Zymolyase

Yeast Lytic Enzyme

Efficient lysis, lot to lot conformity and high reproducibility

Zymolyase 100T is an enzyme preparation from a submerged culture of Arthrobacter luteus which effectively lyses cell walls of viable yeast cells. This preparation is lyophilized enzyme partially purified by affinity chromatography and contains 100,000 units enzyme/g.
The main enzymatic activity is ß-1,3-glucan laminaripentaohydrolase. It hydrolyzes glucose polymers at the ß-1,3-glucan linkages releasing laminaripentaose as the principal product.

Zymolyase 20T is the same enzyme extract, except that the lyophilized powder is prepared by salting out from the culture fluid with ammonium sulphate and contains 20,000 units enzyme/g.

Lytic Spectrum by Zymolyase

  1. Susceptible strains in low concentration (0.2 units/ml)
    Ashbya, Endomyces, Kloeckera, Kluyveromyces, Pullularia, Saccharomyces
  2. Susceptible strains in high concentration (2.0 units/ml)
    Candida, Debaryomyces, Eremothecium, Hansenula, Hanseniaspora, Lipomyces, Metschikowia, Saccharomycopsis, Saccharomycodes, Schizosaccahromyces, Selenozyma, Trigonopsis, Wickerhamia
  3. Susceptibility depending on strains
    Bretanomyces, Cryptococcus, Nadsonia, Pichia, Rodosporidium, Schwanniomyces, Stephnoascus, Torulopsis
  4. No susceptible strains
    Bullera, Pityrosporum, Rhosotorula, Sporidiobolus, Sporobolomyces, Stetigmatomyces, Trichosporon
Cat. No.
DescriptionAmountBrand
08320931
Zymolyase 100t
500 mg
MP Biomedicals
08320932
Zymolyase 100t
250 mg
MP Biomedicals
08320921
Zymolyase 20t
1 g
MP Biomedicals


Technical Note

Zymolyase sensitivity assay.

Yeast cell integrity depends on a particular external envelope: the cell wall, which is necessary not only for maintaining cell morphology but also for protecting cells from extreme conditions. In response to these changes, precise metabolic pathways are coordinated by the cell. Zymolyase-mediated cell wall damage is one of the stress factors used to better understand the response to environment changes(1) or spore formation process(2). Some yeast lines are pathogens for humans: the Zymolyase sensitivity assay of Candida glabrata has used to understand the resistance mechanism by changing wall composition(5).

Protoplast/Spheroplast preparation.

Fission yeast is the favored tool of many productive research groups throughout the world, serving as a useful model for the study of fundamental mechanisms, such as genome organization, differential gene regulation, cell-cycle control, signal transduction, or cellular morphogenesis. Often, the first step needed before to starting analysis techniques is protoplast preparation. Some recent protocols and procedures are:
  • Immunoprecipitation and western blot analysis(4, 16)
  • Vacuolar membranes vesicles(4), or microsomes preparations(6, 10)
  • Protein purification or chromatin fractionation(7, 14)
  • Mitochondria isolation(8)
  • Immunofluorescence with antibodies(9, 12)
  • Fluorescent in situ hybridation(11)
  • Proteasome extracts(13)
  • Yeast DNA purification(15)
  • Nuclei isolation and DNA purification(17)
  • Cytological DNA analysis by DAPI coloration(3)

Other Zymolyase Applications

Yeast transformation, direct PCR on yeast colony, DNA purification.

References:

  1. Clara Bermejo et al. Mol. Biol. Cell, Mar 2008; 19: 1113 - 1124.
  2. Enrico Ragni et al. Eukaryot. Cell, Feb 2007; 6: 302 - 316.
  3. Farokh Dotiwala et al. PNAS, Jul 2007; 104: 11358 - 11363.
  4. Ming Lu et al. J. Biol. Chem., Aug 2007; 282: 24495 - 24503.
  5. Rupinder Kaur et al. PNAS, May 2007; 104: 7628 - 7633.
  6. Andreas Papadopulos et al. J. Biol. Chem., May 2007; 282: 15559 - 15568.
  7. Swarna Swaminathan et al. Mol. Cell. Biol., Jul 2007; 27: 4674 - 4684.
  8. Andrea Zambrano et al. Mol. Biol. Cell, Feb 2007; 18: 523 - 535.
  9. Sumin Han et al. J. Biol. Chem., Sep 2007; 282: 26140 - 26149.
  10. Stefanie Vehring et al. Eukaryot. Cell, Sep 2007; 6: 1625 - 1634.
  11. Fumitaka Mizuki et al. Genes Cells, Jan 2007; 12: 35 - 47.
  12. Thomas Obermeyer et al. J. Lipid Res., Nov 2007; 48: 2354 - 2364.
  13. Mickael M.J. Cohen et al. Mol. Biol. Cell, Mar 2008; 10.1091/mbc.E08-02-0227.
  14. Jason M. Rizzo et al. J. Biol. Chem., Mar 2007; 282: 8521 - 8532.
  15. Hiroyuki Sasanuma, et al. Nucleic Acids Res., Feb 2007; 35: 1119 - 1133.
  16. Ke Liu, Zhaolin Hua et al. Mol. Biol. Cell, Feb 2007; 18: 487 - 14882.
  17. Mary Baum et al. PNAS, Oct 2006; 103: 14877 - 14882.


Related to:
Brands: MP Biomedicals
Product groups: Proteins / Signaling Molecules