ArticleExtremophiles : life under extreme conditions2006
Protein engineering of a cold-active beta-galactosidase from Arthrobacter sp. SB to increase lactose hydrolysis reveals new sites affecting low temperature activity.
Article in Extremophiles : life under extreme conditions, 2006. 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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11 citing papers in PubMed, 32 citations in OpenAlex.
- Biotechnological potential of psychrophilic microorganisms as the source of cold-active enzymes in food processing applications.3 Biotech · 2021Review
- Purified lactases versus whole-cell lactases-the winner takes it all.Applied microbiology and biotechnology · 2021Review
- AntarcticInternational journal of molecular sciences · 2021Article
- Extremophile - An Adaptive Strategy for Extreme Conditions and Applications.Current genomics · 2020Review
- Recent advances in understanding extremophiles.F1000Research · 2019Review
- Molecular cloning, expression, and characterization of four novel thermo-alkaliphilic enzymes retrieved from a metagenomic library.Biotechnology for biofuels · 2017Article
- Discovery, Molecular Mechanisms, and Industrial Applications of Cold-Active Enzymes.Frontiers in microbiology · 2016Review
- Extremophiles and biotechnology: current uses and prospects.F1000Research · 2016Review
- A novel cold-adapted β-galactosidase isolated from Halomonas sp. S62: gene cloning, purification and enzymatic characterization.World journal of microbiology & biotechnology · 2013Article
- Lactulose biosynthesis by β-galactosidase from a newly isolated Arthrobacter sp.Journal of industrial microbiology & biotechnology · 2011Article
- Marine metagenomics: strategies for the discovery of novel enzymes with biotechnological applications from marine environments.Microbial cell factories · 2008Article
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2 authors at 1 institution in 1 country.
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Abstract
We examined variants of an especially cold-active beta-galactosidase (BgaS) to better understand features affecting enzyme activity at temperature extremes. We targeted locations corresponding to a region in the LacZ enzyme previously shown to increase activity and decrease thermostability. Changes in this region of BgaS consistently caused the elimination or reduction of activity. A gene (bgaS3) encoding a loss of function variant was subjected to random mutagenesis to restore activity and discover potential interactions important in cold activity. Gene sequences from the resulting library indicated that only two amino acid alterations, E229D and V405A, were required to restore activity. Genes with combinations of these mutations were constructed and their enzymes purified. Enzymes with the E229D/V405A/G803D alterations (BgaS6), or E229D/V405A (BgaS7) had similar thermal optima and thermostabilities as BgaS. BgaS7, however, showed a 2.5-fold increase in catalytic activity at 15 degrees C and hydrolyzed 80% of lactose in skim milk in less than half the time of BgaS at 2.5 degrees C. Computer-generated models predicted that the substitutions at positions 229 and 405 yielded fewer contacts at the enzyme's activating interface. Results from regional saturation mutagenesis supported this hypothesis and suggested that not easily predicted, subtle, cooperative intramolecular interactions contributed to thermal adaptation.
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