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A Thermostable Acid α‐Glucosidase from Tetrahymena thermophila: Purification and Characterization
Author(s) -
BANNO YOSHIKO,
SASAKI NOBORU,
YOSHINO TIKAKO,
MOCHIZUKI JUNICHIROH,
HIRATA HAJIME,
NOZAWA YOSHINORI
Publication year - 1989
Publication title -
the journal of protozoology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 0022-3921
DOI - 10.1111/j.1550-7408.1989.tb01097.x
Subject(s) - tetrahymena , chemistry , biochemistry , biology
An acid α‐glucosidase (EC 3.2.1.20) was purified to homogeneity from the culture medium of Tetrahymena thermophila CU 399. Its general molecular, catalytic and immunological properties were compared to those of the T. pyriformis W enzyme. The enzyme from T. thermophila was a 105‐kD monomer and the N‐terminus (25 amino acid residues) displayed some homology with that of T. pyriformis enzyme. The purified enzyme was most active at 56° C and showed resistance to thermal inactivation. The acid α‐glucosidase appears to have α‐1,6‐glucosidase as well as α‐1,4‐glucosidase activity. The Km values determined with p‐nitrophenyl‐α‐glucopyranoside, maltose, isomaltose and glycogen were 0.7 mM, 2.5 mM, 28.5 mM and 18.5 mg/ml, respectively. The enzyme was antigenically distinct from T. pyriformis acid α‐glucosidase.