ArticleExtremophiles : life under extreme conditions2019
Purification and characterization of a novel thermophilic β-galactosidase from Picrophilus torridus of potential industrial application.
Article in Extremophiles : life under extreme conditions, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 17 citations in OpenAlex.
- Usage of nanobody-beta-galactosidase fusion in immunoassays and its application in detecting a peanut allergen.Food chemistry. Molecular sciences · 2026Article
- Kinetic and physicochemical modeling of β-galactosidase from Rhynchophorus palmarum larvae.PloS one · 2026Article
- Prebiotic Effects of α- and β-Galactooligosaccharides: The Structure-Function Relation.Molecules (Basel, Switzerland) · 2025Review
- Moderately thermostable GH1 β-glucosidases from hyperacidophilic archaeon Cuniculiplasma divulgatum S5.FEMS microbiology ecology · 2024Article
- Article
- A Review on the Various Sources of β-Galactosidase and Its Lactose Hydrolysis Property.Current microbiology · 2023Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
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Abstract
Intracellular β-galactosidase (E.C 3.2.1.23) produced by the thermoacidophilic archeon Picrophilus torridus DSM 9790 was purified to homogeneity using a combination of DEAE Sepharose, gel filtration, hydroxyapatite and chromatofocusing chromatographies. LC-MS/MS analysis was used to confirm the identity of the purified protein. The enzyme was found to be a homotrimer, with a molecular mass of 157.0 kDa and an isoelectric point of 5.7. To our knowledge, this enzyme has the lowest pH optimum of any intracellular β-galactosidase characterized to date. Maximal activity was exhibited at acidic pH values of 5.0-5.5 and at 70 °C. The enzyme retained > 95% activity after heating to 70 °C for 1 h, or after incubation at pH 5.5 for 1 h. The enzyme may be of interest for high-temperature bioprocessing, such as in the production of lactulose. This investigation suggests that the β-galactosidase activity produced by P. torridus is potentially more useful than several enzymes already characterized for such an application.
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