109
Views
56
CrossRef citations to date
0
Altmetric
Research Article

Microbial β-Glucanases Different from Cellulases

&
Pages 275-304 | Published online: 27 Sep 2008

References

  • Haliwell G. Microbial β-glucanases. Progress in Industrial Microbiology, H. J. Bull. Pergamon Press, Elmsford, NY 1975; Vol. 15
  • Shiota M., Nakajima T., Satoh A., Shida M., Matsuda K. Comparison of β-glucan structures in a cell wall mutant of Saccharomyces cerevisiae and the wild type. J. Biochem 1985; 98: 1301
  • McClear B. V., Glennic-Holmes M. Enzymic qualification of (1–3)(1–4)-β-D-glucan in barley and malt. J. Inst. Brew 1985; 91: 285
  • Yalpani M. Polysaccharides, Synthesis, Modification and Structure/Property Relations. Elsevier, Amsterdam 1988
  • Bull A. T., Chesters C. G. C. The biochemistry of laminarin and the nature of laminarinase, Advances in Enzymology, F. F. Nord. Interscience, New York 1963; Vol. 28: 325
  • Mann J. W., Jeffries T. W., Macmillan J. D. Production and ecological significance of yeast cell wall degrading enzymes from Oerskovia. Appl. Environ. Microbiol 1978; 36: 594
  • Eukenlund J. Externally added beta-glucanase, Process. Biochem 1972; 7: 27
  • Fogarty W. M., Griffin P. J., Joyce A. M. Enzymes of, Bacillus species. Process Biochem 1974; 9: 11
  • Wieg A. J. Technology of barley brewing. Process Biochem 1970; 5: 46
  • Kobayashi R. K., Miwa T., Yamamoto S., Nagasaki S. Preparation and evaluation of an enzyme which degrades yeast cell walls. Eur. J. Appl. Microbiol. Biotechnol 1982; 15: 14
  • Jamas R., Rha C. K., Sinskey A. J. Morphology of yeast cell wall as affected by genetic manipulation of β-(1–6)-glucosidic linkage. Biotech. Bioeng
  • Asenjo J. A., Andrews B. A., Hunter J. B., Lecorre S. Microbial cell lytic enzyme systems: production and reaction kinetics, Process. Biochem 1985; 10: 158
  • Kitamura K. A high yeast cell wall lytic enzyme producing mutant of Arthrobacter luteus. J. Ferm. Technol 1982; 60: 253
  • Misaki A., Johanson J. J., Kirkwood S., Scaletti J. V., Smith F. Structure of the cell wall glucan of yeast. Carbohydr. Res 1968; 6: 150
  • Manners D. J., Masson A. J., Patterson J. C. The structure of a β-(1–3)-D-glucan from yeast cell walls. Biochem. J 1973; 135: 19
  • Manners D. J., Masson A. J., Patterson J. C. The structure of a β-(1–6)-D-glucan from yeast cell walls. Biochem. J 1973; 135: 31
  • Bacon J. S. D., Farmer V. C., Jones D., Taylor I. F. The glucan components of the cell wall of baker's yeast (Saccharomyces cerevisiae) considered in relation to its infrastructure. Biochem. J 1969; 114: 557
  • Fleet G. M., Manners D. J. Isolation and composition of an alkali-soluble glucan from the cell walls of, Saccharomyces cerevisiae. J. Gen. Microbiol 1976; 941: 180
  • Fleet G. H., Manners D. J. The enzymic degradation of an alkali-soluble glucan from the cell walls in Saccharomyces cerevisiae. J. Gen. Microbiol 1977; 98: 315
  • Wolska-Mitaszko B. Metabolism of yeast cell wall polymers, I. Metabolism of glucans. Postepy Mikrobiol 1985; 25/3: 187
  • Mac William I. C. The structure, synthesis and functions of yeast cell wall. J. Inst. Brew 1970; 76: 524
  • Houwink A. L., Kreger D. R. Observation on the cell wall of yeasts. An electron microscope and X-ray diffraction study, Antonie van Leeuwenhoek. J. Microbiol. Serol 1953; 19: 233
  • Kreger D. R., Kopecka M. On the nature and formation of the fibrillar nets produced by protoplasts of Saccharomyces cerevisiae in liquid media: an electronmicroscopic X-ray diffraction and chemical study. J. Gen. Microbiol 1976; 92: 207
  • Necas Q. Cell wall synthesis in yeast protoplasts. Bacteriol. Rev 1971; 35: 149
  • Shematek E. M., Cabib E. Biosynthesis of the yeast cell wall. II. Regulation of β(1–3)glucan synthetase by ATP and GTP. J. Biol. Chem 1980; 255: 895
  • Sietsma J. H., Wessels J. G. H. Chemical analysis of the hyphal wall of, Schizophyllum commune. Biochem. Biophys. Acta 1977; 496: 225
  • Grimmecke H. D., Meyer H., Scheller D., Reuter G. Struktur der Zellwandpolysaccharide in der Futtereiweiss-Hefe. Candida spec. H. Z. Allg. Mikrobiol 1981; 21: 201
  • Bush D. A., Horisberger M., Horman I., Wursh P. The wall structure of Schizosaccharomycespombe. J. Gen. Microbiol 1974; 81: 199
  • Manners D. J., Meyer M. T. The molecular structures of some glucans from the cell walls of Schizosaccharomyces pombe. Carbohydr. Res 1977; 57: 189
  • Lee T. H., Arai M., Murao S. Structure of fucogalactomannan of red yeast cell wall. Agr. Biol. Chem 1981; 45(6)1301
  • Lampen J. O. External enzymes of yeast: their nature and formation. Antonie van Leeuwenhoek. J. Microbiol. Serol 1968; 34: 1
  • Kid D. K., Davies R. Invertase and disulfide bridges in the yeast wall. J. Gen. Microbiol 1970; 61: 327
  • Zlotnik H., Fernandez M. P., Bowers B., Cabib E. Saccharomyces cerevisiae mannoproteins form an external cell wall layer that determines wall porosity. J. Bacterial 1984; 159: 1018
  • Shibata N., Mizugami K., Takano K., Suzuki S. Isolation of mannoprotein complexes from viable cells of Saccharomyces cerevisiae X2180–1A wild type and Saccharomyces cerevisiae X2180–1A-5 mutant strains by the action of zymolyase 60000. J. Bacteriol 1983; 156: 552
  • Bacon J. S. P., Gordon A. N., Jones D., Taylor I. F., Webley D. M. The separation of β-glucanases produced by Cytophage johnsonii and their role in the lysis of yeast cell walls. Biochem. J 1970; 120: 67
  • Cabib E., Roberts R., Bowers B. Synthesis of the yeast cell wall and its regulation. Annu. Rev. Biochem 1982; 51: 763
  • Barkai-Golan R., Sharon M. Lectins as a tool for the study of yeast cell walls. Exp. Mycol 1978; 2: 110
  • Hayasibe M., Kathoda S. Initiation of budding and chitin ring. J. Gen. Appl. Microbiol 1973; 19: 23
  • Vrsanska M., Kratky Z., Biely P., Machala J. Chitin structures of the ceil walls of synchronously grown virgin cells of Saccharomyces cerevisiae. Z. Allg. Mikrobiol 1979; 19: 357
  • Molano J., Bowers B., Cabib E. Distribution of chitin in the yeast cell wall. An ultrastructural and chemical study. J. Cell Biol 1980; 85(2)199
  • Takahashi F., Harada T., Koreeda A., Harada A. Structure of curdlan that is resistant to 1,3-β-D-glucanase. Carbohydr. Polym 1986; 6: 407
  • Harada T. Succinoglucan and gel-forming beta-1,3-glucan. Process Biochem 1974; 1: 21
  • Kanazawa Y., Harada T., Koreeda A., Harada A. Difference of molecular association in two types of curdlan gel. Carbohydr. Polym 1989; 10: 299
  • Kanazawa Y., Harada T., Koreeda A., Harada A. Curdlan gel formed by neutralizing its alkaline solution. Agric. Biol. Chem 1987; 51: 1839
  • Kanazawa Y., Koreeda A., Harada A., Harada T. Electron microscopy of the gel-forming ability of polysaccharide food additives. Agric. Biol. Chem 1989; 53: 979
  • Fulton W. S., Atkins E. D. T. Fiber Diffraction Method, A. D. French, K. H. Garner. ACS Symp. Ser., 141, 1980; 363
  • Cantwell B. A., Ryan T., Hurley J. C., Doherty M., McConnel D. J. Degradation of barley 0-glucan by brewers' yeast. European Brewery Convention-Symposium, Helsinki, Monograph 12. 1986; 186
  • Tvaroska J., Ogawa Y., Deslandes Y., Marchessault R. H. Crystalline conformations and structure of lichenan and barley β-glucan. Can. J. Chem 1983; 61: 1608
  • Slodkl M. E., Wickerham L. J. Extracellular polysaccharides and classification of the genus Lypomyces. J. Gen. Microbiol 1966; 42: 381
  • Bluhm T. L., Deslandes Y., Marchessault R. H., Perez S., Rlnaudo M. Solid state and solution conformation of scleroglucan. Carbohydr. Res 1982; 100: 117
  • Chihara G., Maeda Y. Y., Hamuro J., Sasaki T., Fukuoka F. Inhibition of mouse sarcoma 180 by the polysaccharides from Lentinus edodes (Berk.) Sing. Nature 1969; 222: 687
  • Chihara G., Hamuro J., Maeda Y. Y., Arai Y., Fukuoka F. Fractionation and purification of the polysaccharides with marked antitumor activity, especially lentinan from Lentinus edodes (Berk.) Sing. Cancer Res 1970; 30: 2776
  • Sasaki T., Takasuka N. Further study of lentinan, an antitumor polysaccharide from Lentinus edodes. Carbohydr. Res 1976; 47: 99
  • Chihara G., Maeda Y. Y., Hamuro J. Current status and perspectives of immunomodulators of microbial origin. Int. J. Tiss. Reac 1982; IV(3)207
  • Kikumoto S., Miyazima T., Kimura K., Okubo A., Komatsu N. Study on the polysaccharide produced by Schizophyllum commune. Jap. J. Agr. Chem 1971; 4: 162
  • Norisue T., Yanaki T., Fujita H. Triple helix of a Schizophyllum commune polysaccharide in aqueous solution. J. Polymer Sci 1980; 18: 547
  • Duffus C. M., Duffus J. H. Carbohydrate metabolism in plants. PWRIL, Warsaw 1988, (in Polish)
  • Abd-EI-AI A. T., Phaff H. J. Exo-β-glucanases in yeast. Biochem. J 1968; 109: 347P
  • Rey R. J., Villa T. G., Santos T., Garcia-Acha I., Nombela C. Purification and partial characterization of a new sporulation specific, exo-β-glucanase from Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun 1982; 105: 1347
  • Mori H., Yomamoto S., Nagasaki S. Multiple forms of the lytic glucanase of Flavobacterium dormitator var. glucanolyticae, and the properties of the main component enzyme. Agr. Biol. Chem 1977; 41: 611
  • Nagasaki S., Fukujama I., Yamamoto S., Kobayashi R. Enzymic and structural properties of crystalline yeast cell lytic enzyme from a species of, Fungi Imperfecti. Agr. Biol. Chem 1974; 38: 349
  • Fleet G. H., Phaff H. J. Glucanases in Saccharomyces Isolation and properties of the cell wall associated (1–3)-β-glucanases. J. Biol. Chem 1974; 249: 1717
  • Kabayashi Y., Tanaka H., Ogasawara N. Multiple β-1,3-glucanases in the lytic enzyme complex of Bacillus circulans WL 12. Agr. Biol. Chem 1974; 38: 959
  • Villa T. G., Notario V., Villaneuva I. R. Occurrence of an endo-1,3-beta-glucanase in culture fluids of the yeast Candida utilis Purification and characterization of the enzyme activity. Biochem. J 1979; 177: 107
  • Vrsanska M., Kratky Z., Biely P. Lysis of intact yeast cell and isolated cell walls by inducible enzyme system of Arthrobacter GJM-1. Z. Allg. Mikrobiol 1977; 17: 391
  • Kitamura K., Yamamoto Y. Purification and properties of an enzyme, Zymolyase which lyses viable yeast cells. Arch. Biochem. Biophys 1972; 153: 403
  • Rombouts F. M., Phaff H. J. Lysis of yeast cell walls. Lytic β-(1,3)-glucanases from Bacillus circulans WL-12. Eur. J. Biochem 1976; 63: 109
  • Meyer M. T., Phaff H. J. Survey of α(1,3)-glucanase activity among yeasts. J. Bacteriol 1977; 131: 702
  • Fleet G. H., Phaff H. J. Glucanases in Saccharomyces. Isolation and properties of an exo-β-glucanase from the cell extracts and culture fluid of Schizosaccharomyces japonkus var., varsatilis. Biochem. Biophys. Acta 1975; 401: 318
  • Notario V., Villa T. G., Villaneuva J. R. Purification of an exo-β-D-glucanase from cell free extracts of, Candida utilis. Biochem. J 1976; 159: 555
  • Rombouts F. M., Phaff J. M. Lysis of yeast cell walls. Lytic β-(1–6)-glucanase from Bacillus circulans WL-12. Eur. J. Biochem 1976; 63: 121
  • Firantene R. K., Avizhenis V. Ju., Tiunova N. A. Purification and some properties of 1,3–1,4-beta-glucanase from, Bacillus subtilis. Biokhimiya 1980; 46(4)603
  • Borris R., Noack D., Genther R. Beta-1,3–1,4-glucanase in spore-forming microorganisms VI. Genetic instability of beta-glucan-ase production in a high producer strain of Bacillus amyloliquefaciens grown in a chemostat. Z. Allg. Mikrobiol 1982; 22: 293
  • Martin D. F., Priest F. G., Todd C., Goodfellow M. Distribution of β-glucanases within the genus, Bacillus. Appl. Environ. Microbiol 1980; 40: 1136
  • Santos T., Sanchez M., Villaneuva J. R., Nombela C. Regulation of the beta-1,3-glucanase system in Penicillium italicum: glucose repression of the various enzymes. J. Bacteriol 1978; 133: 465
  • Santos T., Villaneuva J. R., Nombela C. Regulation of beta-1,3-glucanase synthesis in, Penicillium italicum. J. Bacteriol 1978; 133: 542
  • Santos T., Nombela C., Villanoeva J. R., Larriba G. Characterization and synthesis regulator of Penicillium italicum 1, 3-β-glucanase. Arch. Mikrobiol 1979; 121: 265
  • Lahoz R., Fuensanta Reyes, Gomez P., Martinez M. J. Lytic enzyme activity in autolysing mycelium of Aspergillus niger. Z. Allg. Mikrobiol 1983; 23: 17
  • Sharma A., Nakas J. P. Preliminary characterization of I am-inarinase from Trichoderma langibranchiatum. Enzyme Microb. Technol 1987; 9: 89
  • Kitamato Y., Kono R., Shimotari A., Mori N., Ichikawa Y. Purification and some properties of an exo-β-1,3-glucanase from, Trichoderma harzianum. Agric. Biol. Chem 1987; 51: 3385
  • Bamforth Ch. W. The adaptability, purification and properties of exo-β-1,3-glucanase from the fungus, Trichoderma reesei. Biochem. J 1980; 191: 863
  • Merc M., Galas E. β-1,3-glucanase from Trichoderma viride. Purification and characterization. Acta Biotechnol 1984; 4: 67
  • Bielecki S., Galas E. 1,3-β-glucanase from cellulase “Onozuka” SS and its lytic capability. Bioconversion of Cellulosic Substances into Energy, Chemicals and Microbiol. Protein, T. K. Ghose. Symposium IIT, New Delhi 1977; 203
  • Kitamoto Y., Kono R., Shimotori A., Mori N., Ichikawa Y. Purification and some properties of an exo-β-1,3-glucanase from, Trichoderma harzianum. Agric. Biol. Chem 1987; 51: 3385
  • Dubourdieu D., Desphangues C., Villettaz J. C., Ribereau-Gayon P. Investigations of an industrial β-glucanase from, Trichoderma harzianum. Carbohydr. Res 1985; 144: 227
  • Tiunova N. A., Zhloba N. M., Sidorova I. I. Biosynthesis of beta-glucanases and chitinase in the culture of Trichoderma viride mycophilic strain. Mikrobiologija 1983; 52650: 723
  • Copa-Patino J. L., Monistrol I. F., Laborda F., Perez-Leblic M. I. Characterization of 1,3-β-glucanases produced during autolysis of Penicillium oxalicum in different culture media. Trans. Br. Mycol. Soc 1987; 88: 317
  • Perez-Leblic M. I., Copa J. L., Arias M. E., Reyes F., Laborda F. 1,3-β-Glucanases in the autolysis of Penicillium oxalicum. Trans. Br. Mycol. Soc 1985; 84: 467
  • Schep G. P., Shepherd M. G., Sullivan P. A. Purification and properties of a β-1,6-glucanase from, Penicillium brefeldianum. Biochem. J 1984; 223: 707
  • Clark D. R., Johnson J., Jr., Chung K. H., Kirkwood S. Purification, characterization and action pattern studies on the endo-(1–3)-β-D-glucanase from Rhizopus arrhizus QM 1032. Carbohydr. Res 1987; 61: 457
  • Yamamoto S., Shiraishi T., Nagasaki S. Crystalline enzyme which degrades the cell wall of living yeasts. Biochem. Biophys. Res. Commun 1972; 46: 1802
  • Yamamoto S., Kobayashi R., Nagasaki S. Purification and properties of an endo-β-1,6-glucanase from Rhizopus chinensis R-69. Agr. Biol. Chem 1974; 38: 1493
  • Ridout C. J., Coley-Smith J. R., Lynch J. M. Enzyme activity and electrophoretic profile of extracellular protein induced in Trichoderma sp. by cell walls of Rhizoctonia solani. J. Gen. Microbiol 1986; 132: 2345
  • Totsuka A., Usui T. Separation and characterization of the endo-β-(1–3)-D-glucanases from Rhizoctonia solani. Agric. Biol. Chem 1986; 50: 543
  • Hiura N., Kabayashi M., Nakajima T., Matsuda K. Purification and some properties of two-wall associated 1,3-β-glucanases from Neurospora crassa cells. Agric. Biol. Chem 1986; 50: 2451
  • Hiura N., Nakajima T., Matsuda K. Purification and some properties of an endo-β-1,6-glucanase from Neurospora crassa. Agric. Biol. Chem 1987; 51: 3315
  • Ohno N., Hashimoto Y., Yadomes T. Purification and properties of an exo-(1–3)-β-D-glucanase from the culture filtrate of, Mucor hiemalis. Carbohydr. Res 1986; 158: 217
  • Ryan E. M., Ward O. P. Studies on the production and properties of the yeast lytic enzyme of Basidiomycete sp. QM 806. Biotechnol. Lett 1987; 9: 405
  • Tsujisaka Y., Hamada N., Kobayashi R. Purification and some properties of an exo-β-1,3-glucanase from Basidiomycete species. Agric. Biol. Chem 1981; 45: 1201
  • Bielecki S., Antczak T., Galas E. 1,3-β-glucanase from Streptomyces sp. 1228. Third European Congress on Biotechnology. Verlag Chemie, Weinheim 1984; Vol. II: 489
  • Bielecki S., Wnuk M., Szczesna M., Bobowicz-Lassocinska T., Antczak T., Galas E. 1,3-β-glucanases from Streptomyces sp. 1228 lytic enzyme system. Biotech. Lett 1989; 11: 281
  • Bielecki S., Antczak T., Wnuk M., Bobowicz-Lassocinska T., Galas E. Specificity of 1,3-β-glucanases from the lytic system of Streptomyces sp. 1228. Biotech. Lett 1989; 11: 287
  • Scott J. H., Schekman R. Lyticase: endoglucanase and protease activities that act together in yeast cell lysis. J. Bacterial 1980; 142: 414
  • Kusama S., Kusakabe I., Murakami K. Purification and some properties of β-1,3-glucanase from Streptomyces sp. Agric. Biol. Chem 1986; 50: 1101
  • Beyer M., Diekman H. The laminarinase system of Streptomyces sp 1TCC 11238. Appl. Microbiol. Biotechnol 1984; 20: 207
  • Kusama S., Kusakabe I., Murakami K. Studies on the β-1,3-glucanase system of Streptomyces. Part II. A preparation method of gentiobiose from curdlan using the enzyme system from Streptomyces sp. Agric. Biol. Chem 1984; 48: 2655
  • Ahmed T. H., Abd-EI-AI A. T., Phaff H. J. Purification and properties of endo-β-glucanase in the yeast, Hanseniaspora valbyenis. Can. J. Microbiol 1969; 15: 697
  • Zaikina I. V., Tiunova N. A., Kobzeva N. Ya., Berborodow A. M. Study of some properties of exo-1,3-β-glucanases from, Geotrichum candidum 3c. Prikl. Biokhim. Mikrobiol 1985; 21: 461
  • Zaikina I. V., Tiunova N. A., Kobzeva N. Ya. Purification and some properties of 1,3-β-glucanases of the fungus. Geotrichum candidum 3c, Prikl. Biokhim. Mikrobiol 1985; 21: 203
  • Marshall J. J. Studies on the structure and mechanism of action of glucoside hydrolases. Carbohydr. Res 1974; 34: 289
  • Takahaski M., Kamuro M., Sautome S.-I. Purification and properties of β-1,3-glucanase from Lentinus lepideus. J. Ferment. Technol 1978; 56: 499
  • Boderman J., Heiniger U., Hohl H. R. Extracellular enzymes of Phytophora infestans: endo-cellulose, β-glucosidase and 1,3-β-glu-canases. Can. J. Microbiol 1985; 31: 76
  • Fleet G. H. The occurrence and function of endogenous or wall-degrading enzymes in yeast. Microbial Cell Wall Synthesis and Autolysis, C. Nombela. Elsevier, Amsterdam 1984; 227
  • Villaneuva J. R., Gacto M., Duran A. Endogenous lytic enzymes and the yeast cell wall, in Advances in Protoplast Research. Proc. Nat. Acad. Sci. U.S.A 1979; 68: 2627
  • Phaff H. J. A retrospective and current view on endogenous β-glucanases in yeast. Advances in Protoplast Research, Proc. 5th Int. Protopl. Symp. Hungarian Academy of Sciences, Budapest 1979; 171
  • Arnold W. M. Enzymes in Yeast Cell Envelopes: Biochemistry, Biophysics and Ultrastructure, W. N. Arnold. CRC Press, Boca Raton, FL 1981; Vol. 2: 1
  • Villa T. G., Lachance M. A., Phaff H. J. β-glucanases of the yeast Kluyveromyces phaseolosporus, Partial purification and characterization. Exp. Mycol 1978; 2: 12
  • Molina M., Cenamor R., Nombela C. Exo-1,3-β-glucanase activity in Candida albicans: effect of yeast to mycelium transition. J. Gen. Microbiol 1987; 133: 609
  • Santos T. E., Rey F. J., Code J. R., Villanueva J. R., Nombala C. Saccharomyces cerevisiae mutant defective in exo-1,3-β-glucanase production. J. Bacterial 1979; 139: 333
  • Reichlet B. Y., Fleet G. M. Isolation, properties, function and regulation of endo-1,3-β-glucanases in Schizosaccharomyces pombe. J. Bacterial 1981; 147: 1085
  • Hien N. H., Fleet H. G. Separation and characterization of six 1,3-β-glucanases from Saccharomyces cerevisiae. J. Bacteriol 1983; 156: 1204
  • Hien N. H., Fleet H. G. Variation of 1,3-β-glucanase in Saccharomyces cerevisiae during vegetative growth, conjugation and sporulation. J. Bacteriol 1983; 156: 1214
  • Notario V. β-Glucanases from Candida albicans: purification, characterization and the nature of their attachment to cell wall components. J. Gen. Microbiol 1982; 128: 747
  • Cenamor R., Molina M., Galdoma J., Sanchez M. Production and secretion of Saccharomyces cerevisiae β-glucanases: differences between protoplast and periplastic enzymes. J. Gen. Microbiol 1987; 133: 619
  • Notario V., Villa T. G., Villanueva J. R. Purification of an exo-β-glucanase from cell free extracts of Candida utilis. Biochem. J 1976; 159: 555
  • Villa T. G., Notario V., Villaneuva J. R. Direct chemical proof of different glycosylation patterns for yeast exo- and endo-1,3-β-glucanases. J. Gen. Microbiol 1978; 109: 371
  • Nombela C. Exoglucanases in Saccharomyces cerevisiae: chemical nature, regulation, secretory pathway and cellular location. Microbial Cell Wall Synthesis and Autolysis, C. Nombela. Elsevier, Amsterdam 1984; 239
  • Sanchez A., Villaneuva J. R., Villa T. G. Saccharomyces secretes 2 exo-β-glucanases. FEBS Lett 1982; 138: 209
  • Sanchez A., Villaneuva J. R., Villa T. G. Saccharomyces cerevisiae secretes 2 exo-β-glucanases. J. Gen. Microbiol 1982; 128: 3051
  • Kilker R. D., Saunier B., Tkacz J. S., Quaroni A., Hercovies A. Partial purification from Saccharomyces cerevisiae of a soluble glucosidase which removes the terminal glucose from the oligosaccharide Glc3Man9GlcNAc2. J. Biol. Chem 1982; 257: 14155
  • Cartert M., Matile P., Wiekman A. The isolation of glucanase-containing resides from budding yeast. Arch. Microbiol 1972; 82: 189
  • Del Rey F. J., Garcia-Acha L., Nombela C. Synthesis of p glucanase during sporulation in Saccharomyces cerevisiae: formation of a new, sporulation-specific 1,3-β-glucanase. J. Bacteriol 1979; 139: 924
  • Brock T. D. Enzyme synthesis, during conjugation in the yeast Hansenula wingei. J. Cell. Biol 1964; 23: 15A
  • Fleet G. H., Phaff H. J. Effects of glucanases of yeast and bacterial origin on cell walls of Schizosaccharomyces species. Yeast, Mould and Plant Protoplasts, J. K. Villanueva, I. Garcia-Acha, S. Gascon, F. Uruburu. Academic Press, London 1973; 33
  • Crandall M., Egel R., Mackay V. L. Physiology of mating in the yeasts. Adv. Microb. Physiol 1977; 15: 307
  • Rey F. J., Santos T., Garcia-Acha I., Nombela C. Synthesis of β-glucanases during sporulation in Saccharomyces cerevisiae: formation of new, sporulation specific 1,3-β-glucanase. J. Bacteriol 1979; 143: 621
  • Rey F. J., Villa T. G., Santos T. E., Garcia-Acha J., Nombela C. Purification and partial characterization of a new sporulation specific exoglucanase from Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun 1982; 105: 1347
  • Ram S. P., Romana L. K., Shepherd M. G., Sullivan P. A. Exo-1,3-β-glucanase autolysis and trehalase activities during yeast growth and germ tube formation in Candida albicans. J. Gen. Microbiol 1984; 130: 1227
  • Rey F., Garcia-Acha J., Nonivela C. The regulation of 3-glucanase synthesis in fungi and yeast. J. Gen. Microbiol 1979; 110: 83
  • Friebe B., Halldorf A. W. Control of extracellular β-1,3-glu-canaseactivity in abasidiomycte species. J. Bacterial 1975; 122: 818
  • Lilley G., Ball A. T. The production of β-1,3-glucanase by thermophilic species of, Streptomyces. J. Gen. Microbiol 1974; 83: 123
  • Rosa E., Nebreda A. R., Villa T. G. Synthesis and regulation of Bacillus circulans WL-12 1,3-β-glucanases. J. Gen. Microbiol 1984; 130: 2483
  • Kitamura K. A high zymolase producing mutant of, Arthrobacter luteus. Rep. Res. Lab. Kirin Brew. Co 1985; 28: 29
  • Andrews B. A., Asenjo J. A. Synthesis and regulation of extracellular β(1–3)glucanase and protease by Cytophaga sp. in batch and continuous culture. Biotech. Bioeng 1986; 28: 1366
  • Andrews B. A., Asenjo J. A. Production of enzymic systems in continuous culture for the controlled lysis of microbial cells. Ann. N.Y. Acad. Sci 1987; 637
  • Bielecki S. Biosynthesis and characterization of 1,3-β-glucanases from the lytic enzyme system of Streptomyces sp. 1228 and their activity in yeast zymolysis. Sci. Bull., Lodz Tech. Univ 1989; 544: 84
  • Hampel W., John E. A kinetic study on the formation of enzymes in Arthrobacter sp. with lytic action on yeast cell wall compounds. Current Developments in Yeast Research, Advances in Biotechnology, G. G. Stewart, J. Russel. Pergamon Press, Canada 1981; 381
  • Rose H. A. History and scientific basis of commercial exploitation of microbial enzymes and bioconversions. Microbial Enzymes and Bioconversions. Economic Microbiology, A. H. Rose. Academic Press, London 1981; Vol. 5: 25
  • Tanaka H., Kobayashi K., Hakura K., Kamimiya S. Concerted induction of cell wall lytic enzymes in Bacillus circulans. Current Developments in Yeast Research, Advances in Biotechnology, G. G. Stewart, J. Russel. Pergamon Press, Canada 1981; 503
  • Moore A. F., Stone B. A. A β-1,3-glucan hydrolase from Nicotiana glutinosa, II. Specificity, action pattern and inhibitor studies. Biophys. Acta, 258: 248
  • Tiunova N. A., Kobzeva N. Y. Endo-1,3-β-glucanase from, Actinomycetes cellulosae. Biokhimiya 1981; 46: 1175
  • Elyakova L. A., Zvyagintseva T. N. Kinetic peculiarities in the action of 1,3-β-glucanases from different sources. Bioorg. Khim 1981; 7: 680
  • Nazarova N. J., Mazur A. K., Elyakova L. Active sites of the endo-1,3-β-glucanases from Spisula sachalinensis and, Chlamys albidus. Bioorg. Khim 1986; 12: 1478
  • Elyakova L. A., Zvyagintseva T. N., Privalova N. M. Comparative characterization and studies on the active site sorption properties of endo-1,3-β-glucanases from marine invertebrates. Bioorg. Khim 1978; 4: 1553
  • Jeffcoat R., Kirk wood S. Implication of histidine at the active site of exo-1,3–1-D-glucanase from Basidiomycetes sp. QM 806. J. Biolog. Chem 1987; 262: 1088
  • Ohno N., Gotoh Y., Hashimoto Y., Yadomae T. Examination of the active center of 1,3-β-D-glucanase preparation, Zymolyase. Chem. Pharm. Bull 1988; 36: 1007
  • Moore A. F., Stone C. A. A β-1,3-glucan hydrolase from Nicotiana glutinosa I: Extraction, purification and physical properties. Biochem. Biophys. Acta, 258: 238
  • Bang K. W., Song H. I., Kim J. K., Yu T. S., Chung K. T. Purification and properties of 1,3-β-glucanases from Pseudomonas stutzeri KF13. Misaengmul Makhoechi 1987; 25: 1
  • Rafalovskaya T. Ya., Shishkova E. A., Oreschenko L. I. Some properties of β-glucanase of, Bacillus subtilis. Prikl. Biokim. Mikrobiol 1986; 22: 622
  • Bamforth C. W., Martin H. L. β-glucan and β-glucan solubilase in malting and mashing. J. Inst. Brew 1981; 87: 365
  • Enari T.-M., Markkanen P. H. Microbiol β-glucanases in brewing. Proc. Am. Soc. Brew. Chem 1975; 33: 17
  • Borris R., Baumlein H., Hofemeister J. Expression in Escherichia coli of a cloned β-glucanase gene from, Bacillus amyloique-faciens. Appl. Microbiol. Biotechnol 1985; 22: 63
  • Borris R., Zemek J., Augustin J., Pacova Z., Kuniak L. β-1,3–1,4-Glucanase in sporeforming microorganisms. II. Production of B-glucan-hydrolases by various Bacillus species. Zentralbl. Bakteriol., Abt 1980; 2: 135, 435
  • Cant well B. A., Brazil G., Murphy N., McConnel D. J. Comparison of expression of the endo-β-1,3–1,4-glucanase gene from Bacillus subtilis in Saccharomyces cerevisiae from the CYC1 and ADH1 promotors. Curr. Genet 1986; 11: 65
  • Suzuki H., Kaneko T. Degradation of barley glucan and lichenan by a Bacillus pumilis enzyme. Agric. Biol. Chem 1976; 40: 577
  • Zemek J., Augustin J., Borris R., Kuniak L., Svabova M., Pacova Z. Polisaccharide-hydrolysing enzymes in the genus. Bacillus, Folia Microbiol 1981; 26: 403
  • Cantwell B. A., Sharp P. M., Gormley E., McConnell D. J. Molecular cloning Bacillus β-glucanases in Biochemistry and Genetics of Cellulose Degradation, J.-P. Aubert, P. Beguin, J. Millot. Academic Press, London 1988; 181
  • Hofemeister J., Kurtz A., Borris R., Knowles J. The β-glucanase gene from Bacillus amyloliquefaciens shows extensive homology with that of, Bacillus subtilis. Gene 1986; 49: 177
  • Murphy N., McConnell D. J., Cantwell B. A. The DNA sequence of the gene and genetic control sites for the excreted Bacillus subtilis enzyme β-glucanase. Nucl. Acid Res 1984; 12: 5355
  • Cantwell B. S., McConnell D. J. Molecular cloning and expression of a Bacillus subtilis β-glucan gene in, Escherichia coli. Gene 1983; 23: 211
  • Borris R. Purification and characterization of an extracellular β-glucanase from Bacillus IMET B 376. Z. Allg. Mikrobiol 1981; 21: 7
  • Hinchlife E. Cloning and expression of Bacillus subtilis endo-1,3–1,4-glucanase gene in E. coli K 12. J. Gen. Microbiol 1984; 130: 1285
  • McConnell D. J., Cantwell B. A., Derine K. M., Forage A. J., Lacide B. M., O'Kane C., Ollington I. F., Sharp P. M. Genetic engineering of extracellular enzyme system of Bacilli. Ann. N.Y. Acad. Sci 1986; 469: 1
  • Gromley E. P., Cantwell B. A., Barker P. J., Glimour R. S., McConnell D. J. Secretion and processing of the Bacillus subtilis endo-1,3–1,4-β-glucanase in Escherichia coli. Molec. Microbiol 1988; 2: 813
  • Doi K., Doi A. Cloning and expression in Escherichia coli of the gene for an Arthrobacter 1,3-β-glucanase. J. Bacteriol 1986; 168: 1276
  • Hinchlife E., Box W. G. Expression of the cloned endo-1,3–1,4-β-glucanase gene of Bacillus subtilis in Saccharomyces cerevisiae. Curr. Genet 1984; 8: 471
  • Hinchlife E., Box W. G. Beer enzymes and genes. The application of a concerted approach to B-glucan degradation. Proc. 21st Eur. Brew. Congr., Helsinki. IRL Press, Oxford 1985; 267
  • Cantwell B., Brazil G., Hurley J., McConnell D. J. Expression of the gene for the endo-B-1,3–1,4 glucanase from Bacillus subtilis in Saccharomyces cerevisiae. Proc. 21st, Eur. Brew. Conv. Congr, Helsinki. IRL Press, Oxford 1985; 259
  • Kombrink E., Schroder M., Hahlbrock K. Several “pathogenesis-related” proteins in potato are 1,3-β-glucanases and chitinases. Proc. Natl. Acad. Sci. U.S.A 1988; 85: 7–82
  • Ferraris L., Abbatista Gentile J., Matta A. Activation of glycosidase as a consequence of infection stress Fusarium vilt of tomato. J. Phytopathol 1987; 118: 317
  • Boiler T. Induction of hydrolases as a defense reaction against pathogens. Cellular and Molecular Biology of Plant Stress. Alan R. Liss, New York 1985; 247
  • Szklar B. M. Microorganisms producers of biologically active compounds. Nauka Technika, Minsk 1973
  • Vrsanska M., Biely P., Kratky Z. Enzymes of the yeast lytic system produced by Arthrobacter GJM-1 bacterium and their role in the lysis of yeast cell wall. Z. Allg. Mikrobiol 1977; 17: 465
  • Hunter J. B., Asenjo J. A. Kinetics of enzymatic lysis and disruption of yeast cells: I. Evaluation of two lytic systems with different properties. Biotech. Bioeng 1987; 30: 471
  • Eveleigh D. E. Trichoderma. Biology of Industrial Microorganism, A. L. Demain, N. A. Solomon. B. Cummings. 1985
  • Elad Y., Chet I., Henis Y. Degradation of plant pathogenic fungi by Trichoderma harzianum. Can. J. Microbiol 1982; 28: 719
  • Elad Y., Barak R., Chet J. Parasitism of sclerotia of Sclerotium rolfsii by Trichoderma harzianum. Soil. Biol. Biochem 1984; 16: 381
  • Yamamoto R., Arai M., Murao S. Physicochemical and chemical properties of red yeast cell wall lytic enzyme from, Penicillum lilacinum. Agric. Biol. Chem 1978; 42: 1593
  • Yamamoto S., Fukujama J., Nagasaki S. Production, purification, crystallization and some properties of yeast cell lytic enzyme from a species of, Fungi Imperfecti. Agr. Biol. Chem, 38: 329
  • Uyeda M., Ikeda A., Machimoto T., Shibata M. Effect of validamycin on production of some enzymes in, Rhizoctonia solani. Agric. Biol. Chem 1985; 49: 3485
  • Usui T., Oguchi M. Purification of a protease from Rhizoctonia solani lysing yeast cell walls. Agric. Biol. Chem 1986; 50: 535
  • Galas E., Bielecki S., Antczak T., Bobowicz-Lassocinska T. Polish Patent. 125 898, 1984
  • Galas E., Antczak T., Bielecki S., Szczesna M. Polish Patent. 125 942, 1984
  • Tanaka H., Phaff H. J. Enzymatic hydrolysis of yeast cell walls. J. Bacteriol 1965; 89: 1570
  • McLellan W. L., McDaniel L. E., Lampen J. O. Purification of phosphomannanase and its action on the yeast cell wall. J. Bacteriol 1970; 102: 261
  • Hunter J. B., Asenjo J. A. A distributed model of enzymatic lysis of microbial cells. Ann. N.Y. Acad. Sci 1987; 506: 649
  • Kitamura K. A protease that participates in yeast cell wall lysis during zymolyase digestion. Agric. Biol. Chem 1982; 46: 2093
  • Hunter J. B., Asenjo J. A. A population balance model of enzymatic lysis of microbial cells. Biotech. Bioeng 1990; 35: 31
  • Chisti Y., Moo-Young M. Disruption of microbial cells for intracellular products, Enzyme. Microb. Technol 1986; 8: 194
  • Ryan E., Word O. P. The application of lytic enzymes from Basidiomycete aphyllophoroles in production of yeast extract, Process. Biochem 1988; 23: 12
  • Ryan E., Ward O. P. Study of the effect of 1,3-β-glucanase from Basidiomycete on yeast extract production. Biotechnol. Lett 1985; 7: 409
  • Galas E., Bielecki S., Antczak T., Bobowicz-Lassocinska T., Szczesna M. Polish Patent. 204705
  • Cameron D. R., Cooper D. G., Neufeld R. J. The mannoproteins of Saccharomyces cerevisiae is an effective bioemulsifier. Appl. Environ. Microbiol 1989; 54: 1420
  • Cope R. EP. 230378
  • Cope R. UK Patent GB. 2185489
  • Peberdy J. F. Fungal protoplast: isolation and reversion and fusion. Ann. Rev. Microbiol 1979; 33: 21
  • Stephen E. R., Nasim A. Production of protoplasts in different yeast by Mutanase. Can. J. Microbiol 1981; 27: 550
  • Kitamoto Y., Mori N., Yamamoto M., Ohiwa T., Ichikawa Y. A simple method for protoplast formation and improvement of protoplast regeneration from various fungi using an enzyme from, Trichoderma harzianum. Appl. Microbiol. Biotechnol 1988; 28: 445
  • Hrmova M., Selitrennikoff C. P. Protoplast formation of Neu rospora crassa by an inducible enzyme system of Arthrobacter GJM-1. Curr. Microbiol 1987; 16: 33
  • Billich A., Keller M., Kleinkauf H., Zocher R. Production of protoplasts from Fusarium scirpi by lytic enzymes from, Streptomyces tsusimaensis. Appl. Microbiol. Biotechnol 1988; 28: 442
  • Kistler H. C., Leong S. A. Linear plasmidlike DNA in the plant pathogenic fungus Fusarium oxysporum f. sp., conglutionans. J. Bacteriol 1986; 167: 587
  • Zomer E., Er-EI Z., Rokem J. S. Production of intracellular enzymes by enzymic treatment of yeast. Enzyme Microb. Technol 1987; 9: 281
  • Pastor F. I. J., Valentin E., Herrero E., Sentandreu R. Structure of the Saccharomyces cerevisiae cell wall: mannoproteins released by Zymolase and their contribution to wall architecture. Biochim. Biophys. Acta 1984; 802: 292
  • Frevert J., Ballou C. E. Saccharomyces cerevisiae structural cell wall mannoprotein. Biochemistry 1985; 24: 753
  • Herrero E., Boyd A. Mannoproteins from the cell wall of Kluyveromyces lactis. FEMS Microbiol. Lett 1986; 36: 207
  • Gopal P., Sullivan P. A., Shepherd M. G. Isolation and structure of glucan from regenerating spheroplasts of Candida albicans. J. Gen. Microbiol 1984; 130: 1217
  • Elorza V., Margui A., Sentandreu R. Dimorphism in Candida albicans: contribution of mannoproteins to the architecture of yeast and mycelial cell walls. J. Gen. Microbiol 1985; 131: 2209
  • Sundstrom P. M., Kenny G. E. Enzymic release of germ tube specific antigens from cell walls of Candida albicans. Infect. Immun 1985; 49: 609
  • Antczak T. Immobilization of Lytic Enzymes of Streptomyces sp. 1228. Ph.D. thesis, Technical University of Lodz. 1981
  • Galas E., Bielecki S., Antczak T. Lytic enzymes and possibilities of their application. Kvasny Prum 1983; 29: 130
  • Chet J., Elad Y. Mechanism of mycoparasitism. Colloq. INRA 1983; 18: 35
  • Nishibashi H., Katabami T., Oyama M., Matsubayashi T. Japan Patent. 61/92589 A2 ‘86/92589’, 1986
  • Nishibashi H., Katabami T., Oygama M., Matsubayashi T. Japan Patent. 61/96995 A2 ‘86/96995’, 1986
  • Kusama S., Kusakbe I., Nakamure Y., Eda S., Murakami K. Transglucosylation into stevioside by the enzyme system from Streptomyces sp. Agric. Biol. Chem 1986; 50: 2445

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.