Protein Cross‐linking in Food – Structure, Applications, Implications for Health and Food Safety

Gerrard, Juliet A.; Cottam, J.

doi:10.1002/9781118308035.ch10

Cited by 6 publications

(5 citation statements)

References 172 publications

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“…"Therefore, mTg can enhance the immunogenicity of gluten and should not be used in food products intended for consumption by CD patients" [46]. In fact, the worries and warnings on safe usage of the industrial enzyme exist in multiple publications [9][10][11][12][13][14]25,28,29,43,46,[111][112][113][114]. Notably, in some European countries like Switzerland and Germany, or in Canada, the public was notified of potential public safety concerns, and recommended labeling the enzyme on the final product [115,116].…”

Section: Warnings For Use Of Microbial Transglutaminasementioning

confidence: 99%

Microbial Transglutaminase Is a Very Frequently Used Food Additive and Is a Potential Inducer of Autoimmune/Neurodegenerative Diseases

Lerner

Benzvi

2021

Toxics

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Microbial transglutaminase (mTG) is a heavily used food additive and its industrial transamidated complexes usage is rising rapidly. It was classified as a processing aid and was granted the GRAS (generally recognized as safe) definition, thus escaping full and thorough toxic and safety evaluations. Despite the manufacturers claims, mTG or its cross-linked compounds are immunogenic, pathogenic, proinflammatory, allergenic and toxic, and pose a risk to public health. The enzyme is a member of the transglutaminase family and imitates the posttranslational modification of gluten, by the tissue transglutaminase, which is the autoantigen of celiac disease. The deamidated and transamidated gliadin peptides lose their tolerance and induce the gluten enteropathy. Microbial transglutaminase and its complexes increase intestinal permeability, suppresses enteric protective pathways, enhances microbial growth and gliadin peptide’s epithelial uptake and can transcytose intra-enterocytically to face the sub-epithelial immune cells. The present review updates on the potentially detrimental side effects of mTG, aiming to interest the scientific community, induce food regulatory authorities’ debates on its safety, and protect the public from the mTG unwanted effects.

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Section: Warnings For Use Of Microbial Transglutaminasementioning

confidence: 99%

Microbial Transglutaminase Is a Very Frequently Used Food Additive and Is a Potential Inducer of Autoimmune/Neurodegenerative Diseases

Lerner

Benzvi

2021

Toxics

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“…TGase has been extensively investigated in meat (Marques et al, 2010), plant (Dube et al, 2007) and dairy (Huppertz, 2009;Jaros et al, 2006a;Loveday et al, 2013) protein applications. In addition to TGase, which is a transferase, oxidative enzymes such as tyrosinases, laccases, peroxidases, and sulphydryl oxidases (SOXs) have also been shown to have the ability to introduce covalent cross-links between/within proteins with or without use of auxiliary substances (see recent reviews by Buchert et al, 2007Buchert et al, , 2010Gerrard and Cottam, 2012;Heck et al, 2013;Huppertz, 2009;Zeeb et al, 2014). TGase is currently used for protein cross-linking in industrial production of various food commodities for improved product texture, stability and overall profitability.…”

Section: Enzymatic Cross-linking Of Proteinsmentioning

confidence: 99%

Enzymatic modification of dairy product texture

Ercili-Cura

Huppertz

Kelly

2015

Modifying Food Texture

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“…The ongoing introduction of innovative processing technologies designed to produce affordable, safe and healthy foods has prompted studies focused on revealing protein modifications in treated products (Arena et al, 2014; Hellwig & Henle, 2014; Scaloni, 2020; Van Lancker et al, 2011). Within this context, a detailed molecular description of cross‐linked proteins in foods in keeping with modern chemistry standards is mandatory with the aim to characterize their nature before processing, but also to assess any structural changes after technological treatments, to evaluate corresponding nutritional/nutraceutical properties and any toxic effects (Gerrard & Cottam, 2012). This information is also essential for digestion models to gain an understanding of food protein breakdown dynamics and assimilation.…”

Section: Introductionmentioning

confidence: 99%

Cross‐linking reactions in food proteins and proteomic approaches for their detection

Renzone

Arena

Scaloni

2021

Mass Spectrometry Reviews

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Various protein cross‐linking reactions leading to molecular polymerization and covalent aggregates have been described in processed foods. They are an undesired side effect of processes designed to reduce bacterial load, extend shelf life, and modify technological properties, as well as being an expected result of treatments designed to modify raw material texture and function. Although the formation of these products is known to affect the sensory and technological properties of foods, the corresponding cross‐linking reactions and resulting protein polymers have not yet undergone detailed molecular characterization. This is essential for describing how their generation can be related to food processing conditions and quality parameters. Due to the complex structure of cross‐linked species, bottom‐up proteomic procedures developed to characterize various amino acid modifications associated with food processing conditions currently offer a limited molecular description of bridged peptide structures. Recent progress in cross‐linking mass spectrometry for the topological characterization of protein complexes has facilitated the development of various proteomic methods and bioinformatic tools for unveiling bridged species, which can now also be used for the detailed molecular characterization of polymeric cross‐linked products in processed foods. We here examine their benefits and limitations in terms of evaluating cross‐linked food proteins and propose future scenarios for application in foodomics. They offer potential for understanding the protein cross‐linking formation mechanisms in processed foods, and how the inherent beneficial properties of treated foodstuffs can be preserved or enhanced.

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Protein Cross‐linking in Food – Structure, Applications, Implications for Health and Food Safety

Cited by 6 publications

References 172 publications

Microbial Transglutaminase Is a Very Frequently Used Food Additive and Is a Potential Inducer of Autoimmune/Neurodegenerative Diseases

Microbial Transglutaminase Is a Very Frequently Used Food Additive and Is a Potential Inducer of Autoimmune/Neurodegenerative Diseases

Enzymatic modification of dairy product texture

Cross‐linking reactions in food proteins and proteomic approaches for their detection

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