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Literature summary for 4.1.2.47 extracted from

  • Hasslacher, M.; Schall, M.; Hayn, M.; Bona, R.; Rumbold, K.; Lueckl, J.; Griengl, H.; Kohlwein, S.D.; Schwab, H.
    High-level intracellular expression of hydroxynitrile lyase from the tropical rubber tree Hevea brasiliensis in microbial hosts (1997), Protein Expr. Purif., 11, 61-71.
    View publication on PubMed

Application

Application Comment Organism
synthesis the enzyme is a potent biocatalyst for the industrial production of chemicals Hevea brasiliensis

Cloned(Commentary)

Cloned (Comment) Organism
limitations in enzyme supply from natural resources are overcome by production of the enzyme in the microbial host systems Escherichia coli, Sachycharomyces cerevisiae, and Pichia pastoris. Expression of Hnl in the prokaryotic system leads to the formation of inclusion bodies whereas in both yeast hosts high levels of soluble protein are obtained. Highest yields are obtained in a high cell density batch fermentation of a Pichia pastoris transformant that expresses heterologous Hnl to about 50% of the soluble cytosolic protein. At a cell density of 100 g/liter cell dry weight, a volume yield of 22 g/liter of heterologous product is obtained. Attempts to produce the Hnl protein extracellularly with the yeast hosts by applying different leader peptide strategies are not successful. Immunofluorescence microscopy studies indicate that the secretion-directed heterologous Hnl protein accumulates in the plasma membrane forming aggregated clusters of inactive protein Hevea brasiliensis

Organism

Organism UniProt Comment Textmining
Hevea brasiliensis P52704
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