Properties and Potential Applications of Arginase Immobilized by Radiation‐induced Polymerization of Acrylic Monomers<sup>a</sup>

Veronese, Francesco M.; Visco, C.; Benassi, C. A.; Lora, S.; Carenza, M.; Palma, G.

doi:10.1111/j.1749-6632.1988.tb25815.x

Cited by 10 publications

(3 citation statements)

References 4 publications

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“…This could be ascribed to the denaturing action of acrylic monomers on arginase. This is partly due to the free acid present in the commercial products and partly to the monomers' own properties [13]. Satisfactory yields of incorporation in the polymer matrix were only obtained with highly purified HEA and by reducing as much as possible the duration of contact between the enzyme and the monomer at room temperature.…”

Section: Discussionmentioning

confidence: 99%

Arginase Immobilization on Poly(hydroxyethyl acrylate) Matrix Beads

Veronese

Boccù

Caliceti

et al. 1989

Journal of Bioactive and Compatible Polymers

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A study was made on the preparation and behaviour of polymer matrix im mobilized arginase, an enzyme involved in the urea cycle. Immobilization of purified calf liver arginase was obtained by a physical entrapment method based on the low temperature polymerization induced by radiation of a glass forming monomer mixed with an aqueous solution of the enzyme. Enzymatic activity was found to be retained in an acceptable range (30-35%) in a bead shaped matrix only when the monomer was hydroxyethylacrylate (HEA) purified by alkaline extraction and a particular sample preparation procedure was followed. The poly(hydroxyethyl acrylate) (PHEA) immobilized arginase was characterized by evaluating its chemical and enzymological properties such as Km, activation energy, stability to proteolytic enzymes, and activity de pendence on pH. Performance runs of continuous biocatalytic conversion of ar ginine to ornithine were carried out utilizing a reactor consisting of a column with immobilized arginase beads. After weeks of operation the substrate con version remained almost constant, indicating a practically unaltered enzy matic activity. PHEA immobilized arginase beads also retained their activity for days either in the presence of whole blood or when implanted intraperi toneally or subcutaneously into rats. No significant inflammation or other adverse reactions were observed after one week of residence of such implants. This seems promising for lowering the arginine blood level in specific diseases

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Section: Discussionmentioning

confidence: 99%

Arginase Immobilization on Poly(hydroxyethyl acrylate) Matrix Beads

Veronese

Boccù

Caliceti

et al. 1989

Journal of Bioactive and Compatible Polymers

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“…Most examples of studies on the application of arginase are focused on analytical purposes,30–34 while only a few investigate its application for the production of L ‐ornithine 35–37. One of the more elaborate studies on the enzymatic L ‐ornithine production is by Bommarius et al 37.…”

Section: Introductionmentioning

confidence: 99%

“…On an industrial scale, the immobilization of enzymes is desirable, as this enables reuse and overcomes problems with product recovery. There are several example of arginase immobilization, either by entrapment in a matrix32,35 or covalent binding to a support 30,31,34,36. However, immobilization of arginase on commercially available and industrially relevant epoxy‐activated supports was not tested until now.…”

Section: Introductionmentioning

confidence: 99%

Stabilized and Immobilized Bacillus subtilis Arginase for the Biobased Production of Nitrogen‐Containing Chemicals

et al. 2010

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l-Ornithine could serve as an intermediate in the biobased production of 1,4-diaminobutane from l-arginine. Using the concept of biorefinery, larginine could become widely available from biomass waste streams via the nitrogen storage polypeptide cyanophycin. Selective hydrolysis of l-arginine to l-ornithine is difficult to perform chemically, therefore the stabilization and immobilization of Bacillus subtilis arginase (EC 3.5.3.1) was studied in a continuously stirred membrane reactor system. Initial pH of the substrate solution, addition of l-aspartic acid and reducing agents all appeared to have an effect on the operational stability of B. subtilis arginase. A remarkably good operational stability (total turnover number, TTN = 1.13·10 8 ) at the pH of arginine free base (pH 11.0) was observed, which was further improved with the addition of sodium dithionite to the substrate solution (TTN > 1·10 9 ). B. subtilis arginase was successfully immobilized on three commercially available epoxy-activated supports. Immobilization on Sepabeads EC-EP was most promising, resulting in a recovered activity of 75% and enhanced thermostability. In conclusion, the stabilization and immobilization of B. subtilis arginase has opened up possibilities for its application in the biobased production of nitrogen-containing chemicals as an alternative to the petrochemical production.

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Immobilization, characterization, and laboratory-scale application of bovine liver arginase

Dala¹,

Szajáni²

1994

Appl Biochem Biotechnol

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Arginase isolated from beef liver was covalently attached to a polyacrylamide bead support bearing carboxylic groups activated by a water-soluble carbodiimide. The most favorable carbodiimide was N-cyclohexyl-N'-(methyl-2-p-nitrophenyl-2-oxoethyl) aminopropyl carbodiimide methyl bromide, but for practical purposes, N-cyclohexyl-N'-morpholinoethyl carbodiimide methyl tosylate was used. The optimal conditions for the coupling procedure were determined. The catalytic activity of the immobilized arginase was 290-340 U/g solid or 2.9-3.4 U/mL wet gel. The pH optimum for the catalytic activity was pH 9.5, the apparent temperature maximum was at 60 degrees C and Kmapp was calculated to be 0.37M L-arginine. Immobilization markedly improved the conformational stability of arginase. At 60 degrees C, the pH for maximal stability was found to be 8.0. The immobilized arginase was used for the production of L-ornithine and D-arginine.

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Properties and Potential Applications of Arginase Immobilized by Radiation‐induced Polymerization of Acrylic Monomers^a

Cited by 10 publications

References 4 publications

Arginase Immobilization on Poly(hydroxyethyl acrylate) Matrix Beads

Arginase Immobilization on Poly(hydroxyethyl acrylate) Matrix Beads

Stabilized and Immobilized Bacillus subtilis Arginase for the Biobased Production of Nitrogen‐Containing Chemicals

Immobilization, characterization, and laboratory-scale application of bovine liver arginase

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Properties and Potential Applications of Arginase Immobilized by Radiation‐induced Polymerization of Acrylic Monomersa

Cited by 10 publications

References 4 publications

Arginase Immobilization on Poly(hydroxyethyl acrylate) Matrix Beads

Arginase Immobilization on Poly(hydroxyethyl acrylate) Matrix Beads

Stabilized and Immobilized Bacillus subtilis Arginase for the Biobased Production of Nitrogen‐Containing Chemicals

Immobilization, characterization, and laboratory-scale application of bovine liver arginase

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Properties and Potential Applications of Arginase Immobilized by Radiation‐induced Polymerization of Acrylic Monomers^a