Characterization and rational modification of aspartate 4‐decarboxylase from Acinetobacter radioresistens for the production of l‐alanine
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DOI: 10.1002/bit.27761
Abstract: Enzymatic synthesis of l‐alanine has the advantages of less byproducts, strong stereoselectivity, and high catalytic efficiency. Aspartate 4‐decarboxylase (ASD) is used industrially in DL‐aspartic acid resolution and l‐alanine production because it catalyzes the decarboxylation of… read more here.
Keywords: acinetobacter radioresistens; alanine; aspartate decarboxylase; production ... See more keywords
Extracellular Expression of L-Aspartate-α-Decarboxylase from Bacillus tequilensis and Its Application in the Biosynthesis of β-Alanine
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DOI: 10.1007/s12010-019-03013-1
Abstract: L-aspartate-α-decarboxylase was extracellularly expressed to enhance its production for β-alanine biosynthesis. L-aspartate-α-decarboxylase and cutinase were coexpressed in Escherichia coli; more than 40% of the L-aspartate-α-decarboxylase was secreted into the medium. Selection of best conditions among… read more here.
Keywords: alanine; decarboxylase; extracellular expression; aspartate decarboxylase ... See more keywords
Pantothenate auxotrophy in Zymomonas mobilis ZM4 is due to a lack of aspartate decarboxylase activity.
Sign Up to like & getrecommendations! Published in 2017 at "FEMS microbiology letters"
DOI: 10.1093/femsle/fnx136
Abstract: The bacterium Zymomonas mobilis naturally produces ethanol at near theoretical maximum yields, making it of interest for industrial ethanol production. Zymomonas mobilis requires the vitamin pantothenate for growth. Here we characterized the genetic basis for… read more here.
Keywords: pantothenate auxotrophy; zymomonas mobilis; aspartate decarboxylase; mobilis ... See more keywords