Biochemical modifications of gliadins induced by microbial transglutaminase on wheat flour

Mazzeo, Maria Fiorella; Bonavita, Roberta; Maurano, Francesco; Bergamo, Paolo; Siciliano, Rosa Anna; Rossi, Mauro

doi:10.1016/j.bbagen.2013.07.021

Cited by 40 publications

(32 citation statements)

References 33 publications

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“…This work is in agreement with Mazzeo et al that three Q sites were modied in the sequence of the 33-mer peptide (displayed in bold, LQLQPFPQPQLPYPQPQLPYPQPQLPYPQPQPF). 20 Moreover, it has been shown that most of the modications by mTG could be explained by mentioned patterns in the previous study that the Q is not a target of mTG in QP and QXXP sequences, while the Q is a target of mTG in the sequences QXP, QXX(FYWMLIV) and QXPF(YWMLIV). 27 Actually, based on this mechanism, three Q modication sites were deduced in the 33-mer peptide, which are displayed in bold (33-mer: LQLQPFPQPQLPYPQP QLPYPQPQLPYPQPQPF).…”

Section: Discussionmentioning

confidence: 91%

“…[16][17][18][19] In addition, recent study highlighted the potential of mTG transamidation to block nonimmune mechanisms related to gluten toxicity. 20 On this basis, it is of interest to study other compounds that might substitute for lysine as acyl-acceptor substrates with the aim of diversifying biocatalytic applications of mTG in the modication of gluten and the breadth of utility as a green biocatalyst in the food industry. In this experiment, it was the aim to investigate the transamidation of the 33-mer peptide using mTG and different acyl-acceptor substrates, namely Llysine (LYS), L-lysine methyl ester (LME), glycine ethyl ester hydrochloride (GEE), 6-aminocaproic acid (6-AA) and hydroxylamine (HA), which have different molecular weights (Fig.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Blocking celiac antigenicity of the glutamine-rich gliadin 33-mer peptide by microbial transglutaminase

Zhou

Cheng

et al. 2017

RSC Adv.

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Section: Discussionmentioning

confidence: 91%

Section: Introductionmentioning

confidence: 99%

Blocking celiac antigenicity of the glutamine-rich gliadin 33-mer peptide by microbial transglutaminase

Zhou

Cheng

et al. 2017

RSC Adv.

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“…and baking performance. For example, glutenin macropolymers (GMP) are believed to make the largest contribution to dough properties and their amount in wheat flour has significantly correlated with dough strength and loaf volume (Mazzeo et al 2013;Steffolani et al 2010). Naturally HMW glutenin subunits are not present in flour and dough as monomers.…”

Section: Introductionmentioning

confidence: 99%

Rheological and functional properties of composite sweet potato – wheat dough as affected by transglutaminase and ascorbic acid

et al. 2015

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Effect of transglutaminase (TGM) and ascorbic acid (AA) on composite sweet potato - wheat dough functional and rheological properties was studied. Partial substitution of wheat flour with sweet potato flour at the level of 20 % significantly (P ≤ 0.05) reduced glutenin, gliadin, dough stability, protein weakening, storage modulus (G') and viscous modulus (G″). Mixolab revealed that both TGM and AA treated dough had stability and protein weakening closed to wheat dough (control), with TGM treated dough having the highest values. TGM Introduced new cross-link bonds as shown by the change of amino acid concentration, leading to an increase in storage modulus (G') and viscous modulus (G″), with G' being higher at all levels of TGM concentration. The opposite was observed for composite dough treated with AA as measured by controlled - stress rheometer. TGM treatment increased glutenin and gliadin content. Compared with the control, dough treated with AA exhibited high molecular weight of polymers than TGM treated dough. The results indicate that the TGM and AA modification of the mixolab and dynamic rheological characteristics (G' and G″) dependent on the changes of GMP, glutenin, gliadin and protein weakening in the composite dough. TGM and AA treatment could improve functional and rheological properties of sweet potato - wheat dough to levels that might be achieved with normal wheat bread. However, it's extremely important to optimize the concentrations of both additives to obtain the optimum response.

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“…In the same year, further delineation of the biochemical modifications of gliadin induced by mTG on wheat flour, was reported [22]. Gliadin and glutenin yields decreased to 7.6±0.5% and 7.5±0.3%, respectively, after a two-step transamidation reaction that produced a water-soluble protein fraction.…”

Section: Mtg As a Potential Therapy For Cd-the Treatmentioning

confidence: 85%

“…One of the dietary strategies is to detoxify and abolish the immunogenicity of the gluten peptides using various probiotic bacteria or isolated enzymes, be it in the bakery or by oral ingestion. Recently, an Italian group from Avellino, presented an interesting and novel approach to detoxify gluten using TG enzymes [20,21,22,23]. Strangely enough, the authors used tTg, the same CD autoantigen that it is logical to inhibit [4,9,24], in vitro, to decrease the immunogenicity of gluten peptides, thus turning swords into plowshares [25].…”

Section: Mtg As a Potential Therapy For Cd-the Treatmentioning

confidence: 99%

Food Industrial Microbial Transglutaminase in Celiac Disease: Treat or Trick

Lerner¹,

Tenbusch²

2016

IJCD

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The surge in incidence of celiac disease (CD) is due more to environmental than to genetic changes. It is paralleled by a food industry that is continuously introducing additives to processed products. Microbial transglutaminase (mTG) is an enzyme that deamidates/transamidates proteins, enabling cross-linkage of molecules and revolutionizing the properties of many food products. It belongs to the family of transaminases and tissue transglutaminase (tTG) has been identified as the autoantigen in CD. Both enzymes de/transamidate gluten, the nutritional environmental factor that induces CD. Although several studies have shown that mTG transamidation of wheat flour/gluten can detoxify gluten peptide in vitro, by inhibiting the response to intestinal gliadin, inducing T cells and reducing INFγ production without influencing their main technological properties, a word of caution is advised. The oral challenge of adult CD patients with mTG transamidated flour was found to be only partially effective, not fulfilling expectations, and there have been multiple recent observations that indicate that mTG transamidated flour/gluten could be dangerous to gluten sensitive populations: mTG cross-linking of gluten may be hazardous in CD since the enzyme can deamidate gluten, thus mimicking endogenous tTG, it can link an extensive repertoire of proteins and other macromolecules with immunogenic potential, mTG treated gluten peptides are immunogenic to celiac patients, inducing specific IgA antibodiesand are recognized by gluten-specific humanT cells. Their effect on CD intestinal permeability has not yet been studied. To better understand the actual processes and events, associated with the suggested mTG therapy, long-term ex vivo and in vitro studies are needed. Until then, it is best to respect the data but suspect the safety of the gluten sensitive populations.

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Biochemical modifications of gliadins induced by microbial transglutaminase on wheat flour

Cited by 40 publications

References 33 publications

Blocking celiac antigenicity of the glutamine-rich gliadin 33-mer peptide by microbial transglutaminase

Blocking celiac antigenicity of the glutamine-rich gliadin 33-mer peptide by microbial transglutaminase

Rheological and functional properties of composite sweet potato – wheat dough as affected by transglutaminase and ascorbic acid

Food Industrial Microbial Transglutaminase in Celiac Disease: Treat or Trick

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