Immobilization of d-amino acid oxidase from different yeasts: Characterization and application in the deamination of cephalosporin C

1995 ◽  
Vol 17 (4) ◽  
pp. 324-329 ◽  
Author(s):  
P. Golini ◽  
D. Bianchi ◽  
E. Battistel ◽  
P. Cesti ◽  
R. Tassinari
Keyword(s):  
Amino Acid ◽  
Acid Oxidase ◽  
Cephalosporin C ◽  
Amino Acid Oxidase

Production ofD-amino acid oxidase byAspergillussp. strain O20 active on cephalosporin C

1997 ◽  
Vol 43 (3) ◽  
pp. 292-295 ◽  
Author(s):  
Salim K. Mujawar ◽  
Jaiprakash G. Shewale
Keyword(s):  
Amino Acids ◽  
Enzyme Activity ◽  
Amino Acid ◽  
Stationary Growth Phase ◽  
Acid Oxidase ◽  
Cephalosporin C ◽  
Production Medium ◽  
Stationary Growth ◽  
Amino Acid Oxidase ◽  
Aspergillus Sp

Aspergillus sp. strain O20 produces inducible D-amino acid oxidase intracellularly, only in the presence of some amino acids. The enzyme was induced most effectively by the addition of DL-alanine (1% w/v) to the production medium. Among the various compounds studied, production of the D-amino acid oxidase was enhanced by Aerosol-22, glucose, and sodium nitrate. D-Amino acid oxidase formation was observed during the onset of the stationary growth phase. Maximum enzyme activity was recorded after 96 h of fermentation (1000 IU/L).Key words: D-amino acid oxidase, Aspergillus sp., 7-aminocephalosporanic acid, cephalosporin C.

scholarly journals Multipoint TvDAAO Mutants for Cephalosporin C Bioconversion

2019 ◽  
Vol 20 (18) ◽  
pp. 4412
Author(s):  
Denis L. Atroshenko ◽  
Mikhail D. Shelomov ◽  
Sophia A. Zarubina ◽  
Nikita Y. Negru ◽  
Igor V. Golubev ◽  
...  
Keyword(s):  
Amino Acid ◽  
Thermal Denaturation ◽  
Catalytic Properties ◽  
Acid Oxidase ◽  
Cephalosporin C ◽  
Wild Type ◽  
Wild Type Enzyme ◽  
Amino Acid Oxidase ◽  
Catalytic Constant ◽  
Biotechnological Processes

d-amino acid oxidase (DAAO, EC 1.4.3.3) is used in many biotechnological processes. The main industrial application of DAAO is biocatalytic production of 7-aminocephalosporanic acid from cephalosporin C with a two enzymes system. DAAO from the yeast Trigonopsis variabilis (TvDAAO) shows the best catalytic parameters with cephalosporin C among all known DAAOs. We prepared and characterized multipoint TvDAAO mutants to improve their activity towards cephalosporin C and increase stability. All TvDAAO mutants showed better properties in comparison with the wild-type enzyme. The best mutant was TvDAAO with amino acid changes E32R/F33D/F54S/C108F/M156L/C298N. Compared to wild-type TvDAAO, the mutant enzyme exhibits a 4 times higher catalytic constant for cephalosporin C oxidation and 8- and 20-fold better stability against hydrogen peroxide inactivation and thermal denaturation, respectively. This makes this mutant promising for use in biotechnology. The paper also presents the comparison of TvDAAO catalytic properties with cephalosporin C reported by others.

Bioconversion of cephalosporin C with D-amino acid oxidase from the yeastRhodosporidium toruloides

1994 ◽  
Vol 16 (5) ◽  
pp. 467-472 ◽  
Author(s):  
Yun-Huey Lee ◽  
Wen-Shen Chu ◽  
Wen-Hwei Hsu
Keyword(s):  
Amino Acid ◽  
Acid Oxidase ◽  
Cephalosporin C ◽  
Amino Acid Oxidase
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