EC Number   |
Application |
Reference |
|---|
    3.2.1.23 | analysis |
comparison of commercially available kits to assess water quality and evaluation of their ability to detect Escherichia coli. Chromocult, MI agar, Readycult, and Colilert detect beta-glucuronidase production from respectively 79.9, 79.9, 81.1, and 51.4% of the 74 Escherichia coli strains tested. These four methods detect beta-galactosidase production from respectively 85.1, 73.8, 84.1, and 84.1% of the total coliform strains tested. The high level of false-negative results for Escherichia coli recognition obtained by all four methods suggests that they may not be appropriate for identification of presumptive Escherichia coli strains |
699502 |
| 3.2.1.23 | analysis |
electrophoretic mobility and catalytic activity of individual molecules of enzyme are reproducible for each molecule but different for individual molecules. The observed ranges in electrophoretic motility are similar for different experimental protocols. There is no relationship between the observed activities and electrophoretic motilities |
697603 |
| 3.2.1.23 | analysis |
enzyme can be used as a tool in the structural analysis of D-galactose-containing oligosaccharide chains, as well as for the synthesis of glycoconjugates |
171338 |
| 3.2.1.23 | analysis |
enzyme functions both as a marker, promoting colony color development in the presence of a lactose analogue S-gal, and as a reporter enabling quantitative measurement by a simple colorimetric assay. The combination of BgaB expressed from promoters of varying strength with S-gal produces distinct black colonies in aerobic and anaerobic conditions at temperatures ranging from 37 to 60°C, being an advantage over the conventional beta-galactosidase (LacZ) and substrate X-gal. The system allows for construction and measurement of expression levels of a library in just 4 days |
743998 |
| 3.2.1.23 | analysis |
precise and reliable detection of Escherichia coli strains for differentiation from biochemically and phylogenetically related bacteria. Method is based on polymerase chain reaction, in which four genes coding for lactose permease, cytochrome bd complex, beta-D-glucuronidase, and beta-D-galactosidase, serve as target DNA sequences |
698525 |
| 3.2.1.23 | analysis |
the enzyme is a reliable marker for the course of replicative cell senescence |
677571 |
| 3.2.1.23 | biofuel production |
the saccharification yield of rice straw using Trichoderma reesei cellulase is improved by the addition of MeBglD2. These results show that MeBglD2 can be used to improve plant biomass saccharification, because both substrates and products can activate its enzymatic activity |
749691 |
| 3.2.1.23 | biotechnology |
single enzyme molecule assays performed on the native enzyme as well as recombinant enzyme with and without His-tag reveal significant differences in the average combined turnover numbers indicating that in vivo and in vitro produced enzymes are not identical and the presence of a C-terminal His-tag may alter the activity of beta-galactosidase |
701079 |
| 3.2.1.23 | biotechnology |
the enzyme is suitable for obtaining fermentable sugars from whey wastes |
663632 |
| 3.2.1.23 | degradation |
evaluation of different commercial soluble beta-galactosidases for removal of the residual lactose in crude galactooligosaccharides. Best enzyme tested is lactase NL, with a hydrolytic activity of 286 IU/mg and a half-life of 9 h at 35°C in the presence of 1 mM Mn2+. The best reaction conditions are 35°C, 50% initial carbohydrate concentration and 135 IU/g, leading to 70% reduction of lactose in raw galactooligosaccharides, with an increase of 48% in monosaccharides and of 30% in galactooligosaccharides |
745563 |
