CROSSLINKING OF MILK PROTEINS BY TRANSGLUTAMINASE: FUNCTIONAL PROPERTIES MODIFICATIONS AND USE IN DAIRY PRODUCTS
DOI:
https://doi.org/10.5380/cep.v26i1.11798Keywords:
TRANSGLUTAMINASE, CASEÍNA, a-LACTOALBUMINA, b-LACTOGLOBULINA, PROPRIEDADES FUNCIONAIS.Abstract
This paper presents a literature review of the main characteristics of a microbial transglutaminase isolated from Streptoverticilium mobaraense, its effects on the functional properties of milk proteins and applications on dairy products. It was demonstrated the principal characteristic of the enzyme and the reactions catalyzed by it, having as outstanding characteristic its behavior in different substrates (caseins and whey proteins) and changes on functional properties of milk proteins after enzymatic reaction. The crosslinking of milk proteins through transglutaminase appears to constitute effective mean to the improvement of physical milk properties of products such as cheeses, milks, ice cream and yogurt.The enzymatic reaction catalyzed by transglutaminase attributes to the formed products unique characteristics and its use has great potential for the food industry. That is because it is considered to be a safe mean of protein modification.
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