Skip to main content
Log in

Degradation of the compatible solute trehalose in Ectothiorhodospira halochloris: isolation and characterization of trehalase

  • Original Papers
  • Published:
Archives of Microbiology Aims and scope Submit manuscript

Abstract

Trehalase, which hydrolyzes the disaccharide trehalose to α-d-glucose was isolated and partially purified (124-fold) from the phototrophic halo-alkaliphilic bacterium Ectothiorhodospira halochloris. The molecular mass was determined to be 480,000 and the isoelectric point pH 5.6. Temperature optimum was found to be 40°C and the pH-optimum 7.8–8.1. In spite of its high K m-value of 0.5 M, trehalase of E. halochloris was shown to be specific for trehalose. Trehalase is activated by phosphate which is, however, not involved in the reaction mechanism. The enzyme is activated by the compatible solute betaine and inhibited by salts. In the presence of betaine the K m-value is lowered from 0.5 M to 0.16 M; moreover, betaine partially protects enzymatic activity from salt inhibition. The findings indicate that betaine might regulate the trehalose level in the cells by affecting trehalase activity.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  • BelocopitowE, MaréchalLR (1970) Trehalose phosphorylase from Euglena gracilis. Biochim Biophys Acta 198:151–154

    Google Scholar 

  • BergmeyerHU (1974) Methods of enzymatic analysis, vol VI. Verlag Chemie, Weinheim, pp 163–198

    Google Scholar 

  • BodeR, BirnbaumD (1986) Threonine dehydratase activity from several yeast species is activated and affected by phosphate. FEMS Microbiol Lett 37:189–192

    Google Scholar 

  • BoosW, EhmannU, BremerE, MeddendorfA, PostmaP (1987) Trehalase of Escherichia coli. J Biol Chem 262:13212–13218

    Google Scholar 

  • BradfordMH (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254

    Google Scholar 

  • BrownAD (1976) Microbial water stress. Bacteriol Rev 40:803–846

    Google Scholar 

  • CollinsKD, MashabaughMW (1985) The Hofmeister effect and behaviour of water at interfaces. Quarterly Rev Biophys 18: 323–422

    Google Scholar 

  • CroweJH, CroweLM, ChapmanD (1984) Preservation of membranes in anhydrobiotic organisms: the role of trehalose. Science 223:701–703

    Google Scholar 

  • Cruz MartinM, DiazLA, ManzanalMB, HardissonC (1986) Role of trehalose in spores of Streptomyces. FEMS Microbiol Lett 35:45–54

    Google Scholar 

  • ElbeinAD (1974) The metabolism of α,α-trehalose. Adv Carbo Chem Biochem 30:227–256

    Google Scholar 

  • FriedenC (1970) Kinetic aspects of regulation of metabolic processes. J Biol Chem 245:5788–5799

    Google Scholar 

  • GalinskiEA, HerzogRM (1990) The role of trehalose as a substitute for N-containing compatible solutes (Ectothiorhodospira halochloris). Arch Microbiol 153:607–613

    Google Scholar 

  • GalinskiEA, TrüperHG (1982) Betaine, a compatible solute in the extremely halophilic phototrophic bacterium Ectothiorhodospira halochloris. FEMS Microbiol Lett 13:357–360

    Google Scholar 

  • GalinskiEA, PfeifferHP, TrüperHG (1985) 1,4,5,6-Tetrahydro-2-methyl-4-pyrimidinecarboxylic acid. A novel cyclic amino acid from the halophilic phototrophie bacteria of the genus Ectothiorhodospira. Eur J Biochem 149:135–139

    Google Scholar 

  • ImhoffJF, TrüperHG (1977) Ectothiorhodospira halochloris sp. nov., a new extremely halophilic phototrophic bacterium containing bacteriochlorophyll b. Arch Microbiol 114:115–121

    Google Scholar 

  • KemekuraM (1986) Production and function of enzymes of eubacterial halophytes. FEMS Microbiol Rev 39:145–150

    Google Scholar 

  • LarsenPI, SydnesLK, LandfaldB, StromAR (1987) Osmoregulation in Escherichia coli by accumulation of organic osmolytes: betaines, glutamic acid and trehalose. Arch Microbiol 147: 1–7

    Google Scholar 

  • LopezMF, TorreyJG (1985) Purification and properties of trehalase in Frankia ArI3. Arch Microbiol 143:209–215

    Google Scholar 

  • MackayMA, NortonRS, BorowitzkaLJ (1984) Organic osmoregulatory solutes in cyanobacteria. J Gen Microbiol 130: 2177–2191

    Google Scholar 

  • MaurerJH (1971) Disc electrophoresis and related techniques of polyacrylamid gel electrophoresis. Walter de Gruyter, Berlin New York

    Google Scholar 

  • PollardA, Wyn JonesRG (1979) Enzyme activities in concentrated solutions of glycinebetaine and other solutes. Planta 144:291–298

    Google Scholar 

  • ReedRH, RichardsonDL, WarrSRC, StewartWDP (1984) Carbohydrate accumulation and osmotic stress in cyanobacteria. J Gen Microbiol 130:1–4

    Google Scholar 

  • RudolphAS, CroweJH (1985) Membrane stabilization during freezing: the role of two natural cryoprotectants, trehalose and proline. Cryobiology 22:367–377

    Google Scholar 

  • StreeterJG (1982) Enzymes of sucrose, maltose and α,α-trehalose catabolism in soybean root nodules. Planta 155:112–115

    Google Scholar 

  • TheveleinJM (1984) Regulation of trehalose mobilization in funghi. Microbiol Rev 48:42–59

    Google Scholar 

  • TrüperHG, GalinskiEA (1986) Concentrated brines as habitats for microorganisms. Experientia 42:1182–1187

    Google Scholar 

  • Tschichholz I, Trüper HG (1990) Fate of compatible solutes during dilution stress in Ectothiorhodospira halochloris. FEMS Microbiol Ecol (in press)

  • VanLaereA (1989) Trehalose, reserve and/or stress metabolite. FEMS Microbiol Rev 63:201–210

    Google Scholar 

  • WarrSRC, ReedRH, StewartWDP (1984) Osmotic adjustment of cyanobacteria: the effects of NaCl, KCl, sucrose and glycine-betaine on glutamine synthetase activity in a marine and a halotolerant strain. J Gen Microbiol 130:2169–2175

    Google Scholar 

  • YanceyPH, ClarkME, HandSC, BowlusRD, SomeroGN (1982) Living with water stress: evolution of osmolyte systems. Science 217:1214–1222

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Herzog, R.M., Galinski, E.A. & Trüper, H.G. Degradation of the compatible solute trehalose in Ectothiorhodospira halochloris: isolation and characterization of trehalase. Arch. Microbiol. 153, 600–606 (1990). https://doi.org/10.1007/BF00245272

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00245272

Key words

Navigation