We examined the effects of encapsulation on the stability of a proteolytic enzyme trypsin to different combinations of pH and temperature. For encapsulation, we used alginate and lipids, two types of natural, biodegradable polymers. In the first part of this study we focused on the encapsulation of trypsin into alginate microbeads. By varying the parameters of the encapsulation process we were looking to achieve as high encapsulation efficiency as possible. Using alginate we achieved between 1,3 and 2,9 % efficiency, which is far too low for any research or industrial application. As a result of low encapsulation efficiency, we did not evaluate the effect on encapsulation in alginate on the stability of trypsin. In the second stage our research was focused on encapsulation of trypsin into liposomes, where we achieved 54 % encapsulation efficiency. We exposed the prepared samples of encapsulated trypsin to various combinations of pH (7.0 and 9.0) and temperatures (4, 25 and 37 °C). To evaluate the effect of encapsulation on the stability of trypsin, we prepared samples of free enzyme in the same manner. We observed an increase in stability of encapsulated trypsin at temperatures of 4 and 25 °C at both pH values. This effect was not observed with the samples incubated at 37 °C, i.e. the effect was negligible.
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