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Simple enzymatic procedure forl-carnosine synthesis: whole-cell biocatalysis and efficient biocatalyst recycling.
- Source :
- Microbial Biotechnology; Jan2010, Vol. 3 Issue 1, p74-83, 10p, 2 Diagrams, 2 Charts, 6 Graphs
- Publication Year :
- 2010
-
Abstract
- β-Peptides and their derivates are usually stable to proteolysis and have an increased half-life compared with α-peptides. Recently, β-aminopeptidases were described as a new enzyme class that enabled the enzymatic degradation and formation of β-peptides. As an alternative to the existing chemical synthesis routes, the aim of the present work was to develop a whole-cell biocatalyst for the synthesis and production of β-peptides using this enzymatic activity. For the optimization of the reaction system we chose the commercially relevant β, α-dipeptidel-carnosine ( β-alanine-l-histidine) as model product. We were able to show that different recombinant yeast and bacteria strains, which overexpress a β-peptidase, could be used directly as whole-cell biocatalysts for the synthesis ofl-carnosine. By optimizing relevant reaction conditions for the best-performing recombinant Escherichia coli strain, such as pH and substrate concentrations, we obtained highl-carnosine yields of up to 71%. Long-time as well as biocatalyst recycling experiments indicated a high stability of the developed biocatalyst for at least five repeated batches. Application of the recombinant E. coli in a fed-batch process enabled the accumulation ofl-carnosine to a concentration of 3.7 g l<superscript>−1</superscript>. [ABSTRACT FROM AUTHOR]
- Subjects :
- CARNOSINE
ENZYMES
PEPTIDES
PROTEOLYSIS
BIOSYNTHESIS
CHEMICAL reactions
Subjects
Details
- Language :
- English
- ISSN :
- 17517907
- Volume :
- 3
- Issue :
- 1
- Database :
- Complementary Index
- Journal :
- Microbial Biotechnology
- Publication Type :
- Academic Journal
- Accession number :
- 47051367
- Full Text :
- https://doi.org/10.1111/j.1751-7915.2009.00143.x