Abstract
Raffinose family oligosaccharides (RFOs) are mainly containing raffinose and stachyose. They are antinutrient compounds and the major factors responsible for the flatulence upon ingestion of soymilk. α-Galactosidases can hydrolyse RFOs to digestible oligosaccharides. α-Galactosidase was partially purified from watermelon and then immobilized on Sepabeads EC-EP with 56% of activity yield by determined best immobilization conditions. The optimum temperature and pH for both enzymes were found as 65 °C and pH 6.0, respectively. They showed an excellent stability between pH 3.0–7.0 and below 70 °C. The effect of several sugars and metal ions showed that both enzymes affected at different rates. Reusability of the immobilized enzyme with pNPG and raffinose as substrates indicated that the enzyme can be used for a long time with over 50% recovered activity. The enzymatic hydrolysis of the RFOs was realized and HPLC analysis demonstrated that 77.5% and 72.7% of the stachyose and raffinose presented in soymilk is hydrolyzed by the immobilized enzyme during 24 h incubation, respectively. This practical and alternative approach may be a potential to improve the nutritional value of soymilk by eliminating RFOs. Because of its high activity and stability properties the immobilized α-galactosidase may also find several applications in food and feed industries.
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