Product deactivation in recombinant Streptomyces
- 1 July 1990
- journal article
- research article
- Published by Wiley in Biotechnology & Bioengineering
- Vol. 36 (3) , 243-251
- https://doi.org/10.1002/bit.260360305
Abstract
The production of tyrosinase by Streptomyces antibioticus (p1J7O2) was investigated as a model system for recombinant protein production by Streptomyces. Product deactivation was found to have a severe effect on the levels of tyrosinase obtained. Tyrosinase deactivation was detected during all phases of batch cultures, with higher specific deactivation rates observed during the stationary phase. The specific deactivation rate exhibited an Arrhenius dependence on temperature, with approximately a twofold increase in the deactivation rate between 25°C and 30°C. The effect of deactivation on the determination of tyrosinase production kinetics is discussed. A strategy was implemented to increase tyrosinase productivity by enriching the growth medium and reducing the culture temperature during the period of maximum tyrosinase production. This strategy resulted in a shorter culture time and a 2.5-fold increase in tyrosinase activity compared to a culture grown at 25°C using a standard growth medium.This publication has 15 references indexed in Scilit:
- Induction of tyrosinase by L-methionine in Streptomyces antibioticusCanadian Journal of Microbiology, 1988
- Intracellular degradation of recombinant proteins in relation to their location in Escherichia coli cellsJournal of Biotechnology, 1987
- Cloning and expression of the genetically unstable tyrosinase structural gene from Streptomyces glaucescensMolecular Genetics and Genomics, 1985
- The nucleotide sequence of the tyrosinase gene from Streptomyces antibioticus and characterization of the gene productGene, 1985
- Dephenolization of industrial wastewaters catalyzed by polyphenol oxidaseBiotechnology & Bioengineering, 1984
- Optimization of Fermentation Processes Through the Control of In Vivo Inactivation of Microbial Biosynthetic EnzymesPublished by American Chemical Society (ACS) ,1983
- pIJ101, a multi-copy broad host-range Streptomyces plasmid: Functional analysis and development of DNA cloning vectorsMolecular Genetics and Genomics, 1982
- E. coli contains eight soluble proteolytic activities, one being ATP dependentNature, 1981
- Purification and Characterization of a Tyrosinase from Streptomyces glaucescensEuropean Journal of Biochemistry, 1972
- Role of Proteases in SporulationCurrent Topics in Cellular Regulation, 1972