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Some properties of a β‐galactosidase from an extremely thermophilic bacterium
Author(s) -
Cowan D. A.,
Daniel R. M.,
Martin A. M.,
Morgan H. W.
Publication year - 1984
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260261002
Subject(s) - thermophile , thermus aquaticus , thermus , reagent , chemistry , bacteria , strain (injury) , product inhibition , biochemistry , enzyme , biology , organic chemistry , non competitive inhibition , anatomy , genetics
An inducible β‐galactosidase from an extremely thermophilic organism, Thermus strain 4−1A, has been isolated and partially purified. There were significant dissimilarities to T. aquaticus β‐galactosidase. It had a pl of 4.5, was inhibited by sulphydryl inhibitors and a number of transition metals, and was activated by EDTA and SH‐containing reagents. The β‐galactosidase showed strong product inhibition, and weaker inhibition by some other mono‐ and disaccharides. It was very stable up to 90°C at pH 8. On immobilization by diazonium linkage to porous glass, the pH optimum (6.0), the K M with ONPG (5m M ) and the product inhibition were not altered.