Production of D-amino acid oxidase from Aspergillus sojae

Mamoru Wakayama; Yuka Takeuchi; Katsuyuki Tasaka; Kenji Sakai; Mitsuaki Moriguchi

doi:10.1016/0922-338X(96)85045-8

Production of D-amino acid oxidase from Aspergillus sojae

Mamoru Wakayama, Yuka Takeuchi, Katsuyuki Tasaka, Kenji Sakai, Mitsuaki Moriguchi

Research output: Contribution to journal › Article › peer-review

6 Citations (Scopus)

Abstract

D-Amino acid oxidase activities for D-glutamate (D-Glu), D-aspartate (D- Asp) and D-alanine (D-Ala) were found in cell-free extract of Aspergillus sojae (A. sojae). The enzyme activities for these three substrates increased over 30-fold by the addition of 0.25% D-Ala to the culture medium. Glycerol was an effective carbon source for increasing the enzyme activities. D-Ala, D-serine (D-Ser), and D-tryptophan (D-Trp) were better inducers than other D- amino acids. D-Glu and D-Asp were oxidized at rates of 70 and 6%, respectively, relative to the rate of oxidation of D-Ala which was taken as 100%. A. sojae D-amino acid oxidase showed no inhibition by sodium benzoate or dicarboxylates and had a molecular weight of 129,000, which differed substantially from those of D-amino acid oxidases of porcine and rabbit kidney.

Original language	English
Pages (from-to)	177-179
Number of pages	3
Journal	Journal of Fermentation and Bioengineering
Volume	82
Issue number	2
DOIs	https://doi.org/10.1016/0922-338X(96)85045-8
Publication status	Published - 1996
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biotechnology
Applied Microbiology and Biotechnology

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10.1016/0922-338X(96)85045-8

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@article{2706247115b84bdfb98d650ed762c576,

title = "Production of D-amino acid oxidase from Aspergillus sojae",

abstract = "D-Amino acid oxidase activities for D-glutamate (D-Glu), D-aspartate (D- Asp) and D-alanine (D-Ala) were found in cell-free extract of Aspergillus sojae (A. sojae). The enzyme activities for these three substrates increased over 30-fold by the addition of 0.25% D-Ala to the culture medium. Glycerol was an effective carbon source for increasing the enzyme activities. D-Ala, D-serine (D-Ser), and D-tryptophan (D-Trp) were better inducers than other D- amino acids. D-Glu and D-Asp were oxidized at rates of 70 and 6%, respectively, relative to the rate of oxidation of D-Ala which was taken as 100%. A. sojae D-amino acid oxidase showed no inhibition by sodium benzoate or dicarboxylates and had a molecular weight of 129,000, which differed substantially from those of D-amino acid oxidases of porcine and rabbit kidney.",

author = "Mamoru Wakayama and Yuka Takeuchi and Katsuyuki Tasaka and Kenji Sakai and Mitsuaki Moriguchi",

year = "1996",

doi = "10.1016/0922-338X(96)85045-8",

language = "English",

volume = "82",

pages = "177--179",

journal = "Journal of Fermentation and Bioengineering",

issn = "0922-338X",

publisher = "The Society for Biotechnology, Japan",

number = "2",

}

TY - JOUR

T1 - Production of D-amino acid oxidase from Aspergillus sojae

AU - Wakayama, Mamoru

AU - Takeuchi, Yuka

AU - Tasaka, Katsuyuki

AU - Sakai, Kenji

AU - Moriguchi, Mitsuaki

PY - 1996

Y1 - 1996

N2 - D-Amino acid oxidase activities for D-glutamate (D-Glu), D-aspartate (D- Asp) and D-alanine (D-Ala) were found in cell-free extract of Aspergillus sojae (A. sojae). The enzyme activities for these three substrates increased over 30-fold by the addition of 0.25% D-Ala to the culture medium. Glycerol was an effective carbon source for increasing the enzyme activities. D-Ala, D-serine (D-Ser), and D-tryptophan (D-Trp) were better inducers than other D- amino acids. D-Glu and D-Asp were oxidized at rates of 70 and 6%, respectively, relative to the rate of oxidation of D-Ala which was taken as 100%. A. sojae D-amino acid oxidase showed no inhibition by sodium benzoate or dicarboxylates and had a molecular weight of 129,000, which differed substantially from those of D-amino acid oxidases of porcine and rabbit kidney.

AB - D-Amino acid oxidase activities for D-glutamate (D-Glu), D-aspartate (D- Asp) and D-alanine (D-Ala) were found in cell-free extract of Aspergillus sojae (A. sojae). The enzyme activities for these three substrates increased over 30-fold by the addition of 0.25% D-Ala to the culture medium. Glycerol was an effective carbon source for increasing the enzyme activities. D-Ala, D-serine (D-Ser), and D-tryptophan (D-Trp) were better inducers than other D- amino acids. D-Glu and D-Asp were oxidized at rates of 70 and 6%, respectively, relative to the rate of oxidation of D-Ala which was taken as 100%. A. sojae D-amino acid oxidase showed no inhibition by sodium benzoate or dicarboxylates and had a molecular weight of 129,000, which differed substantially from those of D-amino acid oxidases of porcine and rabbit kidney.

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U2 - 10.1016/0922-338X(96)85045-8

DO - 10.1016/0922-338X(96)85045-8

M3 - Article

AN - SCOPUS:0029793526

SN - 0922-338X

VL - 82

SP - 177

EP - 179

JO - Journal of Fermentation and Bioengineering

JF - Journal of Fermentation and Bioengineering

IS - 2

ER -

Production of D-amino acid oxidase from Aspergillus sojae

Abstract

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