Calcium Alginate Bead Immobilization of Cells Containing Tyrosine Ammonia Lyase Activity for Use in the Production of p-Hydroxycinnamic Acid
Autor: | Robert DiCosimo, F. Sima Sariaslani, Lixuan Huang, Arie Ben-Bassat, Carl E. Camp, Grace A. Crum, Robert J Trotman, Sharon L. Haynie |
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Rok vydání: | 2008 |
Předmět: |
Ammonia-Lyases
Calcium alginate Coumaric Acids Alginates Bioconversion chemistry.chemical_element Calcium Catalysis chemistry.chemical_compound Glucuronic Acid Phenols Enzyme Stability Polyethyleneimine Organic chemistry Tyrosine chemistry.chemical_classification Molecular Structure urogenital system Hexuronic Acids Temperature Cells Immobilized Hydrogen-Ion Concentration Hydroxycinnamic acid Microspheres Tyrosine ammonia-lyase activity chemistry Glutaral Glutaraldehyde Biotechnology Nuclear chemistry |
Zdroj: | Biotechnology Progress. 23:638-644 |
ISSN: | 8756-7938 |
DOI: | 10.1021/bp060379e |
Popis: | An Escherichia coli catalyst with tyrosine ammonia lyase activity (TAL) has been stabilized for repeated use in batch conversions of high tyrosine solids to p-hydroxycinnamic acid (pHCA). The TAL biocatalyst was stabilized by controlling the reaction pH to 9.8 +/- 0.1 and immobilizing the cells within a calcium alginate matrix that was cross-linked with glutaraldehyde and polyethyleneimine (GA/PEI). We found a GA range where the bead-encapsulated TAL was not inactivated, and the resulting cross-linking provided the beads with the mechanical stability necessary for repeated use in consecutive batch reactions with catalyst recycle. The GA/PEI calcium alginate TAL catalyst was used in 41 1-L batch reactions where 50 g L(-1) tyrosine was converted to 39 +/- 4 g L(-1) pHCA in each batch. The practical usefulness and ease of this process was demonstrated by scaling up the TAL bead immobilization and using the immobilized TAL catalyst in four 125-L bioconversion reactions to produce over 12 kg of purified pHCA. |
Databáze: | OpenAIRE |
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