ArticleApplied microbiology and biotechnology2012
Production of cyanophycin in Rhizopus oryzae through the expression of a cyanophycin synthetase encoding gene.
Article in Applied microbiology and biotechnology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- CRISPR-Cas9 induces point mutation in the mucormycosis fungus Rhizopus delemar.Fungal genetics and biology : FG & B · 2019Article
- Autotrophic production of stable-isotope-labeled arginine in Ralstonia eutropha strain H16.Applied and environmental microbiology · 2012Article
- Metabolic engineering of Rhizopus oryzae for the production of platform chemicals.Applied microbiology and biotechnology · 2012Review
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4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Cyanophycin or cyanophycin granule peptide is a protein that results from non-ribosomal protein synthesis in microorganisms such as cyanobacteria. The amino acids in cyanophycin can be used as a feedstock in the production of a wide range of chemicals such as acrylonitrile, polyacrylic acid, 1,4-butanediamine, and urea. In this study, an auxotrophic mutant (Rhizopus oryzae M16) of the filamentous fungus R. oryzae 99-880 was selected to express cyanophycin synthetase encoding genes. These genes originated from Synechocystis sp. strain PCC6803, Anabaena sp. strain PCC7120, and a codon optimized version of latter gene. The genes were under control of the pyruvate decarboxylase promoter and terminator elements of R. oryzae. Transformants were generated by the biolistic transformation method. In only two transformants both expressing the cyanophycin synthetase encoding gene from Synechocystis sp. strain PCC6803 was a specific enzyme activity detected of 1.5 mU/mg protein. In one of these transformants was both water-soluble and insoluble cyanophycin detected. The water-soluble fraction formed the major fraction and accounted for 0.5% of the dry weight. The water-insoluble CGP was produced in trace amounts. The amino acid composition of the water-soluble form was determined and constitutes of equimolar amounts of arginine and aspartic acid.
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