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ABSTRACT
The enzymatic activity and temperature optima of ƒÒ-Galactosidase from Escherichia coli with its substrate, ƒß-nitrophenol-ƒÒ-D-Galactopyranoside, were investigated. Samples of ƒß-nitrophenol-ƒÒ-D-Galactopyranoside were added to ƒÒ-Galactosidase in the presence of a pH 7. ... The ƒÒ-Galactosidase samples held at 37¢XC had the highest level of activity compared to the 10¢XC, 25¢XC, 45¢XC, and 60¢XC samples. ... Thus, such research concerning temperature optima of enzymes is essential, since enzymatic activity is dependent on the environment of the enzyme.
INTRODUCTION
ƒÒ-Galactosidase from Escherichia coli hydrolyzes lactose and other ƒÒ-Galactosides into monosaccharides (Douglas H. ... , 2000), and has therefore recently evoked considerable interest because of its applications in the food industry, nutrition, and medicine (Nagy Z. ... (2000), the enzyme, when incubated at the original pH and under optimum temperature conditions, showed potential for several industrial applications, such as the removal of 67% of lactose from milk and 84% of lactose from milk whey.
Approximate Word count = 660
Approximate Pages = 2.6
(250 words per page double spaced)
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