Optimization of the immobilization parameters and operational stability of immobilized hydantoinase and l-N-carbamoylase from Arthrobacter aurescens for the production of optically pure l-amino acids

Enzyme and Microbial Technology
K RagnitzM Pietzsch

Abstract

2The immobilization parameters were optimized for the hydantoinase and the L-N-carbamoylase from Arthrobacter aurescens DSM 3747 or 3745, respectively. To optimize activity yields and specific activities for the immobilization to Eupergit C, Eupergit C 250 L, and EAH-Sepharose wild-type, recombinant and genetically modified ('tagged') enzymes were investigated concerning the influence of the protein concentration, the kind of support and the immobilization method. For both enzymes, the use of the recombinant proteins resulted in enhanced specific activities especially when using a hydrophilic support for immobilization such as Sepharose. In the case of a genetically modified hydantoinase carrying a His(6)-tag, affinity coupling led to a loss of activity of higher than 80%. Both enzymes were significantly stabilized by immobilization: In packed bed reactors, Eupergit C 250 L (NH(2))-immobilized hydantoinase and EAH-Sepharose-immobilized L-N-carbamoylase showed half-life times of approx. 14000 and 900 hours, respectively. Together with specific activities of the immobilized enzymes of 2.5 U/g wet carrier (hydantoinase) and 10 U/g wet carrier (L-N-carbamoylase) the newly developed biocatalysts are sufficient to fulfill industrial ...Continue Reading

Citations

Feb 19, 2002·Current Opinion in Biotechnology·J AltenbuchnerC Syldatk
Sep 27, 2002·Current Opinion in Biotechnology·Jeroen van RoonHans Tramper
Jan 28, 2005·Biotechnology and Bioengineering·J L van RoonH H Beeftink
Jan 2, 2007·Biotechnology Advances·J L van RoonH H Beeftink
May 21, 2013·Biotechnology and Applied Biochemistry·Hemraj S NandanwarGurinder S Hoondal
Mar 1, 2013·Chemical Society Reviews·Andreas Liese, Lutz Hilterhaus

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