60 species encode β-glucuronidase and β-galactosidase (also known as β-gal).
β-Galactosidase (β-gal) enzymatic activities in lactose metabolism
- Cleaves the disaccharide lactose to undergo transglycosylation and hydrolysis
- Catalyzes the transgalactosylation of lactose to allolactose
- Allolactose can then be cleaved to the monosaccharides galactose and glucose which can then enter glycolysis
Production of β-gal
- β-gal is present in mammals during the breast-feeding period, however β-gal activity decreases after this period
- In humans, this enzyme is abundantly found in colon where it facilitates lactose fermentation, and its activity is measured to indicate the capacity of microbiota of the colon to ferment the intestinal lactose (Jain et al. 2007).
- β-galactosidases have been isolated from various sources such as bacteria, fungi, yeast, vegetables, and recombinant sources
β-gal Use in Food and Supplement Industry
- Manufacture lactose-hydrolyzed lactose-free milk products
- Lactose is hygroscopic and causes crystallization in food products; hence, b-galactosidases are used to hydrolyze lactose to solve lactose-related crystallization in frozen, concentrated desserts.
- b-Galactosidase are used to treat whey to convert it into useful products such as ethanol and sweet syrup that has further wide range of applications in confectionary, bakery, and other industries
- b-galactosidases are also used to solve whey disposal issues on commercial scale
- Production of galacto-oligosaccharides for prebiotics and FOS
β-gal plays a role in estradiol transcriptional activity
- β-gal plays a role in estradiol transcriptional activity, the higher the b-gal activity, the higher the estrogen receptor transcription, transactivation, and signaling
- B-gal activity can be inhibited by the isoflavones genistein and daidzein and the flavone luteolin
60 bacterial genera that encode beta-glucuronidase and beta-galactosidase
| Genus | ß-glucuronidase | ß-galactosidase |
| Bacteroides | + | + |
| Bifidobacterium | + | + |
| Citrobacter | + | + |
| Clostridium | + | + |
| Dermabacter | + | + |
| Escherichia | + | + |
| Faecalibacterium | + | + |
| Lactobacillus | + | + |
| Marvinbryantia | + | + |
| Propionibacterium | + | + |
| Roseburia | + | + |
| Tannerella | + | + |
| Actinomyces | — | + |
| Alistipes | — | + |
| Anaerostipes | — | + |
| Bacteroides | — | + |
| Barnesiella | — | + |
| Bifidobacterium | — | + |
| Blautia | — | + |
| Butyricicoccus | — | + |
| Butyrivibrio | — | + |
| Catenibacterium | — | + |
| Cedecea | — | + |
| Cetobacterium | — | + |
| Citrobacter | — | + |
| Clostridium | — | + |
| Collinsella | — | + |
| Coprobacillus | — | + |
| Coprococcus | — | + |
| Dorea | — | + |
| Dysgonomonas | — | + |
| Enterobacter | — | + |
| Enterococcus | — | + |
| Eubacterium | — | + |
| Fusobacterium | — | + |
| Hafnia | — | + |
| Holdemania | — | + |
| Klebsiella | — | + |
| Lactobacillus | — | + |
| Megamonas | — | + |
| Mitsuokella | — | + |
| Odoribacter | — | + |
| Paenibacillus | — | + |
| Parabacteroides | — | + |
| Paraprevotella | — | + |
| Pediococcus | — | + |
| Porphyromonas | — | + |
| Prevotella | — | + |
| Pseudoflavonifractor | — | + |
| Roseburia | — | + |
| Ruminococcus | — | + |
| Staphylococcus | — | + |
| Streptococcus | — | + |
| Subdoligranulum | — | + |
| Turicibacter | — | + |
| Weissella | — | + |
| Yokenella | — | + |
References
- Juers, D. H., Matthews, B. W., & Huber, R. E. (2012). LacZ β-galactosidase: Structure and function of an enzyme of historical and molecular biological importance. Protein Science, 21(12), 1792–1807. https://doi.org/10.1002/pro.2165
- Kwa, M., Plottel, C. S., Blaser, M. J., & Adams, S. (2016). The Intestinal Microbiome and Estrogen Receptor-Positive Female Breast Cancer. Journal of the National Cancer Institute, 108(8), djw029. https://doi.org/10.1093/jnci/djw029
- Pinto, B., Bertoli. A., Noccioli, C., Garritano, S., Reali, D., & Pistelli, L. (2008). Estradiol-antagonistic activity of phenolic compounds from leguminous plants. Phytotherapy Research, 22(3), 362–366. doi:10.1002/ptr.2327
- Saqib, S., Akram, A., Halim, S. A., & Tassaduq, R. (2017). Sources of β-galactosidase and its applications in food industry. 3 Biotech, 7(1), 79. https://doi.org/10.1007/s13205-017-0645-5
