Antarctic Sea Ice Bacterium Research Articles

A novel cold-adapted nitroreductase from Psychrobactersp. ANT206: Heterologous expression, characterization and nitrobenzene reduction capacity

Widely used in multiple industrial processes, nitro-aromatic compounds, especially nitrobenzene, in low temperature environment are considered as heavy pollutants. Among the disposal methods, the bioreduction method has attracted much attention. In this study, a novel cold-adapted nitroreductase gene (psntr) was cloned from Antarctic sea-ice bacteria Psychrobacter sp. ANT206. The psntr gene was 813 bp in length and encoded a protein with flavin mononucleotide (FMN) binding sites. Homology modeling was performed to obtain structural information such as the longer loops and reduced amount of hydrogen bonds, which might be related to the high catalytic efficiency of PsNTR at low temperature. The psntr gene was successfully cloned in cold-shock pCold I vector and transformed to the expression host Escherichia coli (E. coli) BL21 with the induction by isopropyl β-D-thiogalactoside (IPTG) at low temperature (16 °C) for 24 h. The recombinant PsNTR (rPsNTR) was purified using Ni-NTA with the specific activity of 51.59 μmol/min/mg. Interestingly, rPsNTR displayed the highest activity at 25 °C and still maintained 46.9% of the activity at 0 °C. rPsNTR also exhibited the highest activity (136.4%) at 1.0 M NaCl with incredible salt tolerance. The kinetic parameters and substrates specificity analysis demonstrated that rPsNTR could reduce various nitro-aromatic compounds. Moreover, the result of the reduction capability revealed that the recombinant E. coli exhibited a maximum nitrobenzene reduction rate of 3.03 mM/h at 16 °C. These findings revealed that the characteristics of rPsNTR might make it an excellent candidate for the bioreduction of various nitro-aromatic compounds in the low temperature and high-salt wastewater.

Purification and characterization of a novel wild-type α-amylase from Antarctic sea ice bacterium Pseudoalteromonas sp. M175

A novel wild-type α-amylase named wtAmy175 from Pseudoalteromonas sp. M175 strain was purified through ammonium sulphate precipitation, DEAE cellulose, and Sephadex G-75 sequentially (25.83-fold, 7.67%-yield) for biochemical characterization. SDS-PAGE and zymographic activity staining of purified enzyme showed a single band with a predicted molecular mass of about 61 kDa. The optimum temperature and pH for enzyme activity were 30 °C and 7.5, respectively. Additionally, the enzyme exhibited high activity and remarkable stability in 0–10 mM SDS. The values of Km and Vmax for soluble starch as substrate were 2.47 mg/ml and 0.103 mg/ml/min, respectively. Analysis of hydrolysis products of soluble starch and maltooligosaccharides showed that wtAmy175 cleaved the interior and the terminal α-1,4-glycosidic linkage in starch, and had transglycosylation activity. The result of fluorescence spectroscopy showed that wtAmy175 had strong binding affinity with soluble starch. In brief, this study discovered the first wild-type α-amylase so far with several distinctive properties of cold activity, SDS-resistance, and the mixed activity of α-amylase and α-glucosidase, suggesting that wtAmy175 possess high adaptive capability to endure harsh industrial conditions and would be an excellent candidate in detergent and textile industries.

Cold-Adapted Glutathione S-Transferases from Antarctic Psychrophilic Bacterium Halomonas sp. ANT108: Heterologous Expression, Characterization, and Oxidative Resistance.

Glutathione S-transferases are one of the most important antioxidant enzymes to protect against oxidative damage induced by reactive oxygen species. In this study, a novel gst gene, designated as hsgst, was derived from Antarctic sea ice bacterium Halomonas sp. ANT108 and expressed in Escherichia coli (E. coli) BL21. The hsgst gene was 603 bp in length and encoded a protein of 200 amino acids. Compared with the mesophilic EcGST, homology modeling indicated HsGST had some structural characteristics of cold-adapted enzymes, such as higher frequency of glycine residues, lower frequency of proline and arginine residues, and reduced electrostatic interactions, which might be in relation to the high catalytic efficiency at low temperature. The recombinant HsGST (rHsGST) was purified to apparent homogeneity with Ni-affinity chromatography and its biochemical properties were investigated. The specific activity of the purified rHsGST was 254.20 nmol/min/mg. The optimum temperature and pH of enzyme were 25 °C and 7.5, respectively. Most importantly, rHsGST retained 41.67% of its maximal activity at 0 °C. 2.0 M NaCl and 0.2% H2O2 had no effect on the enzyme activity. Moreover, rHsGST exhibited its protective effects against oxidative stresses in E. coli cells. Due to its high catalytic efficiency and oxidative resistance at low temperature, rHsGST may be a potential candidate as antioxidant in low temperature health foods.

A Novel Cold-Adapted Leucine Dehydrogenase from Antarctic Sea-Ice Bacterium Pseudoalteromonas sp. ANT178.

l-tert-leucine and its derivatives are useful as pharmaceutical active ingredients, in which leucine dehydrogenase (LeuDH) is the key enzyme in their enzymatic conversions. In the present study, a novel cold-adapted LeuDH, psleudh, was cloned from psychrotrophic bacteria Pseudoalteromonas sp. ANT178, which was isolated from Antarctic sea-ice. Bioinformatics analysis of the gene psleudh showed that the gene was 1209 bp in length and coded for a 42.6 kDa protein containing 402 amino acids. PsLeuDH had conserved Phe binding site and NAD+ binding site, and belonged to a member of the Glu/Leu/Phe/Val dehydrogenase family. Homology modeling analysis results suggested that PsLeuDH exhibited more glycine residues, reduced proline residues, and arginine residues, which might be responsible for its catalytic efficiency at low temperature. The recombinant PsLeuDH (rPsLeuDH) was purified a major band with the high specific activity of 275.13 U/mg using a Ni-NTA affinity chromatography. The optimum temperature and pH for rPsLeuDH activity were 30 °C and pH 9.0, respectively. Importantly, rPsLeuDH retained at least 40% of its maximum activity even at 0 °C. Moreover, the activity of rPsLeuDH was the highest in the presence of 2.0 M NaCl. Substrate specificity and kinetic studies of rPsLeuDH demonstrated that l-leucine was the most suitable substrate, and the catalytic activity at low temperatures was ensured by maintaining a high kcat value. The results of the current study would provide insight into Antarctic sea-ice bacterium LeuDH, and the unique properties of rPsLeuDH make it a promising candidate as a biocatalyst in medical and pharmaceutical industries.

Cloning, expression and enzymatic characteristics of a 2-Cys peroxiredoxin from Antarctic sea-ice bacterium Psychrobacter sp. ANT206.

Peroxiredoxin (Prx, EC 1.11.1.15) is a family of the thiol-dependent antioxidant enzyme. In this study, a cold-adapted Prx gene from Antarctic psychrophilic bacterium Psychrobacter sp. ANT206 (PsPrx) consisted of an open reading frame (ORF) of 567 bp was cloned. Amino acid sequence analysis revealed that PsPrx contained one catalytic site (Thr45, Cys48 and Arg121) and could be categorized as a typical 2-Cys Prx. Compared with the mesophilic StPrx, PsPrx with a reduced amount of hydrogen bonds and salt bridges and other characteristics, may be responsible for its enzymatic stability and flexibility at low temperature. The recombinant PsPrx (rPsPrx) was purified to homogeneity by Ni-NTA and its enzymatic characterization was described. Interestingly, rPsPrx exhibited the maximum activity at 30 °C and remained 42.6% of its maximum activity at 0 °C. rPsPrx was a salt-tolerance enzyme that showed 42.2% of its maximum activity under 2.5 M NaCl. The kinetic parameters of different substrates revealed that it could efficiently catalyze the peroxides, especially H2O2 and t-BOOH (tert‑butyl hydroperoxide). Moreover, rPsPrx exhibited the ability to protect super-coiled DNA from oxidative damage. These results indicated that rPsPrx has special catalytic properties and may be a promising candidate for food and industrial applications.

Molecular Cloning and Characterization of a Novel α-Amylase from Antarctic Sea Ice Bacterium Pseudoalteromonas sp. M175 and Its Primary Application in Detergent.

A novel cold-adapted and salt-tolerant α-amylase gene (amy175) from Antarctic sea ice bacterium Pseudoalteromonas sp. M175 was successfully cloned and expressed. The open reading frame (ORF) of amy175 had 1722 bp encoding a protein of 573 amino acids residues. Multiple alignments indicated Amy175 had seven highly conserved sequences and the putative catalytic triad (Asp244, Glu286, and Asp372). It was the first identified member of GH13_36 subfamily which contained QPDLN in the CSR V. The recombinant enzyme (Amy175) was purified to homogeneity with a molecular mass of about 62 kDa on SDS-PAGE. It had a mixed enzyme specificity of α-amylase and α-glucosidase. Amy175 displayed highest activity at pH 8.0 and 25°C and exhibited extreme salt-resistance with the maximum activity at 1 M NaCl. Amy175 was strongly stimulated by Mg2+, Ni2+, K+, 1 mM Ca2+, 1 mM Ba2+, 1 mM Pb2+, 1 mM sodium dodecyl sulphate (SDS), and 10% dimethyl sulfoxide (DMSO) but was significantly inhibited by Cu2+, Mn2+, Hg2+, 10 mM β-mercaptoethanol (β-ME), and 10% Tween 80. Amy175 demonstrated excellent resistance towards all the tested commercial detergents, and wash performance analysis displayed that the addition of Amy175 improved the stain removal efficiency. This study demonstrated that Amy175 would be proposed as a novel α-amylase source for industrial application in the future.

Effect of Marine-Derived Ice-Binding Proteins on the Cryopreservation of Marine Microalgae.

Ice-binding protein (IBPs) protect cells from cryo-injury during cryopreservation by inhibiting ice recrystallization (IR), which is a main cause of cell death. In the present study, we employed two IBPs, one, designated LeIBP from Arctic yeast, and the other, designated FfIBP from Antarctic sea ice bacterium, in the cryopreservation of three economically valuable marine microalgae, Isochrysis galbana, Pavlova viridis, and Chlamydomonas coccoides. Both of the IBPs showed IR inhibition in f/2 medium containing 10% DMSO, indicating that they retain their function in freezing media. Microalgal cells were frozen in 10% DMSO with or without IBP. Post-thaw viability exhibited that the supplementation of IBPs increased the viability of all cryopreserved cells. LeIBP was effective in P. viridis and C. coccoides, while FfIBP was in I. galbana. The cryopreservative effect was more drastic with P. viridis when 0.05 mg/mL LeIBP was used. These results clearly demonstrate that IBPs could improve the viability of cryopreserved microalgal cells.

Coarse grained simulation reveals antifreeze properties of hyperactive antifreeze protein from Antarctic bacterium Colwellia sp.

The novel hyperactive antifreeze protein (AFP) of Antarctic sea ice bacterium Colwellia sp. provides a target for studying the protection of psychrophilic microgoranisms against freezing environment. Interestingly, the Colwellia sp. hyperactive antifreeze protein (ColAFP) was crystallized without the structural dynamic characteristics. Here, the result indicated, through coarse grained simulation of ColAFP under various subfreezing temperature, that ColAFP remains active at temperature of equal and greater than 275K (∼2°C). Extensive simulation analyses also revealed the adaptive mechanism of ColAFP in subfreezing environment. Our result provides a structural dynamic understanding of the ColAFP.

Distinct molecular features facilitating ice-binding mechanisms in hyperactive antifreeze proteins closely related to an Antarctic sea ice bacterium

Antifreeze proteins or ice-binding proteins (IBPs) facilitate the survival of certain cellular organisms in freezing environment by inhibiting the growth of ice crystals in solution. Present study identifies orthologs of the IBP of Colwellia sp. SLW05, which were obtained from a wide range of taxa. Phylogenetic analysis on the basis of conserved regions (predicted as the ‘ice-binding domain’ [IBD]) present in all the orthologs, separates the bacterial and archaeal orthologs from that of the eukaryotes’. Correspondence analysis pointed out that the bacterial and archaeal IBDs have relatively higher average hydrophobicity than the eukaryotic members. IBDs belonging to bacterial as well as archaeal AFPs contain comparatively more strands, and therefore are revealed to be under higher evolutionary selection pressure. Molecular docking studies prove that the ice crystals form more stable complex with the bacterial as well as archaeal proteins than the eukaryotic orthologs. Analysis of the docked structures have traced out the ice-binding sites (IBSs) in all the orthologs which continue to facilitate ice-binding activity even after getting mutated with respect to the well-studied IBSs of Typhula ishikariensis and notably, all these mutations performing ice-binding using ‘anchored clathrate mechanism’ have been found to prefer polar and hydrophilic amino acids. Horizontal gene transfer studies point toward a strong selection pressure favoring independent evolution of the IBPs in some polar organisms including prokaryotes as well as eukaryotes because these proteins facilitate the polar organisms to acclimatize to the adversities in their niche, thus safeguarding their existence.

Hyperactive antifreeze protein from an Antarctic sea ice bacterium Colwellia sp. has a compound ice-binding site without repetitive sequences.

Antifreeze proteins (AFPs) are structurally diverse macromolecules that bind to ice crystals and inhibit their growth to protect the organism from injuries caused by freezing. An AFP identified from the Antarctic bacterium Colwellia sp. strain SLW05 (ColAFP) is homologous to AFPs from a wide variety of psychrophilic microorganisms. To understand the antifreeze function of ColAFP, we have characterized its antifreeze activity and determined the crystal structure of this protein. The recombinant ColAFP exhibited thermal hysteresis activity of approximately 4°C at a concentration of 0.14mm, and induced rapid growth of ice crystals in the hexagonal direction. Fluorescence-based ice plane affinity analysis showed that ColAFP binds to multiple planes of ice, including the basal plane. These observations show that ColAFP is a hyperactive AFP. The crystal structure of ColAFP determined at 1.6Å resolution revealed an irregular β-helical structure, similar to known homologs. Mutational and molecular docking studies showed that ColAFP binds to ice through a compound ice-binding site (IBS) located at a flat surface of the β-helix and the adjoining loop region. The IBS of ColAFP lacks the repetitive sequences that are characteristic of hyperactive AFPs. These results suggest that ColAFP exerts antifreeze activity through a compound IBS that differs from the characteristic IBSs shared by other hyperactive AFPs. This study demonstrates a novel method for protection from freezing by AFPs in psychrophilic microorganisms. Structural data for ColAFP have been submitted to the Protein Data Bank (PDB) under accession number 3WP9.

Cloning, expression, purification, and characterization of glutaredoxin from Antarctic sea-ice bacterium Pseudoalteromonas sp. AN178.

Glutaredoxins (Grxs) are small ubiquitous redox enzymes that catalyze glutathione-dependent reactions to reduce protein disulfide. In this study, a full-length Grx gene (PsGrx) with 270 nucleotides was isolated from Antarctic sea-ice bacterium Pseudoalteromonas sp. AN178. It encoded deduced 89 amino acid residues with the molecular weight 9.8 kDa. Sequence analysis of the amino acid sequence revealed the catalytic motif CPYC. Recombinant PsGrx (rPsGrx) stably expressed in E. coli BL21 was purified to apparent homogeneity by Ni-affinity chromatography. rPsGrx exhibited optimal activity at 30°C and pH 8.0 and showed 25.5% of the activity at 0°C. It retained 65.0% of activity after incubation at 40°C for 20 min and still exhibited 37.0% activity in 1.0 M NaCl. These results indicated that rPsGrx was a typical cold active protein with low thermostability.

Molecular cloning, expression, purification and characterization of thioredoxin from Antarctic sea-ice bacteria Pseudoalteromonas sp. AN178

Thioredoxin (Trx) is a highly conserved and multi-functional protein that plays a pivotal role in maintaining the redox state of the cell and in protecting the cell against oxidative stress. Trx gene from Antarctic sea-ice bacteria Pseudoalteromonas sp. AN178 was cloned and expressed as soluble protein in Escherichia coli (designated as PsTrx). Trx gene consisted of an open reading frame of 324-bp nucleotides encoding a protein of 108 amino acids with a calculated molecular mass of 11.88kDa. The deduced protein included the conserved Cys-Gly-Pro-Cys active-site sequence. After purification by a single step Ni-NTA affinity chromatography, recombinant PsTrx with a high specific activity of 96.67U/mg was obtained. The purified PsTrx had an optimal temperature and pH of 25°C and 7.0, respectively, and showed about 55% of the residual catalytic activity even at 0-10°C. It had high tolerance to a wide range of NaCl concentrations (0-2M NaCl) and was stable in the presence of H2O2. This research suggested that PsTrx displayed unique catalytic properties.

Molecular cloning, expression and enzymatic characterization of glutathione S-transferase from Antarctic sea-ice bacteria Pseudoalteromonas sp. ANT506

A glutathione S-transferase (GST) gene from Antarctic sea-ice bacteria Pseudoalteromonas sp. ANT506 (namely PsGST), was cloned and expressed in Escherichia coli. The open reading frame of PsGST comprised 654bp encoding a protein of 217 amino acids with a calculated molecular size of 24.3kDa. The rPsGST possesses the conserved amino acid defining the binding sites of glutathione (G-site) and substrate binding pocket (H-site) in GST N_3 family. PsGST was expressed in E. coli and the recombinant PsGST (rPsGST) was purified by Ni-affinity chromatography with a high specific activity of 74.21U/mg. The purified rPsGST showed maximum activity at 40°C and exhibited 14.2% activity at 0°C. It was completely inactivated at 50°C for 40min. These results indicated that rPsGST was a typical cold active GST with low thermostability. The enzyme was little affected by H2O2 and Triton X-100, and 50.2% of the remaining activity was detected in the presence of high salt concentrations (2M NaCl). The enzymatic Km values for CDNB and GSH was 0.22mM and 1.01mM, respectively. These specific enzyme properties may be related to the survival environment of Antarctic sea ice bacteria.

Purification and biochemical characterization of a cold-active lipase from Antarctic sea ice bacteria Pseudoalteromonas sp. NJ 70

An extracellular cold-active lipase from Antarctic sea ice bacteria Pseudoalteromonas sp. NJ 70 was purified and characterized. The overall purification based on lipase activity was 27.5-fold with a yield of 25.4 %. The purified lipase showed as a single band on SDS-PAGE with an apparent molecular weight of 37 kDa. The optimum temperature and pH were 35 °C and 7.0, respectively. The lipase activity was enhanced by Ca(2+) and Mg(2+), while was partially inhibited by other metals such as Cu(2+), Zn(2+), Ba(2+), Pb(2+), Fe(2+) and Mn(2+). The lipase had high tolerance to a wide range of NaCl concentrations (0-2 M NaCl). It exhibited high levels of activity in the presence of DTT, Thiourea, H(2)O(2) as well as in the presence of various detergents such as Span 60, Tween-80, Triton X-100. In addition, the lipase showed a preference for long-chain p-nitrophenyl esters (C(12)-C(18)). These results indicated that this lipase could be a novel cold-active lipase.

Genome sequence of proteorhodopsin-containing sea ice bacterium Glaciecola punicea ACAM 611T.

Here, we report the draft genome sequence of Antarctic sea ice bacterium Glaciecola punicea ACAM 611(T), the type species of the genus Glaciecola. A blue-light-absorbing proteorhodopsin gene is present in the 3.08-Mb genome. This genome sequence can facilitate the study of the physiological metabolisms and ecological roles of sea ice bacteria.

Phylogenetic analyses of bacteria in sea ice at Cape Hallett, Antarctica

Every year, an area of sea ice forms around the continent of Antarctica that is inhabited by communities of microbes. Although the microbial component of this habitat has been postulated to play an ecologically important role in the Southern Ocean, our understanding of the diversity of Antarctic sea-ice bacteria is limited. The aim of this study was to identify bacterial components present in sea ice at Cape Hallett. Total community DNA was isolated from sea-ice cores and the 16S ribosomal RNA genes were amplified by polymerase chain reaction (PCR) using a range of universal and targeted primer sets. PCR products were de-replicated using restriction fragment length polymorphism (RFLP) and distinct RFLP types were sequenced. The major bacterial classes identified consisted of α-proteobacteria, γ-proteobacteria, Cytophaga–Flavobacteria–Bacteroides group and a small number of Gram-positive species. Our findings indicate that the bacterial component of sea ice at Cape Hallett is primarily heterotrophic. Cyanobacteria and Archaea were not detected using the methods and primer sets employed in this study. However, bacteria whose 16S rDNA sequences cluster with species that encode phototrophic genes were detected in our sea-ice samples. This raised the possibility that bacterial phototrophy may occur in Antarctic sea ice.

Coagulation enhancement of exopolysaccharide secreted by an Antarctic sea-ice bacterium on dye wastewater

The purpose of this paper is to study the enhancement of Bsi20310 exopolysaccharide (Bsi20310 EPS, secreted by an Antarctic sea-ice bacterium Pseudoalteromonas sp. Bsi20310), on coagulation of reactive brilliant red X-3B (RX-3B) by ferric chloride. The effect of solution pH, EPS addition timing and NaCl concentration for coagulation of RX-3B was investigated. The results showed that at pH 10, Fe(III) dosage of 55 mg/L, adding 150 mg/L Bsi20310 EPS enhanced the decolorization effectively. NaCl had little effect on the enhancement of Bsi20310 EPS. The EPS had negative surface charge and could combine with positive Fe(III)–dye flocs to form neutralized settleable Fe(III)–dye–EPS flocs. Results of residual Fe(III) concentration and ferric–ferron reaction kinetics indicated that EPS addition led not only more Fe(III) to participate in coagulation but also to form more Fe b (the most effective ferric hydrolysis species) in coagulation. Bsi20310 EPS enhanced Fe(III) coagulation performance by neutralization, bridging and sweeping to improve the floc aggregation.

Low Salinity and High-Level UV-B Radiation Reduce Single-Cell Activity in Antarctic Sea Ice Bacteria

Experiments simulating the sea ice cycle were conducted by exposing microbes from Antarctic fast ice to saline and irradiance regimens associated with the freeze-thaw process. In contrast to hypersaline conditions (ice formation), the simulated release of bacteria into hyposaline seawater combined with rapid exposure to increased UV-B radiation significantly reduced metabolic activity.

High single-cell metabolic activity in Antarctic sea ice bacteria

AME Aquatic Microbial Ecology Contact the journal Facebook Twitter RSS Mailing List Subscribe to our mailing list via Mailchimp HomeLatest VolumeAbout the JournalEditorsSpecials AME 52:25-31 (2008) - DOI: https://doi.org/10.3354/ame01205 NOTEHigh single-cell metabolic activity in Antarctic sea ice bacteria Andrew Martin1,*, Julie A. Hall2, Ronan O’Toole1, Simon K. Davy1, Ken G. Ryan1 1Victoria University of Wellington, PO Box 600, Wellington 6140, New Zealand 2National Institute of Water and Atmospheric Research, PO Box 11-115, Hamilton 3216, New Zealand *Email: andrew.martin@vuw.ac.nz ABSTRACT: Antarctic sea ice bacteria have historically been examined by techniques that measure bulk community properties. In recognition of the complexity of microbial community structure and function, methods are now available to assess the physiological status of individual bacterial cells. We employed 3 assays: Nucleic Acid Double Staining (NADS), modified Vital Stain and Probe (mVSP) and 5-cyano-2,3-ditolyl tetrazolium chloride (CTC) to (1) quantify the cell-specific metabolic status of bacteria present in the bottom of Antarctic fast-ice and (2) determine whether physiological probes can be used to quantify short-term changes in bacterial metabolic activity. Each assay was used in manipulative experiments (<8 h) conducted on bacteria from melted ice cores with dark/light (5 µmol photons m-2 s-1) and the presence/absence of microalgae (filtered, unfiltered samples) as treatment variables. Estimates of cell viability (intact membranes) were >68% (NADS) and >95% (mVSP) of the post-incubation cell count. High cellular rRNA content was observed using fluorescence in situ hybridisation with an average of 80% of DAPI-stained cells hybridising with the general bacterial probe EUB338 (mVSP). An average of 32% of the bacterial cells were undergoing active respiration (CTC+) which is significantly higher than the 2 to 10% level of activity typical for most marine systems. The short-term effect of incubation irradiance or manipulation of microalgal photosynthate was not significant for any assay. Single-cell analysis of melted ice cores suggests that sea ice is among the most productive microbial habitats, while CTC is favoured for establishing a real-time bacterial response in the sea ice ecosystem. KEY WORDS: Sea ice bacteria · Antarctica · Activity · Viability · Physiological probes Full text in pdf format PreviousNextCite this article as: Martin A, Hall JA, O’Toole R, Davy SK, Ryan KG (2008) High single-cell metabolic activity in Antarctic sea ice bacteria. Aquat Microb Ecol 52:25-31. https://doi.org/10.3354/ame01205 Export citation RSS - Facebook - Tweet - linkedIn Cited by Published in AME Vol. 52, No. 1. Online publication date: June 19, 2008 Print ISSN: 0948-3055; Online ISSN: 1616-1564 Copyright © 2008 Inter-Research.

High single-cell metabolic activity in Antarctic sea ice bacteria

High single-cell metabolic activity in Antarctic sea ice bacteria