Enzymatic antioxidant response to low-temperature acclimation in the cyanobacterium Arthrospira platensis
- 243 Downloads
Changes in antioxidant enzyme activities in response to low-temperature-induced photoinhibition were investigated in the two strains of the cyanobacterium Arthrospira platensis, Kenya and M2. When transferred to 15°C from 33°C, cells exhibited an immediate cessation of growth followed by a new acclimated growth rate. Although both strains had similar growth rates at 33°C, once transferred to a lower temperature environment, Kenya had a faster growth rate than M2. There were variations in the antioxidant enzyme activities of both strains during 15°C acclimation. The activity of superoxide dismutase from Kenya was higher than that from M2 and increased remarkably with acclimation time. Catalase activity of both strains increased at first but decreased later in the acclimation process. Ascorbate-dependent peroxidase activity of the Kenya strain declined when transferred to the low-temperature environment while peroxidase activity of M2 decreased in the beginning and then increased with time. The dehydroascorbate reductase activity of both strains was variable during the acclimation period while the glutathione reductase activity was not modified immediately. Our finding may support that the faster growth rate of the Kenya strain at lower temperatures as compared with the M2 strain might be explained by the higher antioxidant enzyme activities of Kenya at lower temperatures and through its ability to apply a more efficient regulatory strategy of enzymatic antioxidant response to low-temperature-induced photoinhibition.
KeywordsCatalase Dehydroascorbate reductase Enzymatic antioxidant Glutathione reductase Low temperature Peroxidase Superoxide dismutase
This work was supported by a fellowship to Lee-Feng Chien from the Blaustein Center for scientific collaboration in the Jacob Blaustein Institutes for Desert Research, Israel. We would like to acknowledge the significant contribution of Ms. Nurit Novsplanski for reading and preparing the paper for publication, and for technical assistance. The secretarial help from Ilana Saller is also greatly appreciated.
- Asada K (1994) Mechanism for scavenging reactive molecules generated in chloroplasts under light stress. In: Baker NR, Bowyer JR (eds) Photoinhibition of photosynthesis from molecular mechanism to the field. Bios Scientific, Lancaster, pp 129–142Google Scholar
- Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 82:327Google Scholar
- Hall DO, Rao KK (1999) Chapter 3: photosynthetic apparatus. In: Hall DO, Rao KK (eds) Photosynthesis. Cambridge University Press, Cambridge, pp 32–54Google Scholar
- Mallick N, Mohn FH (2000) Reactive oxygen species: response of algal cells. J Plant Physiol 157:183–193Google Scholar
- Mallick N, Rai LC (1999) Response of the antioxidant systems of the nitrogen fixing cyanobacterium Anabaena doliolum to copper. J Plant Physiol 155:146–149Google Scholar
- Miyake C, Michihata F, Asada K (1991) Scavenging of hydrogen peroxide in prokaryotic and eukaryotic algae: acquisition of ascorbate peroxidase during the evolution cyanobacteria. Plant Cell Physiol 32:33–43Google Scholar
- Srivastava AK, Bhargava P, Mishra Y, Shukla B, Rai LC (2006) Effect of pretreatment of salt, copper and temperature on ultraviolet-B-induced antioxidants in diazotrophic cyanobacterium Anabaena doliolum. J Basic Microbiol 46:134–144Google Scholar
- Vonshak A (1997) Outdoor mass production of Spirulina: the basic concept. In: Vonshak A (ed) Spirulina platensis (Arthrospira): physiology, cell-biology and biotechnology. Taylor & Francis, London, pp 79–99Google Scholar