Diamine oxidase from Lens esculenta seedlings: Purification and properties

Floris, Giovanni; Giartosio, Anna; Rinaldi, Augusto

doi:10.1016/0031-9422(83)80004-1

Cited by 75 publications

(33 citation statements)

References 8 publications

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“…Some parameters of functionality and stability of the activated polymer were also calculated and the results are reported in Table 3 and in Figs. 3 and 4, in comparison with those related to the free enzyme found following the kinetic procedures of Moosavi-Nejad et al (2001) and Floris et al (1983).…”

Section: Catalytic Characteristic Of Linked Lsaomentioning

confidence: 62%

“…The pH curves, clearly similar in native and immobilized LSAO, suggest that the linkage between the Floris et al (1983). Fig.…”

Section: Catalytic Characteristic Of Linked Lsaomentioning

confidence: 62%

“…1.4.3.6] from Lens esculenta seedlings (LSAO) was prepared according to Floris et al (1983) and had a specific activity of 110 IU/mg of protein using putrescine as substrate. AO from bovine serum (BSAO) was purified according to Turini et al (1982) with minor modifications and showed a specific activity of 0.28 IU/mg of protein.…”

Section: Reagents Enzymes and Supportsmentioning

confidence: 99%

“…LSAO activity was measured recording the oxygen uptake by a Clark electrode, using 1,4-diaminebutane (putrescine) as substrate as previously reported (Floris et al, 1983).…”

Section: Activity Measurementmentioning

confidence: 99%

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Polyketone polymer: A new support for direct enzyme immobilization

Agostinelli

Belli

Tempera

et al. 2007

Journal of Biotechnology

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Polyketone polymer [ CO CH 2 CH 2 ] n , obtained by copolymerization of ethene and carbon monoxide, is utilized for immobilization of three different enzymes, one peroxidase from horseradish (HRP) and two amine oxidases, from bovine serum (BSAO) and lentil seedlings (LSAO). The easy immobilization procedure is carried out in diluted buffer, at pH 7.0 and 3 • C, gently mixing the proteins with the polymer. No bifunctional reagents and spacer arms are required for the immobilization, which occurs exclusively via a large number of hydrogen bonds between the carbonyl groups of the polymer and the NH groups of the polypeptidic chain. Experiments demonstrate a high linking capacity of polymer for BSAO and an extraordinary strong linkage for LSAO. Moreover, activity measurements demonstrate that immobilized LSAO totally retains the catalytic characteristics of the free enzyme, where only a limited increase of K M value is observed. Finally, the HRP-activated polymer is successfully used as active packed bed of an enzymatic reactor for continuous flow conversion and flow injection analysis of hydrogen peroxide containing solutions.

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Section: Catalytic Characteristic Of Linked Lsaomentioning

confidence: 62%

“…The pH curves, clearly similar in native and immobilized LSAO, suggest that the linkage between the Floris et al (1983). Fig.…”

Section: Catalytic Characteristic Of Linked Lsaomentioning

confidence: 62%

Section: Reagents Enzymes and Supportsmentioning

confidence: 99%

“…LSAO activity was measured recording the oxygen uptake by a Clark electrode, using 1,4-diaminebutane (putrescine) as substrate as previously reported (Floris et al, 1983).…”

Section: Activity Measurementmentioning

confidence: 99%

See 2 more Smart Citations

Polyketone polymer: A new support for direct enzyme immobilization

Agostinelli

Belli

Tempera

et al. 2007

Journal of Biotechnology

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“…Materials LSAO was purified as previously described (Floris et al, 1983). Putrescine (1,4-diaminobutane) and horseradish peroxidase were purchased from the Sigma Chemical Co. (St. Louis, USA).…”

Section: Methodsmentioning

confidence: 99%

Conformational Lock and Dissociative Thermal Inactivation of Lentil Seedling Amine Oxidase

Moosavi-Nejad¹,

Moosavi-Movahedi²,

Rezaei‐Tavirani³

et al. 2003

BMB Reports

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The kinetics of thermal inactivation of copper-containing amine oxidase from lentil seedlings were studied in a 100 mM potassium phosphate buffer, pH 7, using putrescine as the substrate. The temperature range was between 47-60 o C. The thermal inactivation curves were not linear at 52 and 57 o C; three linear phases were shown. The first phase gave some information about the number of dimeric forms of the enzyme that were induced by the higher temperatures using the "conformational lock" pertaining theory to oligomeric enzyme. The "conformational lock" caused two additional dimeric forms of the enzyme when the temperature increased to 57 o C. The second and third phases were interpreted according to a dissociative thermal inactivation model. These phases showed that lentil amine oxidase was reversibly-dissociated before the irreversible thermal inactivation. Although lentil amine oxidase is not a thermostable enzyme, its dimeric structure can form "conformational lock," conferring a structural tolerance to the enzyme against heat stress.

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Analysis of the glycosylation pattern of plant copper amine oxidases by MALDI‐TOF/TOF MS coupled to a manual chromatographic separation of glycans and glycopeptides

et al. 2013

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The N-glycosylation in pea seedling amine oxidase and lentil seedling amine oxidase was analyzed in the present work. For that purpose, the enzymes were purified as native proteins from their natural sources. An enzymatic deglycosylation of pea seedling amine oxidase by endoglycosidase H under denaturing conditions combined with its proteolytic digestion by trypsin was carried out in order to analyze both N-glycans and "trimmed" N-glycopeptides with a residual N-acetylglucosamine attached at the originally occupied N-glycosylation sites. The released N-glycans were subjected to a manual chromatographic purification followed by MALDI-TOF/TOF MS. MS and MS/MS analyses were also performed directly on peptides and N-glycopeptides generated by proteolytic digestion of the studied enzymes. Sequencing of glycopeptides by MALDI-TOF/TOF MS/MS after their separation on a RP using a microgradient chromatographic device clearly demonstrated binding of paucimannose and hybrid N-glycan structures at Asn558. Such carbohydrates have been reported to exist in many plant N-glycoproteins, e.g. in peroxidases. Although high-mannose glycan structures were identified after the enzymatic deglycosylation, they could not be assigned to a particular N-glycosylation site. The presence of unoccupied glycosylation sites in several peptides was also confirmed from MS/MS results.

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Diamine oxidase from Lens esculenta seedlings: Purification and properties

Cited by 75 publications

References 8 publications

Polyketone polymer: A new support for direct enzyme immobilization

Polyketone polymer: A new support for direct enzyme immobilization

Conformational Lock and Dissociative Thermal Inactivation of Lentil Seedling Amine Oxidase

Analysis of the glycosylation pattern of plant copper amine oxidases by MALDI‐TOF/TOF MS coupled to a manual chromatographic separation of glycans and glycopeptides

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