Zymolyase 20T (Lyticase, Yeast Lytic Enzyme)

Referência Z1000-100mg

Tamanho : 100mg

Marca : US Biological

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Z1000 Zymolyase 20T (Lyticase, Yeast Lytic Enzyme)

Clone Type
Polyclonal
Grade
Molecular Biology Grade
Shipping Temp
Blue Ice
Storage Temp
4°C

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.||Properties of Zymolyase:|Specificity (lytic spectrum)(5): Ashbya, Candida, Debaryomyces, Eremothecium, Endomyces, Hansenula, Hanseniaspora, Kloekera, Kluyveromyces, Lipomyces, Metschikowia, Pichia, Pullularia, Torulopsis, Saccharomyces, Saccharomcopsis, Saccharomycodes, Schwanniomyces, etc|Susceptible strains in low concentration (0.2 units/ml):|Ashbya, Endomyces, Kloekera, Kluyveromyces, Pullularia, Saccharomyces|Susceptible strains in high concentration (2.0 units/ml):|Candida, Debaryomyces, Eremothecium, Hansenula, Hanseniaspora, Lipomyces, Metschnikowia, Saccharomycopsis, Saccharomycodes, Schizosaccharomyces, Selenozyma, Trigonopsis, Wickerhamia|Susceptibility depending upon strains:|Bretanomyces, Cryptococcus, Nadsonia, Picia, Rodosporidium, Schwanniomyces, Stephnoascus, Torulopsis|No susceptible strains:|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.

Applications
* Lyticase is similar but testing has shown that Zymolyase exhibits greater lytic activity.||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.
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.

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