Toxicological Evaluation for Food Applications of Transglutaminase from a Newly Isolated Bacillus circulans BL32

Souza, Cláucia Fernanda Volken de; Venzke, Janaína Guimarães; Rosa, Renato Moreira; Henriques, José; Dallegrave, Eliane; Flôres, Simone Hickmann; Ayub, Marco Antônio Záchia

doi:10.3923/ajft.2011.460.471

Cited by 2 publications

(1 citation statement)

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“…None of the samples analyzed in this study exhibited spleen cell cytotoxicity after a 72 h-culture ( Figure 5 ), indicating that the inhibitory effects on cytokine release caused by TG were due to a lower reactivity of the cross-linked proteins. Other in vivo and in vitro studies of toxicity of microbial TG have revealed safety concerns about its food applications [ 34 ] and therefore more research is need in this regard.…”

Section: Resultsmentioning

confidence: 99%

IgE-Binding and Immunostimulating Properties of Enzymatic Crosslinked Milk Proteins as Influenced by Food Matrix and Digestibility

et al. 2022

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Dairy foods are essential in the diet, although in some susceptible individuals they may cause allergy to cow’s milk proteins. Therefore, alternative methods are sought to reduce their allergenicity. Transglutaminase (TG) is widely used in dairy products mainly to improve texture. Although it has been claimed that TG can be used to modify the digestibility and allergenicity of foods, its impact within a real matrix has been rarely studied. The aim of this work was to assess the allergenic potential of crosslinked skim milk (SM), milk casein fraction (CN), and whey protein (WP). To this purpose, inhibition ELISA with sera from milk allergic patients, in vitro activation tests of mouse mast cells and splenocytes, and simulated gastrointestinal digestion assays were performed. The results showed that cross-linking increased the binding of IgE to WP, but decreased IgE-binding to SM and CN. However, no differences were observed in the ability of cross-linked proteins to induce mast cell degranulation compared to native proteins. The cross-linking of SM and CN reduced Th2 cytokine release from the splenocytes of sensitized mice. All TG-treated samples exhibited more resistance to in vitro digestion than the untreated proteins and the human IgE binding capacity after digestion was higher. In conclusion, TG treatment of milk proteins does not reduce the risk of eliciting allergic symptoms in cow’s milk allergic patients.

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Section: Resultsmentioning

confidence: 99%