Microencapsulation of a Commercial Food-Grade Protease by Spray Drying in Cross-Linked Chitosan Particles

In this study, the use of spray-drying technology for encapsulating Flavourzyme (R) (protease-peptidase complex) was evaluated to overcome the limitations (low encapsulation efficiency and no large-scale production) of other encapsulation processes. To the best of our knowledge, spray drying has not been applied previously for the immobilization of this enzyme. Firstly, bovine serum albumin (BSA), as a model protein, was encapsulated by spray drying in chitosan and tripolyphoshate (TPP) cross-linked-chitosan shell matrices. The results showed that the chitosan-TPP microcapsules provided a high encapsulation efficiency and better protein stability compared to the non-crosslinked chitosan microcapsules. The effect of enzyme concentration and drying temperature were tested during the spray drying of Flavourzyme (R). In this regard, an activity yield of 88.0% and encapsulation efficiency of 78.6% were obtained with a concentration of 0.1% (v/v) and an inlet temperature of 130 degrees C. Flavourzyme (R)-loaded chitosan microcapsules were also characterized in terms of their size and morphology using scanning electron microscopy and laser diffractometry.

Automated summary

This study evaluated the use of spray-drying technology for encapsulating Flavourzyme (R) and found that it provided a more efficient encapsulation method compared to other processes. The study also compared the effect of different cross-linking agents on the encapsulation efficiency and stability of the microcapsules. The results showed that chitosan-TPP microcapsules had higher encapsulation efficiency and protein stability.