ArticleIranian journal of biotechnology2018
Increasing Performance and Thermostability of D-Phenylglycine Aminotransferase in Miscible Organic Solvents.
Article in Iranian journal of biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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2 authors at 1 institution in 2 countries.
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Abstract
backgroundD-Phenylglycine aminotransferase (D-PhgAT) is highly beneficial in pharmaceutical biotechnology. Like many other enzymes, D-PhgAT suffers from low stability under harsh processing conditions, poor solubility of substrate, products and occasional microbial contamination. Incorporation of miscible organic solvents into the enzyme's reaction is considered as a solution for these problems; however, native D-PhgAT is not significantly stable in such solvents.
objectiveHalophiles are known to survive and withstand unsavory habitats owing to their proteome bios. In the current study, with an eye on further industrial applications, we examined the performance and thermostability of four halophilic peptides fused D-PhgAT variants in reaction mixtures of various proportions of different miscible organic solvents and various temperatures as well as desiccation. MATERIALS AND
methodsPlasmid constructs from the previous study (Two alpha helixes and loops between them from
resultsStudy confirmed increased
conclusionOur results suggest that applying this new technique could be invaluable for making enzymes durable in discordant industrial conditions.
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