Immobilization of isoamylase on carboxymethyl-cellulose and chitin |
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Authors: | Hwai-Shen Liu Wei-Hsu Chen Jinn-Tsyy Lai |
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Affiliation: | (1) Department of Chemical Engineering, National Taiwan University, Taipei, Taiwan, ROC |
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Abstract: | Isoamylase, a starch debranching enzyme capable of hydrolyzing α-1,6-glucosidic linkage, was immobilized on CM-cellulose and chitin. The immobilization on chemically modified CM-cellulose (CM-cellulose azide) resulted in a specific activity of 1422 U/g-CMCI (CM-celluloseisoamylase), 24% activity retention, and an optimal pH of 4.0. The immobilization of isoamylase on glutaraldehyde treated chitin gave 1638 U/g-CI (chitin-isoamylase), 46% activity retention, and an optimal pH of 2.4. The kinetic data (K m) indicated that CI (0.69 g/L) has similar mass transfer resistance to free enzyme (0.67 g/L), whereas CMCI (3.57 g/L) has much greater transport resistance. |
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Keywords: | Isoamylase CM-cellulose chitin immobilization kinetics |
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