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Properties of a thermostable β‐galactosidase from a thermophilic Bacillus : Comparison of the enzyme activity of whole cells, purified enzyme and immobilised whole cells
Author(s) -
Griffiths Mansel W.,
Muir D. Donald
Publication year - 1978
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740290904
Subject(s) - thermostability , enzyme , thermophile , enzyme assay , chemistry , biochemistry , bacillus (shape) , chromatography , specific activity , immobilized enzyme , biology , microbiology and biotechnology
The properties of a β‐galactosidase from a thermophilic Bacillus have been studied and compared with the properties of the enzyme contained in whole cells and in cells entrapped in a polyacrylamide gel matrix. The partially purified enzyme appears to be optimally active at a temperature of 60°C and pH 6.0. The enzyme activities from whole cells and immobilised whole cells have slightly different temperature optima (being 75 and 65°C respectively) and pH optima (being 6.2 and 6.6 respectively). The enzyme activity from whole cells is significantly more thermostable than that of the partially purified enzyme; the half‐lives being 125 and 22 min respectively at 70°C. In other properties studied, the enzyme activities of the three sources are similar. The thermostability of the enzyme and the broad pH range over which it is active makes this enzyme suitable for use in the dairy industry.