Decarboxylation of l-tyrosine and l-dopa by immobilized cells of Papaver somniferum

Stano, J.; Němec, Pavel; Weissová, K; Kovács, P.; Kákoniová, D.; Lišková, Desana

doi:10.1016/0031-9422(94)00768-o

Cited by 14 publications

(7 citation statements)

References 13 publications

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“…The immobilization of gherkin, poppy and ginseng cells by glutaraldehyde and their storage in 0.15 M NaCl with 0.02% sodium azide solution seems to be a very convenient method for long-term preservation of different catalysts [5,6,241. However, the conservation of multifunctional enzyme systems of the cell needs further study.…”

Section: Methyldodecyi)-dimethylamine-4-oxidementioning

confidence: 99%

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β‐Galactosidase in immobilized cells of Daucus carota L.

Poór¹

1997

Acta Biotechnologica

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The cell suspension cultull: Duuclls curotu L. was permenbilized by Tween 80 and immobilized by glutaraldehyde. j3-Galactosidase showed an optimum pH of 4.7 and an optimum temperature of 55 "C. The enzyme hydrolysis was linear for 3 h, reaching a 65% conversion. A very good level of storage stability wils achieved when using dry catalyst, or a solution of 0.15 M NaCl with the addition of chloramphenicol, (I-methyldodecyl)-dimethylamin-4-oxide (ATDNO), chlortetracycline hydrochloride (CLCTC) or by freezing the immobilized cells in 0.15 M NaC1. The cells characterized by high enzyme activity and stability in long-term storage showed convenient physicomechanical properties.

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Section: Methyldodecyi)-dimethylamine-4-oxidementioning

confidence: 99%

“…Recently, the use of polyvinyl-alcohol and glutaraldehyde [12, 131, or Tween 80 and glutaraldehyde [2] for cell immobilization has been investigated. P-Galactosidase (PD-galactoside galactohydrolase EC 3.2.1.23) catalyzes the hydrolysis of the terminal Pgalactose linkage of glycosides.…”

Section: Introductionmentioning

confidence: 99%

β‐Galactosidase in immobilized cells of Daucus carota L.

Poór¹

1997

Acta Biotechnologica

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“…The spontaneous adhesion or covalent binding of cells to the surface of insoluble carriers was also examined [9, 10]. Recently, polyvinylalcohol and glutaraldehyde [11,12] or Tween 80 and glutaraldehyde [13] have been used for cell immobilization.Melibiase (α-D-galactoside galactohydrolase EC 3.2.1.22) α-galactosidase is an exoglycosidase removing terminal galactose residues from the galactosaccharides and carbohydrate moiety of glycoproteins. Melibiase is of particular interest in view of its biotechnological applications.…”

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confidence: 99%

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Melibiase in Immobilized Cells of Watermelon

et al. 2005

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Cells of suspension culture Citrullus vulgaris cv. "Samara" were permeabilized by Tween 80 and immobilized by glutaraldehyde. The highest melibiase activity was at pH 5.4 and 60°C. The hydrolysis of substrate was linear for 3.5 h, reaching 65-70% conversion of the substrate. The cells, characterized by high enzyme activity and stability in long-term storage, showed convenient physico-mechanical properties (physical protection from shear forces and easy separation of product from biocatalysts).Plant cells were first immobilized by Brodelius et al. 1979 [1]. In the last decades several methods for fixation of biocatalysts have been developed. Enzymes, living or nonliving microorganisms and animal and plant cells, as well as combined systems, have been bound within or to carrier materials [2][3][4][5]. Immobilization of cells or enzymes represents an effective way to obtain highly efficient enzyme catalysts important for biotransformation processes [6]. Many matrices from synthetic polymers or biological materials (e.g., agar, agarose, kappa-carragneenan, collagen, chitosan, polyacrylamide, polyurethane, cellulose) have been used for the immobilization of cells [7,8]. The spontaneous adhesion or covalent binding of cells to the surface of insoluble carriers was also examined [9, 10]. Recently, polyvinylalcohol and glutaraldehyde [11,12] or Tween 80 and glutaraldehyde [13] have been used for cell immobilization.Melibiase (α-D-galactoside galactohydrolase EC 3.2.1.22) α-galactosidase is an exoglycosidase removing terminal galactose residues from the galactosaccharides and carbohydrate moiety of glycoproteins. Melibiase is of particular interest in view of its biotechnological applications. The enzyme has been employed for the hydrolysis of raffinose to aid in the crystallization of sucrose. The studied enzyme is also used to convert the galactooligosaccharides (stachyose, verbascose, ajugose) in soybean meal to food and feed materials [14].Microrgamisms are the preferred sources of melibiase [15]. Although melibiase is generally present also in plants, this source has not been used previously. In this paper, the enzymatic hydrolysis of the terminal α-galactosidic linkage of glycosides (raffinose, stachyose) by free, as well as glutaraldehyde-immobilized, cells of Citrullus vulgaris cv. "Samara" was studied.Cells immmobilized by cell entrapment are cultivated in a similar way as cell suspension cultures [7,8,16]. The microscopic observation of watermelon cells immobilized with glutaraldehyde showed small morphological changes in comparison with cells in suspension. A thinning of the cell walls after permeabilization by Tween 80 was observed. Important was also the appearance of cell plasmolysis and a small aggregation of cells occurring after immobilization. According to the respiration rate and vital staining (fluorescein or 2,3,5-triphenyltetrazolium chloride), cells immobilized by glutaraldehyde were not viable. Also glucose was utilized only by cells in suspension, but not by immobilized ones (Fig. 1).The permeabil...

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“…Currently, the most widely used cell-immobilization technique involves entrapment in hydrogels. The spontaneous adhesion or covalent binding of cells to the surface of insoluble carriers has also been described [3], as well as cell immobilization with polyvinyl alcohol [4] or glutaraldehyde [5] [6].…”

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Bioassay for the Determination of the Intra‐ and Extracellular Activity of Aminopeptidases in Immobilized Tomato Cells

Stano

Mičieta

Tintemann

et al. 2006

Chemistry & Biodiversity

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Permeabilized tomato cells were cross-linked with glutaraldehyde in the absence of a carrier. The immobilized cells demonstrated significantly lower aminopeptidase (AP) activities than untreated control cells. However, when immobilized with pectate and alginate gels, the tomato cells retained their AP activities. A new method for the determination of the activity of both extra- and intracellular AP was developed, based on enzyme-catalyzed hydrolysis of a series of synthetic beta-naphthylamides (betaNA) of the L-amino acids Ala, Arg, Leu, Pro, Tyr, or of the synthetic beta-methoxynaphthylamides (betaMNA) of Ala and Arg. Extracellular AP--produced by calli, cell-suspension culture, or seedlings of tomato cells grown on agar--hydrolyzed these peptidic substrates to the free naphthalene amines and amino acids. Staining with Fast Garnet GBC salt under formation of bright reddish azo dyes readily allowed the determination of AP activities. For the tomato-cell suspension, the intracellular activity accounted for 91.3-93.9% of the total activity, and the extracellular one for 6.1-8.7%, respectively. Our method permits the rapid, simple, and specific determination of plant aminopeptidases.

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Decarboxylation of l-tyrosine and l-dopa by immobilized cells of Papaver somniferum

Cited by 14 publications

References 13 publications

β‐Galactosidase in immobilized cells of Daucus carota L.

β‐Galactosidase in immobilized cells of Daucus carota L.

Melibiase in Immobilized Cells of Watermelon

Bioassay for the Determination of the Intra‐ and Extracellular Activity of Aminopeptidases in Immobilized Tomato Cells

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