Pea Seedling Histaminase as a Novel Therapeutic Approach to Anaphylactic and Inflammatory Disorders

Masini, Emanuela; Bani, Danièle; Marzocca, Cosimo; Mateescu, Mircea Alexandru; Mannaioni, P. F.; Federico, Rodolfo; Mondovı̀, Bruno

doi:10.1100/tsw.2007.139

Cited by 14 publications

(10 citation statements)

References 70 publications

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“…It is worth highlighting that the DAO activity of both products showed minimal variation among different production batches. These results are in good agreement with previously published data indicating a higher catalytic turnover rate for plant-than animal-derived DAO [5,23,37].…”

Section: Suitability Of the Methods For The Determination Of Dao Activsupporting

confidence: 93%

“…DAO (EC 1. 4.3.22), which belongs to the category of copper-containing amine oxidases, is a homodimeric and ubiquitous enzyme found in microorganisms, plants and animals, generally in the range of 140 to 200 kDa [4][5][6][7][8]. In particular, DAO catalyzes the oxidative deamination of the primary amino group of histamine to imidazole acetaldehyde, consuming dioxygen with the concomitant release of stoichiometric amounts of ammonia and hydrogen peroxide ( Figure 1) [9,10].…”

Section: Introductionmentioning

confidence: 99%

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In vitro determination of diamine oxidase activity in food matrices by an enzymatic assay coupled to UHPLC-FL

et al. 2019

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Intestinal diamine oxidase (DAO) acts as a protective barrier against exogenous histamine. A deficit of DAO activity can lead to the appearance of histamine intolerance, a clinical condition that may be treated by a low-histamine diet and oral DAO supplementation to enhance intestinal histamine degradation. As sources of DAO, porcine kidneys and certain legume seedlings are suitable components for the formulation of a DAO supplement. The aim of this work was to develop a rapid and reliable methodology for the in vitro determination of DAO activity in food matrices based on an enzymatic assay coupled to UHPLC-FL. The proposed method showed a satisfactory linearity and sensitivity and provided a relative standard deviation lower than 3%, guaranteeing method precision, and a mean recovery greater than 99% both for lyophilized pea sprouts and porcine kidney protein extracts. A high specificity is a key attribute of this method due to the use of histamine as the reaction substrate and the direct quantification of its degradation. Moreover, the lack of interference of catalase and hydrogen peroxide is another advantage in comparison with previously published methods. Lyophilized pea sprouts showed the greatest histamine-degrading activity (0.40 ±0.01 mU/mg), followed by porcine kidney protein extracts (0.23 ±0.01 mU/mg) and commercial DAO supplements (0.09 ±0.06 mU/mg). This technique could be used as a tool to validate the DAO activity of food matrices of potential interest for the treatment of histamine intolerance.

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Section: Suitability Of the Methods For The Determination Of Dao Activsupporting

confidence: 93%

Section: Introductionmentioning

confidence: 99%

In vitro determination of diamine oxidase activity in food matrices by an enzymatic assay coupled to UHPLC-FL

et al. 2019

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“…A higher catalytic capacity of DAO enzymes of plant origin in degrading certain amino substrates has been described by some authors in comparison with those of animal origin [ 129 , 135 , 136 , 137 ]. Specifically, the germinated sprouts of certain edible legumes have been pointed out as interesting sources of DAO enzyme.…”

Section: Histamine Intolerancementioning

confidence: 99%

Histamine Intolerance: The Current State of the Art

et al. 2020

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Histamine intolerance, also referred to as enteral histaminosis or sensitivity to dietary histamine, is a disorder associated with an impaired ability to metabolize ingested histamine that was described at the beginning of the 21st century. Although interest in histamine intolerance has considerably grown in recent years, more scientific evidence is still required to help define, diagnose and clinically manage this condition. This article will provide an updated review on histamine intolerance, mainly focusing on its etiology and the existing diagnostic and treatment strategies. In this work, a glance on histamine intoxication will also be provided, as well as the analysis of some uncertainties historically associated to histamine intoxication outbreaks that may be better explained by the existence of interindividual susceptibility to ingested histamine.

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“…Plant copper‐containing amines oxidases have been a point of interest in therapeutic studies because other copper oxidases such as ceruloplasmin and bovine serum amine oxidases have been shown to possess antioxidant , cardioprotective , and even antitumoral properties . It has also been suggested that pea seedling DAO can reveal an antioxidant‐like protection by reducing tissue damage induced by reactive oxygen species generated during the anaphylactic reaction . Furthermore, pea seedling DAO was found to counteract cardiac anaphylaxis and pulmonary asthma‐like reaction to aerosolized allergens in sensitized guinea pigs by an antioxidant activity and inactivation of endogenously released histamine .…”

Section: Introductionmentioning

confidence: 99%

Carboxymethyl starch/alginate microspheres containing diamine oxidase for intestinal targeting

Blémur

Marcocci

et al. 2015

Biotech and App Biochem

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The association of carboxymethyl starch (CMS) and alginate is proposed as a novel matrix for the entrapment of bioactive agents in microspheres affording their protection against gastrointestinal degradation. In this study, the enzyme diamine oxidase (DAO) from white pea (Lathyrus sativus) was immobilized by inclusion in microspheres formed by ionotropic gelation of CMS/alginate by complexation with Ca2+. The association of CMS to alginate generated a more compact structure presenting a lesser porosity, thus decreasing the access of gastric fluid inside the microspheres and preventing the loss of entrapped enzyme. Moreover, the immobilized enzyme remained active and was able to oxidize the polyamine substrates even in the presence of degrading proteases of pancreatin. The inclusion yield in terms of entrapped protein was of about 82%–95%. The DAO entrapped in calcium CMS/alginate beads retained up to 70% of its initial activity in simulated gastric fluid (pH 2.0). In simulated intestinal fluid (pH 7.2) with pancreatin, an overall retention of 65% of activity for the immobilized DAO was observed over 24 H, whereas in similar conditions the free enzyme was totally inactivated. Our project proposes the vegetal DAO as an antihistaminic agent orally administered to treat food histaminosis and colon inflammation.

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Pea Seedling Histaminase as a Novel Therapeutic Approach to Anaphylactic and Inflammatory Disorders

Cited by 14 publications

References 70 publications

In vitro determination of diamine oxidase activity in food matrices by an enzymatic assay coupled to UHPLC-FL

In vitro determination of diamine oxidase activity in food matrices by an enzymatic assay coupled to UHPLC-FL

Histamine Intolerance: The Current State of the Art

Carboxymethyl starch/alginate microspheres containing diamine oxidase for intestinal targeting

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