ArticleBMC biotechnology2013
Cloning, overexpression, purification, and characterization of a polyextremophilic β-galactosidase from the Antarctic haloarchaeon Halorubrum lacusprofundi.
Article in BMC biotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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43 citing papers in PubMed, 98 citations in OpenAlex.
- Coordinated proteome-scale remodeling underlies polyextremophilic survival in Antarctic cryo-hypersaline brines.Frontiers in microbiology · 2026Article
- Identification and characterization of a novel β-galactosidase active at low temperatures from the Antarctic fungus Tetracladium sp., expressed in Saccharomyces cerevisiae.Microbial cell factories · 2025Article
- Halophiles and Halotolerants: From Industry to Astrobiology.Current microbiology · 2025Review
- Comprehensive insights on environmental adaptation strategies in Antarctic bacteria and biotechnological applications of cold adapted molecules.Frontiers in microbiology · 2023Review
- Bioactive molecules from haloarchaea: Scope and prospects for industrial and therapeutic applications.Frontiers in microbiology · 2023Review
- Effects of Salinity and Temperature on the Flexibility and Function of a Polyextremophilic Enzyme.International journal of molecular sciences · 2022Article
- Double mutations far from the active site affect cold activity in an Antarctic halophilic β-galactosidase.Protein science : a publication of the Protein Society · 2022Article
- Industrial Biotechnology Based on Enzymes From Extreme Environments.Frontiers in bioengineering and biotechnology · 2022Review
- Biotechnological potential of psychrophilic microorganisms as the source of cold-active enzymes in food processing applications.3 Biotech · 2021Review
- Halophilic archaea and their potential to generate renewable fuels and chemicals.Biotechnology and bioengineering · 2021Review
- Cold-Active β-Galactosidases: Insight into Cold Adaption Mechanisms and Biotechnological Exploitation.Marine drugs · 2021Review
- Identification and characterization of thermophilic amylase producing bacterial isolates from the brick kiln soil.Saudi journal of biological sciences · 2021Article
- Bioprospecting of Novel Extremozymes From Prokaryotes-The Advent of Culture-Independent Methods.Frontiers in microbiology · 2021Review
- Activation of LacZ gene in Escherichia coli DH5α via α-complementation mechanism for β-galactosidase production and its biochemical characterizations.Journal, genetic engineering & biotechnology · 2020Article
- Understanding High-Salt and Cold Adaptation of a Polyextremophilic Enzyme.Microorganisms · 2020Article
- Extremophilic models for astrobiology: haloarchaeal survival strategies and pigments for remote sensing.Extremophiles : life under extreme conditions · 2020Review
- Crystal Structure and Active Site Engineering of a Halophilic γ-Carbonic Anhydrase.Frontiers in microbiology · 2020Article
- Heterologous and Homologous Expression of Proteins from Haloarchaea: Denitrification as Case of Study.International journal of molecular sciences · 2019Review
- Purification and characterization of a novel thermophilic β-galactosidase from Picrophilus torridus of potential industrial application.Extremophiles : life under extreme conditions · 2019Article
- A New β-Galactosidase from the Antarctic Bacterium Alteromonas sp. ANT48 and Its Potential in Formation of Prebiotic Galacto-Oligosaccharides.Marine drugs · 2019Article
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4 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundHalorubrum lacusprofundi is a cold-adapted halophilic archaeon isolated from Deep Lake, a perennially cold and hypersaline lake in Antarctica. Its genome sequencing project was recently completed, providing access to many genes predicted to encode polyextremophilic enzymes active in both extremely high salinity and cold temperatures.
resultsAnalysis of the genome sequence of H. lacusprofundi showed a gene cluster for carbohydrate utilization containing a glycoside hydrolase family 42 β-galactosidase gene, named bga. In order to study the biochemical properties of the β-galactosidase enzyme, the bga gene was PCR amplified, cloned, and expressed in the genetically tractable haloarchaeon Halobacterium sp. NRC-1 under the control of a cold shock protein (cspD2) gene promoter. The recombinant β-galactosidase protein was produced at 20-fold higher levels compared to H. lacusprofundi, purified using gel filtration and hydrophobic interaction chromatography, and identified by SDS-PAGE, LC-MS/MS, and ONPG hydrolysis activity. The purified enzyme was found to be active over a wide temperature range (-5 to 60°C) with an optimum of 50°C, and 10% of its maximum activity at 4°C. The enzyme also exhibited extremely halophilic character, with maximal activity in either 4 M NaCl or KCl. The polyextremophilic β-galactosidase was also stable and active in 10-20% alcohol-aqueous solutions, containing methanol, ethanol, n-butanol, or isoamyl alcohol.
conclusionThe H. lacusprofundi β-galactosidase is a polyextremophilic enzyme active in high salt concentrations and low and high temperature. The enzyme is also active in aqueous-organic mixed solvents, with potential applications in synthetic chemistry. H. lacuprofundi proteins represent a significant biotechnology resource and for developing insights into enzyme catalysis under water limiting conditions. This study provides a system for better understanding how H. lacusprofundi is successful in a perennially cold, hypersaline environment, with relevance to astrobiology.
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