Authors

The use of transglutaminase in milk processing

UDC 577+637

The use of transglutaminase in milk processing

Shleykin A.G., Danilov N.P.

Abstract
This review summarizes data on enzyme technology in milk processing and its prospects. Transglutaminase properties are shown to differ in its relation to milk proteins compared with other proteins. Transglutaminase is shown to be active when pH is from 5 to 8, 7 being the optimum one. The enzyme is proved to be stable when the temperature is below 40 deg C and to be inactivated when the temperature is above 65 deg C. Substrate specificity of transglutaminase to protein is considered. Casein, sodium caseinate, gelatine, myosin, 11S and 7S soya beans globulin are shown to be the best substrates for transglutaminase. Collagen, whey gliadin and glutenin, egg yolk protein are good substrates also. Actin is not usually bound by transglutaminase. The conditions of enzyme binding of whey protein with wheat gluten are considered. When stored for 6 weeks at 4 deg C yogurts made from enzyme processed milk do not change their rheological properties and protein polymerization degree. When whey is incubated by transglutaminase, reducing residual concentration of soluble proteins is proved by electrophoresis and gel chromatography. The binding of gluten with whey proteins results in gluten immune activity lowering and may be used for the production of celiac disorder patients’ food.

Keywords: transglutaminase, casein, gluten, whey protein, milk processing

All references

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