D-Amino Acid Oxidase from Trigonopsis variabilis : Immobilization of Whole Cells in Natural Polymeric Gels for Glutary1-7-Aminocephalosporanic Acid Production

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The enzymatic oxidation of cephalosporin C to glutaryl-7-aminocephalosporanic acid (glutaryl-7-ACA) was carried out utilizing permeabilized whole cells of the yeast Trigonopsis variabilis entrapped in Ca-alginate beads. The biomass, cultured in a rich medium containing DL-methionine and harvested after 72 h of growth, exhibited high levels of D-amino acid oxidase activity. Prior to use, the whole cells were permeabilized with four freeze-thawing cycles and immoblized in polysaccharide matrices, such as Ca-alginate and k-carrageenan, and in an insolubilized gelatin gel. The best results in terms of activity yield and storage stability were obtained with cells entrapped in Ca-alginate beads. These cells were utilized for glutaryl-7-ACA production in a continuous stirred batch reactor (CSTR) and in a packed bed reactor working as a plug flow reactor (PFR), using 50 mM cephalosporin C as substrate. The performances of the two systems were compared. The overall productivities (calculated on a void volume basis) were 1.64 g and 255 mg of glutaryl-7-ACA l^<-1> h^<-1> in the PFR and in the CSTR, respectively.
1996-02-25