Enzymatic hydrolysis of raffinose family oligosaccharides
(RFOs),
mainly raffinose and stachyose, into digestible sugars improves the
nutritional value of soybean and soymilk. α-Galactosidases have
been widely employed for the degradation of RFOs in industrial food
applications. In the present study, α-galactosidase was immobilized
on Sepabeads EC-EA and Sepabeads EC-HA by direct covalent attachment
and also by adsorbtion/crosslinking methods by using glutaraldehyde
chemistry. The covalently immobilized enzyme on Sepabeads EC-HA completely
hydrolyzed both raffinose and stachyose for 24 h. The adsorbed/crosslinked
enzyme on Sepabeads EC-HA hydrolyzed the stachyose and raffinose with
100 and 88.6% degrees at the same time, respectively. The results
suggested that the covalently immobilized enzyme on Sepabeads EC-HA
is more efficient in the degradation of RFOs. Therefore, this form
of enzyme may be a good candidate for removing of RFOs found in many
products of the food industry.