Effects on the hydrolysis of native starch and glycogen by a thermostable α-amylase after immobilization on solid supports

Abstract

A thermostable α-amylase was immobilized on controlled-pore glass beads and contained in enzyme reactors. The optimization of the hydrolytic effect of the immobilized enzyme on glycogen and native starch as substrates was investigated. A pore size of the controlled-pore glass support of about 1489 Å was found to be optimum. The optimum pH was 6.0 for hydrolysis of the substrates. Complete hydrolysis of the substrates to glucose could be accomplished on-line at ambient temperature after passage of a sample through one immobilized α-amylase reactor at pH 6.0 and then through one immobilized amyloglucosidase reactor at pH 4.6.