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Analysis of extracellular proteins of Aspergillus oryzae grown on soy sauce koji
Analysis of extracellular proteins of Aspergillus oryzae grown on soy sauce koji
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Analysis of extracellular proteins of Aspergillus oryzae grown on soy sauce koji

Liang, Y.(South China Univ. of Technology, Guangzhou) ; Pan, L ; Lin, Y

Bioscience, biotechnology, and biochemistry, 2009-01, Vol.73 (1), p.192-195 [Periódico revisado por pares]

Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry

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2
Purification and characterization of an N-terminal acidic amino acid-specific aminopeptidase from soybean cotyledons (Glycine max)
Purification and characterization of an N-terminal acidic amino acid-specific aminopeptidase from soybean cotyledons (Glycine max)
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Purification and characterization of an N-terminal acidic amino acid-specific aminopeptidase from soybean cotyledons (Glycine max)

Asano, M., Ajinomoto Co. Inc., Kawasaki, Kanagawa (Japan). Inst. of Life Sciences ; Nakamura, N ; Kawai, M ; Miwa, T ; Nio, N

Bioscience, biotechnology, and biochemistry, 2010-01, Vol.74 (1), p.113-118 [Periódico revisado por pares]

Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry

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3
Characterization of Aspergillus oryzae aspartyl aminopeptidase expressed in Escherichia coli
Characterization of Aspergillus oryzae aspartyl aminopeptidase expressed in Escherichia coli
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Characterization of Aspergillus oryzae aspartyl aminopeptidase expressed in Escherichia coli

Watanabe, J.(Yamasa Corp., Choshi, Chiba (Japan)) ; Tanaka, H ; Akagawa, T ; Mogi, Y ; Yamazaki, T

Bioscience, biotechnology, and biochemistry, 2007-10, Vol.71 (10), p.2557-2560 [Periódico revisado por pares]

Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry

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4
Purification and characterization of a Cl(-)-activated aminopeptidase from bovine skeletal muscle
Purification and characterization of a Cl(-)-activated aminopeptidase from bovine skeletal muscle
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Purification and characterization of a Cl(-)-activated aminopeptidase from bovine skeletal muscle

Migita, K.(Hiroshima Univ. (Japan)) ; Nishimura, T

Bioscience, biotechnology, and biochemistry, 2006-05, Vol.70 (5), p.1110-1117 [Periódico revisado por pares]

Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry

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5
Biochemical analysis of the yeast proteinase inhibitor (IC) homolog ICh and its comparison with IC
Biochemical analysis of the yeast proteinase inhibitor (IC) homolog ICh and its comparison with IC
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Biochemical analysis of the yeast proteinase inhibitor (IC) homolog ICh and its comparison with IC

Fukuda, H.(Kyoto Univ. (Japan)) ; Mima, J ; Nagayama, M ; Kato, M ; Ueda, M

Bioscience, biotechnology, and biochemistry, 2007-02, Vol.71 (2), p.472-480 [Periódico revisado por pares]

Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry

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6
New deblocking aminopeptidases from Pyrococcus horikoshii
New deblocking aminopeptidases from Pyrococcus horikoshii
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New deblocking aminopeptidases from Pyrococcus horikoshii

Mori, K.(National Inst. of Advanced Industrial Science and Technology Kansai, Ikeda, Osaka (Japan)) ; Ishikawa, K

Bioscience, biotechnology, and biochemistry, 2005-10, Vol.69 (10), p.1854-1860 [Periódico revisado por pares]

Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry

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7
Purification and some properties of an aminopeptidase from the seeds of Cannabis sativa
Purification and some properties of an aminopeptidase from the seeds of Cannabis sativa
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Purification and some properties of an aminopeptidase from the seeds of Cannabis sativa

Arima, K. (Kagoshima Univ. (Japan). Faculty of Science) ; Uchikoba, T ; Shimada, M ; Yonezawa, H ; Kaneda, M

Bioscience, biotechnology, and biochemistry, 2000-05, Vol.64 (5), p.1055-1057 [Periódico revisado por pares]

Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry

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8
Catalytic properties of x-prolyl dipeptidyl aminopeptidase from Lactococcus lactis subsp. cremoris nTR
Catalytic properties of x-prolyl dipeptidyl aminopeptidase from Lactococcus lactis subsp. cremoris nTR
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Catalytic properties of x-prolyl dipeptidyl aminopeptidase from Lactococcus lactis subsp. cremoris nTR

Yan, T.R. (Tatung Inst. of Technology, Taipei (Taiwan)) ; Ho, S.C ; Hou, C.L

Bioscience, biotechnology, and biochemistry, 1992, Vol.56 (5), p.704-707 [Periódico revisado por pares]

ABINGDON: Taylor & Francis

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9
Isolation and characterization of a dipeptidyl aminopeptidase from Streptomyces sp. WM-23
Isolation and characterization of a dipeptidyl aminopeptidase from Streptomyces sp. WM-23
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Isolation and characterization of a dipeptidyl aminopeptidase from Streptomyces sp. WM-23

Murao, S. (Kumamoto Inst. of Technology (Japan)) ; Kitade, T ; Oyama, H ; Shin, T

Bioscience, biotechnology, and biochemistry, 1994, Vol.58 (8), p.1545-1546 [Periódico revisado por pares]

Tokyo: Taylor & Francis

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10
Debittering of a tryptic hydrolysate of casein by incubating with the ice nucleationactive bacterium, Erwinia ananas, and its aminopeptidase at low temperature
Debittering of a tryptic hydrolysate of casein by incubating with the ice nucleationactive bacterium, Erwinia ananas, and its aminopeptidase at low temperature
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Debittering of a tryptic hydrolysate of casein by incubating with the ice nucleationactive bacterium, Erwinia ananas, and its aminopeptidase at low temperature

Watanabe, M. (Tokyo Gakugei Univ., Koganei (Japan)) ; Shimizu, J ; Arai, S

Agricultural and biological chemistry, 1990-12, Vol.54 (12)

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