ArticleBiotechnology letters2022
Identification, molecular and biochemical characterization of a novel thermoactive and thermostable glucoamylase from Thermoanaerobacter ethanolicus.
Article in Biotechnology letters, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed, 4 citations in OpenAlex.
- Extremophilic Microorganisms as a Source of Emerging Enzymes for the Food Industry: A Review.Food science & nutrition · 2025Review
- Microbial glucoamylases: structural and functional properties and biotechnological uses.World journal of microbiology & biotechnology · 2023Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
purposeWe identified a new glucoamylase (TeGA) from Thermoanaerobacter ethanolicus, a thermophilic anaerobic bacterium. Structural studies suggest that TeGA belongs to the family 15 of glycosylhydrolases (GH15).
methodsThe expression of this enzyme was optimized in E. coli (BL21) cells in order to have the highest amount of soluble protein (around 3 mg/l of culture medium).
resultsTeGA showed a high optimum temperature of 75 °C. It also showed one of the highest specific activities reported for a bacterial glucoamylase (75.3 U/mg) and was also stable in a wide pH range (3.0-10.0). Although the enzyme was preferentially active with maltose, it was also able to hydrolyze different soluble starches such as those from potato, corn or rice. TeGA showed a high thermostability up to around 70 °C, which was increased in the presence of PEG8000, and also showed to be stable in the presence of moderate concentrations of ethanol.
conclusionWe propose that TeGA could be suitable for use in different industrial processes such as biofuel production and food processing.
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