Immobilization of Thermostable α-Galactosidase from Pycnoporus cinnabarinus on Chitosan Beads and Its Application to the Hydrolysis of Raffinose in Beet Sugar Molasses
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概要
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α-Galactosidase (EC 3.2.1.22) from Pycnoporus cinnabarinus was immobilized on chitosan beads, BCW 1000,and crosslinked chitosan beads, BCW 3000 and 3500,of three different sizes, which were untreated or previously treated with glutaraldehyde. The activity yields of the immobilized enzymes were between 25 to 45%, except for glutaraldehyde-untreated BCW 1000. Leakage of the enzyme with increasing ionic strength was observed in glutaraldehyde-untreated BCW 1000 and 3000. The α-galactosidases immobilized on glutaraldehyde-treated BCW 3000 and 3500 were active at pH 3-6 and at 70-80℃, and stable between pH 3 and 9,and below 70℃. The immobilized α-galactosidase was continuously used for 30 days to hydrolyze raffinose in beet sugar molasses.
- 1987-08-25
著者
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Mitsutomi Masaru
Department Of Agricultural Chemistry Faculty Of Agriculture Saga University
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Ohtakara Akira
Department Of Agricultural Chemistry Faculty Of Agriculture Saga University
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