 (1996) 292-298
    • (1996) J. Ferment. Bioeng. , vol.81 , pp. 292-298
    • Kaneko, A.1    Sudo, S.2    Takayasu-Sakamoto, Y.3    Tamura, G.4    Ishikawa, T.5    Oba, T.6
  • 43
    • 4444300728 scopus 로고    scopus 로고
    • Molecular cloning and determination of the nucleotide sequence of raw starch digesting α-amylase from Aspergillus awamori KT-11
    • Matsubara T., Ben Ammar Y., Anindyawati T., Yamamoto S., Ito K., Iizuka M., and Minamiura N. Molecular cloning and determination of the nucleotide sequence of raw starch digesting α-amylase from Aspergillus awamori KT-11. J. Biochem. Mol. Biol. 37 (2004) 429-438
    • (2004) J. Biochem. Mol. Biol. , vol.37 , pp. 429-438
    • Matsubara, T.1    Ben Ammar, Y.2    Anindyawati, T.3    Yamamoto, S.4    Ito, K.5    Iizuka, M.6    Minamiura, N.7
  • 44
    • 0029740660 scopus 로고    scopus 로고
    • Raw-starch-digesting and thermostable α-amylase from the yeast Cryptococcus sp. S-2: purification, characterization, cloning and sequencing
    • Iefuji H., Chino M., Kato M., and Iimura Y. Raw-starch-digesting and thermostable α-amylase from the yeast Cryptococcus sp. S-2: purification, characterization, cloning and sequencing. Biochem. J. 318 (1996) 989-996
    • (1996) Biochem. J. , vol.318 , pp. 989-996
    • Iefuji, H.1    Chino, M.2    Kato, M.3    Iimura, Y.4
  • 45
    • 0023037719 scopus 로고
    • Production and characteristics of raw-starch-digesting α-amylase from a protease-negative Aspergillus ficum mutant
    • Hayashida S., and Teramoto Y. Production and characteristics of raw-starch-digesting α-amylase from a protease-negative Aspergillus ficum mutant. Appl. Environ. Microbiol. 52 (1986) 1068-1073
    • (1986) Appl. Environ. Microbiol. , vol.52 , pp. 1068-1073
    • Hayashida, S.1    Teramoto, Y.2
  • 47
    • 0027240370 scopus 로고
    • Characteristics of acid-stable α-amylase production by submerged culture of Aspergillus kawachii
    • Sudo S., Ishikawa T., Takayasu-Sakamoto Y., Sato K., and Oba T. Characteristics of acid-stable α-amylase production by submerged culture of Aspergillus kawachii. J. Ferment. Bioeng. 76 (1993) 105-110
    • (1993) J. Ferment. Bioeng. , vol.76 , pp. 105-110
    • Sudo, S.1    Ishikawa, T.2    Takayasu-Sakamoto, Y.3    Sato, K.4    Oba, T.5
  • 48
    • 0030697488 scopus 로고    scopus 로고
    • Production of acid-stable α-amylase by Aspergillus kawachii during barley shochu-koji production
    • Kajiwara Y., Takeshima N., Ohba H., Omori T., Shimoda M., and Wada H. Production of acid-stable α-amylase by Aspergillus kawachii during barley shochu-koji production. J. Ferment. Bioeng. 84 (1997) 224-227
    • (1997) J. Ferment. Bioeng. , vol.84 , pp. 224-227
    • Kajiwara, Y.1    Takeshima, N.2    Ohba, H.3    Omori, T.4    Shimoda, M.5    Wada, H.6
  • 49
    • 0013669031 scopus 로고
    • Enzymatic modification of glucoamylase of Aspergillus awamori var kawachii
    • Yoshio E., and Hayashida S. Enzymatic modification of glucoamylase of Aspergillus awamori var kawachii. J. Ferment. Technol. 56 (1978) 289-295
    • (1978) J. Ferment. Technol. , vol.56 , pp. 289-295
    • Yoshio, E.1    Hayashida, S.2
  • 50
    • 37049015557 scopus 로고    scopus 로고
    • Acid-stable and neutral α-amylase from shochu koji (Aspergillus kawachii)
    • (in Japanese)
    • Suganuma T. Acid-stable and neutral α-amylase from shochu koji (Aspergillus kawachii). Kagaku to Kogyo 79 (2005) 163-168 (in Japanese)
    • (2005) Kagaku to Kogyo , vol.79 , pp. 163-168
    • Suganuma, T.1
  • 52
    • 0029679085 scopus 로고    scopus 로고
    • N-terminal sequence of amino acids and some properties of an acid-stable α-amylase from citric acid-koji (Aspergillus usamii var.)
    • Suganuma T., Tahara N., Kitahara K., Nagahama T., and Inuzuka K. N-terminal sequence of amino acids and some properties of an acid-stable α-amylase from citric acid-koji (Aspergillus usamii var.). Biosci. Biotechnol. Biochem. 60 (1996) 177-179
    • (1996) Biosci. Biotechnol. Biochem. , vol.60 , pp. 177-179
    • Suganuma, T.1    Tahara, N.2    Kitahara, K.3    Nagahama, T.4    Inuzuka, K.5
  • 53
    • 37049031013 scopus 로고    scopus 로고
    • Study on two types of α-amylase, the acid-stable and the neutral. Characterization of acid-stable α-amylase from citric acid koji
    • (in Japanese)
    • Suganuma T. Study on two types of α-amylase, the acid-stable and the neutral. Characterization of acid-stable α-amylase from citric acid koji. J. Appl. Glycosci. 48 (2001) 187-193 (in Japanese)
    • (2001) J. Appl. Glycosci. , vol.48 , pp. 187-193
    • Suganuma, T.1
  • 54
    • 0030033388 scopus 로고    scopus 로고
    • Elucidation of the subsite structure of bacterial saccharifying α-amylase and its mode of degradation of maltose
    • Suganuma T., Ohnishi M., Hiromi K., and Nagahama T. Elucidation of the subsite structure of bacterial saccharifying α-amylase and its mode of degradation of maltose. Carbohydr. Res. 282 (1996) 171-180
    • (1996) Carbohydr. Res. , vol.282 , pp. 171-180
    • Suganuma, T.1    Ohnishi, M.2    Hiromi, K.3    Nagahama, T.4
  • 55
    • 0014943898 scopus 로고
    • Interpretation of dependency of rate parameters on the degree of polymerization of substrate in enzyme-catalyzed reactions. Evaluation of subsite affinities of exo-enzyme
    • Hiromi K. Interpretation of dependency of rate parameters on the degree of polymerization of substrate in enzyme-catalyzed reactions. Evaluation of subsite affinities of exo-enzyme. Biochem. Biophys. Res. Commun. 40 (1970) 1-6
    • (1970) Biochem. Biophys. Res. Commun. , vol.40 , pp. 1-6
    • Hiromi, K.1
  • 56
    • 0015240182 scopus 로고
    • Subsite mapping of enzymes. Correlation of product patterns with Michaelis parameters and substrate-induced strain
    • Thoma J.A., Rao G.V.K., Brothers C., and Spradlin J. Subsite mapping of enzymes. Correlation of product patterns with Michaelis parameters and substrate-induced strain. J. Biol. Chem. 246 (1971) 5621-5635
    • (1971) J. Biol. Chem. , vol.246 , pp. 5621-5635
    • Thoma, J.A.1    Rao, G.V.K.2    Brothers, C.3    Spradlin, J.4
  • 57
    • 33947186739 scopus 로고    scopus 로고
    • Simultaneous production of glucoamylase and acid-stable α-amylase using novel submerged culture of Aspergillus kawachii NBRC4308
    • Shoji H., Sugimoto T., Hosoi K., Shibata K., Tanabe M., and Kawatsura K. Simultaneous production of glucoamylase and acid-stable α-amylase using novel submerged culture of Aspergillus kawachii NBRC4308. J. Biosci. Bioeng. 103 (2007) 203-205
    • (2007) J. Biosci. Bioeng. , vol.103 , pp. 203-205
    • Shoji, H.1    Sugimoto, T.2    Hosoi, K.3    Shibata, K.4    Tanabe, M.5    Kawatsura, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.