Enzymatic oxidation of cephalosporin C using whole cells of the yeast Triginopsis variabilis within a “cross-flow filter-reactor”

Vicenzi, Jeffrey T.; Hansen, Guy J.

doi:10.1016/0141-0229(93)90150-z

Cited by 39 publications

(23 citation statements)

References 4 publications

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“…The results obtained here show that the stability of the enzyme is greater than that reported by Vicenzy et al 6 for DAAO contained in T variabilis cells permeabilized with acetone, which shows a halflife of 12.5 h in sodium phosphate buffer, pH 7.5 at 25…”

Section: Time (Days)contrasting

confidence: 76%

Thermal deactivation and inhibition of D‐Amino acid oxidase in permeabilized cells of the yeast Trigonopsis variabilis

Moreno

Ruiz

Catalán

et al. 2004

J of Chemical Tech & Biotech

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The inhibition of D-amino acid oxidase contained in permeabilized cells of the yeast Trigonopsis variabilis by α-keto acids (pyruvic acid, phenylpyruvic acid and 4-methylthio-2-oxobutanoic acid), products of the transformation of the corresponding D-amino acids, was studied. In all cases, inhibition was of the mixed type and significant differences with respect to the inhibition shown by the enzyme from other sources such as pig kidney or the yeast Rhodotorula gracilis were observed. A study was also made of the thermal deactivation of the enzyme contained in permeabilized cells of T variabilis in the temperature range 30-50• C in sodium phosphate and Tris hydroxylmethyl aminomethane + CaCl 2 buffers. A deactivation mechanism with two steps in series is proposed to account for the variation in activity with time. The results suggest that the enzyme shows greater stability in phosphate buffer, with half-lives between 7.6 days at 30• C and 8.6 h at 50 • C.  2004 Society of Chemical Industry

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Section: Time (Days)contrasting

confidence: 76%

Thermal deactivation and inhibition of D‐Amino acid oxidase in permeabilized cells of the yeast Trigonopsis variabilis

Moreno

Ruiz

Catalán

et al. 2004

J of Chemical Tech & Biotech

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“…This use was first proposed in the early 1970s when only pkDAAO, an enzyme not suited for its low turnover for industrial applications, was available [89]. Later conversion of cephalosporin C was attempted using immobilized DAAO from T. 6ariabilis (the source cited most in the technical literature) and R. glutinis [90,91]. None of these attempts were successful; either the immobilized system was insufficiently stable or conversion yields were low.…”

Section: Biotechnology Of Daaomentioning

confidence: 99%

D-Amino acid oxidase: new findings

Pilone¹

2000

CMLS, Cell. Mol. Life Sci.

187

177

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The most recent research on D-amino acid oxidases and D-amino acid metabolism has revealed new, intriguing properties of the flavoenzyme and enlighted novel biotechnological uses of this catalyst. Concerning the in vivo function of the enzyme, new findings on the physiological role of D-amino acid oxidase point to a detoxifying function of the enzyme in metabolizing exogenous D-amino acids in animals. A novel role in modulating the level of D-serine in brain has also been proposed for the enzyme. At the molecular level, site-directed mutagenesis studies on the pig kidney D-amino acid oxidase and, more recently, on the enzyme from the yeast Rhodotorula gracilis indicated that the few conserved residues of the active site do not play a role in acid-base catalysis but rather are involved in substrate interactions. The three-dimensional structure of the enzyme was recently determined from two different sources: at 2.5-3.0 A resolution for DAAO from pig kidney and at 1.2-1.8 A resolution for R. gracilis. The active site can be clearly depicted: the striking absence of essential residues acting in acid-base catalysis and the mode of substrate orientation into the active site, taken together with the results of free-energy correlation studies, clearly support a hydrid transfer type of mechanism in which the orbital steering between the substrate and the isoalloxazine atoms plays a crucial role during catalysis.

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“…From the data, the presence of an equilibrium between cephalosporin C and glutaryl-7-ACA can be envisaged, through a reaction intermediate with a R t of about 8.2 rain. It can be suggested that this intermediate is ketoadipyl-7-ACA, which is very unstable in solution and gives unknown decomposition products (Vicenzi et al, 1993), however not detected under our experimental conditions. In the presence of hydrogen peroxide this intermediate deearboxylates, thus shifting the equilibrium towards glutaryl-7-ACA production and increasing bioconversion yield (up to 99 %).…”

Section: Resultsmentioning

confidence: 86%

“…Recently our group developed successfully a bioreactor system for the production of o~-ketoacids by immobilized Rgracilis DAAO (But6 et al, 1994). Bioconversion ofcephalosporin C to ketoadipyl-7-ACA has been previously reported also for DAAO from pig kidney (Mazzeo and Romeo, 1972;Sauber, 1993), from Trigonopsis variabilis (Szwajcer and Mosbach, 1985;Vicenzi and Hansen, 1993) and recently from Rhodosporidium toruloides (YunHuey et al, 1994). In all cases, either with whole cells or purified enzyme, the results were unsatisfactory: a low conversion yield was measured and a massive presence of side-products was detected.…”

Section: Introductionmentioning

confidence: 99%

A process for bioconversion of cephalosporin C by Rhodotorula gracilis D-amino acid oxidase

1995

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A process for the production (in a stirred tank reactor) of glutaryl-7-ACA from cephalosporin C using immobilized D-amino acid oxidase is described. Results so obtained under optimal conditions (1.2 mg coupled enzyme/L, pH 8.5, 2 mM cephalosporin C) point to a system which shows high conversion efficiency and a remarkable operational stability. No exogenous H202 is requested to shift the reaction equilibrium toward glutaryl-7-ACA production, nor any side product is detected. The immobilized system productivity was 54 g/day/mg of enzyme. This process represents the first reported case of a reactor successfully developed with a DAAO for bioconversion of cephalosporin C.

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Enzymatic oxidation of cephalosporin C using whole cells of the yeast Triginopsis variabilis within a “cross-flow filter-reactor”

Cited by 39 publications

References 4 publications

Thermal deactivation and inhibition of D‐Amino acid oxidase in permeabilized cells of the yeast Trigonopsis variabilis

Thermal deactivation and inhibition of D‐Amino acid oxidase in permeabilized cells of the yeast Trigonopsis variabilis

D-Amino acid oxidase: new findings

A process for bioconversion of cephalosporin C by Rhodotorula gracilis D-amino acid oxidase

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