An unconventional immobilization of dextransucrase via entrapment in a
lginate is described, which provides high activity yield and good oper
ational stability. This method is normally restricted to the immobiliz
ation of complete cells or parts of cells. Experiments were designed t
o provide evidence for the immobilization mechanism. It was shown that
a typical globular protein, alpha-chymotrypsin, is neither immobilize
d in an alginate matrix nor by formation of an additional network of d
extran inside alginate. The results suggest that dextransucrase immobi
lization in alginate is due to a unique supramolecular structure.