English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

l -Phenylalanine ammonia-lyase (PAL; EC 4.3.1.5) fromRhodotorula rubra has been used in the commercial manufacture ofl -phenylalanine fromtrans -cinnamic acid. In this study,R. graminis PAL was investigated. Mutant strain GX6000 was isolated after ethyl methanesulfonate mutagenesis of wild-typeR. graminis GX5007 by selecting for resistance to phenylpropiolic acid, an analog oftrans -cinnamic acid. Mutant strain GX6000 produced inducible PAL at levels four- to fivefold higher than had wild-typeR. graminis. Furthermore, this strain had several other physiological traits that make it more commercially useful thanR. rubra. For example, during fermentation, the PAL half-life was three- to fivefold longer, PAL specific activity was six to seven times higher, and PAL synthesis was significantly less inhibited by temperatures above 30°C. Induction of PAL in strain GX6000 appeared to be less tightly regulated;l -leucine acted synergistically withl -phenylalanine, the physiological inducer, to increase the PAL specific activity and titer to 165 U/g (dry weight) and 3,000 U/liter, respectively, a 40% increase over the effect ofl -phenylalanine alone. Strain GX6000 PAL showed significantly greater stability in bioreactors for the synthesis ofl -phenylalanine, a finding that is consistent with the stability properties observed during fermentation.

Strain Improvement of Rhodotorula graminis for Production of a Novel l -Phenylalanine Ammonia-Lyase