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Immobilization of thermostable alpha galactosidase from pycnoporus cinnabarinus on chitosan beads and its application to the hydrolysis of raffinose in beet sugar molasses

Ohtakara, A.; Mitsutomi, M.

Journal of Fermentation Technology 65(4): 493-498

1987


Accession: 005620574

.alpha.-Galactosidase (EC 3.2.1.22) Pycnoporus cinnabarinus was immbolized 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 .alpha.-galactosidases immobilized on glutaraldehyde-treated BCW 3000 and 3500 were active at pH 3-6 and at 70-80.degree. C, and stable between pH 3 and 9, and below 70.degree. C. The immobilized .alpha.-galactosidase was continuously used for 30 days to hydrolyze raffinose in beet sugar molasses.

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