Technical Data

Z1000
CAS Number
37340-57-1
Grade
Molecular Biology Grade
EU Commodity Code
38220090
Shipping Temp
Blue Ice
Storage Temp
4°C
Zymolyase 20T (Lyticase, Yeast Lytic Enzyme)
Arthrobacter luteus

Zymolyase, produced by a submerged culture of Arthrobacter luteus (1), is an enzyme preparation which effectively lyses cell walls of viable yeast cells. An essential enzyme responsible for lysis of viable yeast cells in this preparation is b-1, 3-glucan laminaripentaohydrolase. It hydrolyzes linear glucose polymers with b-1,3-linkages and releases laminaripentaose specifically as the main and minimum product unit (4,5,10,11). This lytic activity releases spheroplasts and protoplasts in the preparation of yeast DNA prior to restriction enzyme digestion and Southern Blot analysis. The extent of lysis of yeast cells by Zymolyase varies with yeast strain, growth stage of yeast and cultural condition (6-8). Further information related to Zymolyase is obtained in the references below.

Source
Arthrobactor luteus
Applications
Protoplast/Spheroplast Preparation Yeast Cell Fusion Yeast Cell Transformation
Appearance
Lyophilized powder
Activity
≥20u/mg
Purity
Purified by ammonium sulfate precipitation.
Unit Definition
One unit of lytic activity is defined as that amount which indicates 30% of decrease in absorbance at 800nm (A800). Refer to Assay for Enzymatic Activity.
Synonyms
Lyticase*, Yeast Lytic Enzyme
Essential Enzyme
b-1,3-glucan laminaripentaohydrolase
Contaminants
DNase, Rnase: Trace levels detected.
Other activities contained
b-1,3-glucanase: ~1.5x10e6u/mg Protease: ~1.0x10e4 units/g Mannanase: 1.0x10e6 units/g Amylase, xylanase, phosphatase: Minute amounts DNase, Rnase: Trace levels detected (See reference No. 3 as to the definition of each enzyme unit. Each activity varies more of less among lots.)
Optimum pH
For cell wall lysis: 7.5, 35°C For yeast glucan hydrolysis: 6.5, 45°C
Stable pH
5-10
Heat Stability
The lytic activity is lost on incubation at 60°C for 5 minutes.
No susceptible strains
Specificity (lytic spectrum)(5): Ashbya, Candida, Debaryomyces, Eremothecium, Endomyces, Hansenula, Hanseniaspora, Kloekera, Kluyveromyces, Lipomyces, Metschikowia, Pichia, Pullularia, Torulopsis, Saccharomyces, Saccharomcopsis, Saccharomycodes, Schwanniomyces, etc Ashbya, Endomyces, Kloekera, Kluyveromyces, Pullularia, Saccharomyces Candida, Debaryomyces, Eremothecium, Hansenula, Hanseniaspora, Lipomyces, Metschnikowia, Saccharomycopsis, Saccharomycodes, Schizosaccharomyces, Selenozyma, Trigonopsis, Wickerhamia Bretanomyces, Cryptococcus, Nadsonia, Picia, Rodosporidium, Schwanniomyces, Stephnoascus, Torulopsis Bullera, Pityosporum, Rhosotorula, Sporidiobolus, Sporobolomyces, Stetigmatomyces, Trichosporon
Activators
SH compound such as cystein, 2-mercaptoethanol of dithiothreitol
Storage and Stability
Stable for 1 year at 4ºC. About 70% of the lytic activity is lost when stored at 30ºC for 3 months.
Companion Products
Z1000: Zymolyase 20T Z1001: Zymolyase 20T Concentrate 50mg/ml, 0.1M Sorbitol Zymolyase 20T shows 20u/mg of the lytic activity, defined after, toward brewer's yeast cells (Saccharomyces cerevisiae, resting stage) or toward yeast cells of Saccharomyces cerevisiae IFO 0565 cultured statically in malt extract medium (Malt extract 2g, peptone 0.5g, water 100ml) at 20ºC for 34 hours.
Z1004: Zymolyase 100T Z1005: Zymolyase 100T Concentrate 10mg/ml, 0.1M Sorbitol Zymolyase 100T, further purified, whose specific activity is 100u/mg.
Note: Zymolyase100T is less soluble than 20T and may not be completely dissolved in buffers. If this is the case use as a suspension.
See useful publication on the use of USBio’s Zymolyase titled
A Comparison of Zymolyase, Lyticase and Glusulase by Dr. David Burden.
Important Note
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.

Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.

References
1. Falcon-Perez, J.M., et al., J. Biol. Chem. 274: 23,584-23,590 (1999). 2. Favre, C., et al., Free Rad. Biol. and Med. 45: 1446-1456 (2008). 3. Albertin, W., et al., J. Evol. Biol. 22: 2157-2170 (2009). 4. Zhang, Y., et al., Mol. Biol. Cell 12: 1303-1314 (2001). General References: 1. Kaneko, T., et al., J. Gen. Appl. Microbiol. 15: 317 (1969). 2. Kitamura, K., et al., Arch. Biochem. Biophys. 145: 402 (1971). 3. Kitamura, K., et al., J. Hen. Appl. Microbiol. 18: 57 (1972). 4. Kitamura, K. & Yamamoto, Y., Arch. Biochem. Biophys. 153: 403 (1972). 5. Kaneko, T., et al., Agric. Biol. Chem. 37: 2295 (1973). 6. Kitamura, K., et al., J. Gen Appl. Microbiol. 20: 323 (1974). 7. Kitamura, K. & Yamamoto, Y., Agric. Biol. Chem. 45: 1761 (1981). 8. Katamura, K. & Tanabe, K., Agric, Biol. Chem. 46: 553 (1982). 9. Katamura, K., J. Ferment. Technol. 60: 257 (1982). 10 Kitamura, K., Agric. Biol. Chem. 46: 963 (1982). 11. Kitamura, K., Agric. Biol. Chem. 46: 2093 (1982). 12. Calza, R.E. & Schroeder, A.L., J. Ben. Microbiol. 129: 413 (1983). 13. Iizuka, M., et al., Agric. Biol. Chem. 47(12): 2767 (1983). 14. Shibata, N., et al., Arch. Biochem. Biophys. 251(2): 697 (1986). 15. Iijima, Y. & Yanagi, S.O., Agric. Biol. Chem. 50(7): 1855 (1986). 16. Herrero, E., et al., J. Gen. Microbiol. 133(10): 2895 (1987). 17. Yamamoto, M. & Fukui, S., Agric. Biol. Chem. 41: 1829 (1977). 18. Hsiao, C. & Carbon, J., Proc. Natl. Acad. Sci. USA 76: 3829 (1979). 19. Arima, K. & Takano, I., Molec. Gen. Genet. 173: 271 (1979). 20. Sambrook, et al., Molecular Cloning, 2nd Edition, 18.36-18.37 (1989). 21. Ausubel, et al., Current Protocols in Molecular Biology, 2nd Ed., A1-64, 13-12, 13-42.
USBio References
US Biological Application References: 1. Falcon-Perez, J.M., et al., J. Biol. Chem. 274: 23,584-23,590 (1999). 2. Favre, C., et al., Free Rad. Biol. and Med. 45: 1446-1456 (2008). 3. Albertin, W., et al., J. Evol. Biol. 22: 2157-2170 (2009). 4. Zhang, Y., et al., Mol. Biol. Cell 12: 1303-1314 (2001).
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