Transglutaminase crosslinking of different protein based foods 2

A tale of bugs and foods: Hwp1 versus...

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BELOW MY HYPOTHESIS:
A tale of bugs and foods: Hwp1 versus...

BELOW AN ABSTRACT OF THE CROSSLINKING OF PROTEINS BY MICROBIAL TRANSGLUTAMINASES:
Transglutaminase crosslinking of different protein-based foods

TGases  have  been  identified  in  many  different  of  taxonomic groups,  including  microorganisms, plants, invertebrates, and mammals (Rachel 2013).

In  nature,  transglutaminases  catalyze  the  formation  of  amide bonds  between proteins  to  form  insoluble  protein  aggregates (Rachel 2013).

Transglutaminase is an enzyme that catalyses the formation of isopeptide bonds between proteins  (Kieliszek 2014)

In commercial food processing, transglutaminase is used to bond proteins together (Wikipedia 2015)

Transglutaminase is produced by Streptoverticillium mobaraense fermentation in commercial quantities or extracted from animal blood (Wikipedia 2015)

The extremely high costs of manufacturing transglutaminase from animal origin have prompted scientists to search for new sources of this enzyme (Kieliszek 2014)

Interdisciplinary efforts have been aimed at producing enzymes synthesised by microorganisms which may have a wider scope of use (Kieliszek 2014)

In 1989, microbial transglutaminase was isolated from Streptoverticillium sp. Its characterisation indicated that this isoform could be extremely useful as a biotechnological tool in the food industry (Kieliszek 2014)

Microbial transglutaminase is an important enzyme in food processing for improving protein properties by catalyzing the cross-linking of proteins (Zhang 2010).

Transglutaminase is also widely used in the meat industry, mainly in the manufacture of restructured meat (Kuraishi et al. 1997).

Microbial transglutaminase is  commonly  employed  as  a  tool  in  the  food  industry  to catalyze  the  cross-linking  of  meat,  soy,  and  wheat  proteins  to  improve  and  modify  their  texture  and
tensile  properties (Rcahel 2013).

It is notable that gluten pretreated with microbial transglutaminase and an amine donor prior to TG2 treatment induces less IFN-γ production by celiac patient biopsy-derived intestinal T cells relative to gluten receiving no pretreatment. This suggests that the specificities of these enzymes (Human Tissue transglutaminase and microbial transglutaminase) do indeed overlap to some extent (Bethune 2008).


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