Abstract
A thermostable β-galactosidase (EC 3.2.1.23) from a thermophilic anaerobe, strain NA10, was purified from the crude extract of the Escherichia coli transformant harboring the lacN gene. The purified enzyme was physically and covalently immobilized to a porous ceramic support, SM-10. Among the supports tested, the highest residual activity after 3 h incubation at 70° C was obtained when the enzyme was covalently immobilized to silanized SM-10 with 3-[2-(2-amino-ethylaminoethylamino)propyl]trimethoxysilane. The amount of the enzyme immobilized was about 60 mg/g of this support. The enzymatic properties were almost the same as those of the free enzyme. The half-life of this immobilized enzyme was estimated to be approximately 450 h at the pasteurization temperature (65° C).
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On leave from Aichi Institute of Technology, Yakusa-cho, Toyota 470-03, Japan
Correspondence to: T. Saito
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Saito, T., Yoshida, Y., Kawashima, K. et al. Immobilization and characterization of a thermostable β-galactosidase from a thermophilic anaerobe on a porous ceramic support. Appl Microbiol Biotechnol 40, 618–621 (1994). https://doi.org/10.1007/BF00173317
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DOI: https://doi.org/10.1007/BF00173317