Abstract:
:By combining gene design and heterologous over-expression of Rhodotorula gracilis D-amino acid oxidase (RgDAO) in Pichia pastoris, enzyme production was enhanced by one order of magnitude compared to literature benchmarks, giving 350 kUnits/l of fed-batch bioreactor culture with a productivity of 3.1 kUnits/l h. P. pastoris cells permeabilized by freeze-drying and incubation in 2-propanol (10% v/v) produce a highly active (1.6 kUnits/g dry matter) and stable oxidase preparation. Critical bottlenecks in the development of an RgDAO catalyst for industrial applications have been eliminated.
journal_name
Biotechnol Lettjournal_title
Biotechnology lettersauthors
Abad S,Nahalka J,Winkler M,Bergler G,Speight R,Glieder A,Nidetzky Bdoi
10.1007/s10529-010-0456-9subject
Has Abstractpub_date
2011-03-01 00:00:00pages
557-63issue
3eissn
0141-5492issn
1573-6776journal_volume
33pub_type
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