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Journal of Applied Phycology

, Volume 23, Issue 5, pp 887–894 | Cite as

Enzymatic antioxidant response to low-temperature acclimation in the cyanobacterium Arthrospira platensis

  • Lee-Feng Chien
  • Avigad Vonshak
Article

Abstract

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.

Keywords

Catalase Dehydroascorbate reductase Enzymatic antioxidant Glutathione reductase Low temperature Peroxidase Superoxide dismutase 

Notes

Acknowledgments

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.

Supplementary material

10811_2010_9607_Fig10_ESM.gif (57 kb)
Fig. S1

A simplified system of scavenging reactive species in cyanobacterium A. platensis. Abbreviations: Asc, ascorbate; CAT, catalase; DHA, dehydroascorbate; DHAR, dehydroascorbate reductase; GR, glutathione reductase; GSH, reduced glutathione; GSSG, oxidized glutathione; H2O2, hydrogen peroxide; MDHA·, monodehydroascorbate radical; MDHAR, monodehydroascorbate reductase; O2·, superoxide; PSI, photosystem I; PSII, photosystem II; PX, peroxidase; SOD, superoxide dismutase (GIF 56 kb)

10811_2010_9607_MOESM1_ESM.tiff (36 kb)
High resolution image file (TIFF 36 kb)
10811_2010_9607_Fig11_ESM.gif (92 kb)
Fig. S2

Measurement of enzyme activity at various Chl a concentrations. The enzyme activities were assayed as described in the “Materials and methods” and measured at concentrations of 2, 4, 6, and 8 μg Chl a mL−1. Data are means ± SE (n = 4, with exception of n = 2 in DHAR measurement) (GIF 91 kb)

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High resolution image file (TIFF 5829 kb)
10811_2010_9607_Fig12_ESM.gif (57 kb)
Fig. S3

Growth of A. platensis Kenya and M2 indicated as increases in Chl concentration during cultivation at 33°C and then shifted to 15°C. The temperature shift was performed when the culture reached 6 μg Chl a mL−1. (Empty circles), Kenya; (filled circles), M2. ‘Day-0’ was defined as the time of cold acclimation. I, II, and III refer to the control, inhibitory, and acclimated stages, respectively. Data are means ± SE (n = 4). (GIF 57 kb)

10811_2010_9607_MOESM3_ESM.tiff (4.3 mb)
High resolution image file (TIFF 4416 kb)

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Copyright information

© Springer Science+Business Media B.V. 2010

Authors and Affiliations

  1. 1.The Landau Family Microalgal Biotechnology Laboratory, The Jacob Blaustein Institutes for Desert ResearchBen-Gurion University of the NegevBeershebaIsrael
  2. 2.Department of Life SciencesNational Chung-Hsing UniversityTaichungTaiwan

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