Визначення взаємодії рецептурних компонентів напівфабрикату збивного борошняного в присутності ферменту трансглютамінази

Abstract

Визначено взаємодію аміногруп лізину з ацильними донорами поліелектролітного комплексу желатинксантан за вмісту ферменту трансглютамінази. Імовірно, під час структуризації розчину желатини і ксантану за температури 50С за вмісту цукру і трансглютамінази відбувається утворення меншої кількості міжмолекулярних водневих зв’язків, ніж за умов проведення процесу без трансглютамінази.

Polyelectrolyte complexes formation mechanism is studied by the IR spectroscopy method, the qualitative assessment of the processes which occur in the studied samples during thermal transformations is carried out. The expediency of combining starch and hydrocolloids of different nature – gelatin and xanthan in combination with the enzyme transglutaminase (TG) during whipped flour semifinished products formation is substantiated; it increases the viscous and elastic properties of the food system. The interaction of lysine amino groups with acyl donors of gelatin-xanthan polyelectrolyte complex under transglutaminase enzyme presence was established. It is probable that during gelatin and xanthan solution structuring at a temperature of 50 °C under sugar and transglutaminase presence, fewer intermolecular hydrogen bonds are formed than when the process is carried out under transglutaminase absence. The TG effect of the flour gelatin-xanthan system on the possible intermolecular hydrogen bonds with flour gluten complex proteins formation and-OH groups binding degree increasing was proved. The TG catalytic effect of gelatin-xanthan system on the lysine amino groups’ interaction with γ-carboxyamide group of glutamine residues bound by peptide bond is proved; it provides higher level of protein skeleton macromolecules crosslinking and can significantly slow down the dehydration process. The obtained results have practical importance for the whipped flour semi-finished product recipe composition formation.