ArticleExtremophiles : life under extreme conditions2017
Characterization of two novel heat-active α-galactosidases from thermophilic bacteria.
Article in Extremophiles : life under extreme conditions, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 27 citations in OpenAlex.
- Biodegradation of sugarcane bagasse biomass using recombinant alpha-galactosidase overexpressing whole-cell3 Biotech · 2024Article
- Activity-based metaproteomics driven discovery and enzymological characterization of potential α-galactosidases in the mouse gut microbiome.Communications chemistry · 2024Article
- Mining thermophiles for biotechnologically relevant enzymes: evaluating the potential of European and Caucasian hot springs.Extremophiles : life under extreme conditions · 2023Review
- Raffinose Family Oligosaccharides: Friend or Foe for Human and Plant Health?Frontiers in plant science · 2022Review
- Chemical and nutritional characteristics, and microbial degradation of rapeseed meal recalcitrant carbohydrates: A review.Frontiers in nutrition · 2022Review
- Identification and Characterization of a Thermostable GH36 α-Galactosidase fromInternational journal of molecular sciences · 2021Article
- β-Galactosidases from a Sequence-Based Metagenome: Cloning, Expression, Purification and Characterization.Microorganisms · 2020Article
- Optimization of Saccharomyces cerevisiae α-galactosidase production and application in the degradation of raffinose family oligosaccharides.Microbial cell factories · 2019Article
- Multidisciplinary involvement and potential of thermophiles.Folia microbiologica · 2019Review
- Galactomannan degradation by thermophilic enzymes: a hot topic for biotechnological applications.World journal of microbiology & biotechnology · 2019Review
- International Conference on Extremophiles 2016.Extremophiles : life under extreme conditions · 2017Article
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Authors and funding
5 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Two genes (agal1 and agal2) encoding α-galactosidases were identified by sequence-based screening approaches. The gene agal1 was identified from a data set of a sequenced hot spring metagenome, and the deduced amino-acid sequence exhibited 99% identity to an α-galactosidase from the thermophilic bacterium Dictyoglomus thermophilum. The gene agal2 was identified from the whole genome sequence of the thermophile Meiothermus ruber. The amino-acid sequences exhibited structural motifs typical for glycoside hydrolase (GH) family 36 members and were also differentiated into different subgroups of this family. Recombinant production of the heat-active GH36b enzyme Agal1 (87 kDa) and GH36bt enzyme Agal2 (57 kDa) was carried out in E. coli. Agal1 exhibited a specific activity of 1502.3 U/mg at 80 °C, pH 6.5, and Agal2 225.4 U/mg at 60-70 °C, pH 6.5. Half-lives of 14 h (Agal1) and 39 h (Agal2) were obtained at 50 °C, and Agal1 showed half-lives of 4 and 2 h at 70 and 80 °C, respectively. In addition to the natural substrates melibiose, raffinose, and stachyose, 4NP α-D-galactopyranoside was hydrolyzed. Galactose was also liberated from locust bean gum. Both heat-active enzymes are attractive candidates for application in food and feed industry for high-temperature processes for the degradation of raffinose family oligosaccharides.
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