The Autolysis of Industrial Filamentous Fungi

REFERENCES

• Brookman, J.L. and Denning, D.W., Molecular genetics in Aspergillus fumigatus, Curr Opin Microbiol., 3, 468–74, 2000.
   PubMed Web of Science ®Google Scholar
• Cohen, B. E., Amphotericin B toxicity and lethality: a tale of two channels, Int. J. Pharmaceutics, 162, 95–106, 1998.
   Google Scholar
• Archer, D. B., MacKenzie, D. A., Jeenes D. J., and Roberts, I. N., Proteolytic degradation of heterologous proteins expressed in Aspergillus niger, Biotechnol. Lett., 14, 357–362, 1992.
   Web of Science ®Google Scholar
• Alfonso, C., Cribiero, L., and F. Reyes, Penicillin amidohydrolases in fungal autolysis, Microbiol. Immunol., 33, 69–74, 1989.
   PubMed Web of Science ®Google Scholar
• White, S., Autolysis in Penicillium chrysogenum, Ph.D. Thesis, University of Strathclyde, U.K, 1999.
   Google Scholar
• Reyes, F., Martinez, J., Alfonso, C., Copa-Patino, J. L., and Soliveri, J., Cephalosporin C acylase in the autolysis of filamentous fungi, J. Pharm. Pharmacol., 42, 128–131, 1990.
   PubMed Web of Science ®Google Scholar
• Bartoshevich, Y. E. and Zaslavskaya. P. L., Morphological and functional characteristics of the growth of Fusidium coccineum strains with different antibiotic activity during their submerged cultivation, Mikrobiologiya, 53, 266–270, 1984.
   Google Scholar
• McNeil, B., Berry, D. R., Harvey, L. M., Grant, A., and White, S., Measurement of autolysis in submerged batch cultures of Penicillium chrysogenum, Biotechnol. Bioeng., 57, 297–305, 1998.
   PubMed Web of Science ®Google Scholar
• Lahoz, R., Reyes, F., and Perez-Leblic, M. I., Lytic enzymes in the autolysis of filamentous fungi, Mycopathologia, 60, 45–49, 1976.
   PubMed Web of Science ®Google Scholar
• Reyes, F., Calatayud, J., Vazquez, C., and Martinez, M. J., β-N-acetylglucosaminidase from Aspergillus nidulans which degrades chitin oligomers during autolysis, FEMS Microbiol. Lett., 65, 83–88, 1989.
   Web of Science ®Google Scholar
• Santamaria, F. and Reyes, F., Proteases produced during autolysis of filamentous fungi, Trans. Br. Mycol. Soc., 91, 217–220, 1988.
   Web of Science ®Google Scholar
• Harvey, L. M., McNeil, B., Berry, D. R., and White, S., Autolysis in batch cultures of Penicillium chrysogenum at varying agitation rates, Enzyme Microb. Technol., 22, 448–458, 1998.
   Web of Science ®Google Scholar
• Vanhoutte, B., Pons, M. N., Thomas, C. R., Louvel, L., and Vivier, H., Characterization of Penicillium chrysogenum physiology in submerged cultures by colour and monochrome image analysis, Biotechnol. Bioeng., 48, 1–11, 1995.
   PubMed Web of Science ®Google Scholar
• Trinci, A. P. J. and Righelato, R. C., Changes in constituents and ultrastructure of hyphal compartments during autolysis of glucose starved Penicillium chrysogenum, J. Gen. Microbiol., 60, 239–249, 1970.
   PubMedGoogle Scholar
• Fencl, Z., Cell ageing and autolysis, in The Filamentous Fungi III, Smith, J. E. and Berry, D. R., Eds., Blackie Scientific Press, London, UK, 1975, 389–405.
   Google Scholar
• Riemay, K. H. and Troger, R., Autolysis in fungi. I. Autolysis in Coprinus and fungal cultures, Z. Allg. Mikrob., 18, 523–540, 1978a.
   PubMedGoogle Scholar
• Riemay, K. H. and Troger, R., Autolysis in fungi. II. Autolytic degradation of carbohydrates, proteins and nucleic acids, Z. Allg. Mikrob., 18, 617–625, 1978b.
   PubMedGoogle Scholar
• Paul, G. C. and Thomas, C. R., Characterization of mycelial morphology using image analysis, Adv. Biochem. Eng. Biotech., 60, 1–59, 1998.
   PubMed Web of Science ®Google Scholar
• Schugerl, K., Gerlach, S. R., and Siedenberg, D., Influence of the process parameters on the morphology and enzyme production of Aspergilli, Adv. Biochem. Eng. Biotech., 60, 195–270, 1998.
   PubMedGoogle Scholar
• Righelato, R. Trinci, C., A. P. J., and Pirt, S. J., The influence of maintenance energy and growth rate on the metabolic activity, morphology and conidiation of Penicillium chrysogenum, J. Gen. Microbiol., 50, 399–412, 1968.
   PubMedGoogle Scholar
• Pusztahelyi, T., Pócsi, I., and Szentirmai, A., Aging of Penicillium chrysogenum cultures under carbon starvation: II protease and N-acetyl-β-d-hexosaminidase production, Biotechnol. Appl. Biochem., 25, 87–93, 1997.
   Web of Science ®Google Scholar
• Pusztahelyi, T., Pócsi, I., Kozma, J., and Szentirmai, A., Aging of Penicillium chrysogenum cultures under carbon starvation I: morphological changes and secondary metabolite production, Biotechnol. Appl. Biochem., 25, 81–86, 1997.
   Web of Science ®Google Scholar
• Rober, B., Riemay, K. H., and Hilpert, A., Growth and autolysis of the ascomycete Hypomyces ochraceus. Metabolism of U-14C-l-leucine 2–14C-dl-threonine and U-14C-l-aspartic acid, J. Basic Microbiol., 26, 475–482, 1986.
   Web of Science ®Google Scholar
• Schrickx, J. M. Krave, A. S., Verdoes, J. C., Van den Hondel, C. A. M. J. J., Stouthamer, A. H., and van. Verseveld, H. W., Growth and product formation in chemostat and recycling cultures by Aspergillus niger N402 and a glucoamylase over producing transformant, provided with multiple copies of the gla A gene, J. Gen. Microbiol., 139, 2801–2810, 1993.
   PubMedGoogle Scholar
• Cohen, B. L., Regulation of intracellular and extracellular neutral and alkaline proteases in Aspergillus nidulans, J. Gen. Micro., 79, 311–320, 1973.
   PubMedGoogle Scholar
• Cohen, B. L., Morris, J. E., and Drucker, H., Regulation of two extracellular proteases of Neurospora crassa by induction and by carbon-, nitrogen- and sulfur-metabolite repression, Arch. Biochem. Biophys., 169, 324–330, 1975.
   PubMed Web of Science ®Google Scholar
• Lilly, W. W., Higgins, S. M., and Wallweber, G. J., Electrophoretic detection of multiple proteases from Schizophyllum commune, Mycologia, 82, 505–508, 1990.
   Web of Science ®Google Scholar
• Higgins, S. M. and Lilly, W.W., Multiple responses to heat stress by the basidiomycete Schizophyllum commune, Curr. Microbiol., 26, 123–127, 1993.
   Web of Science ®Google Scholar
• Breuil, C. and Huang. J., Activities and properties of extracellular proteinases produced by staining fungi grown in protein supplemented liquid media, Enzyme Microb. Technol., 16, 602–607, 1994.
   Web of Science ®Google Scholar
• Gordon, L. J. and Lilly, W. W., Quantitative analysis of Schizophyllum commune metalloprotease ScPrB activity in SDS-gelatin page reveals differential mycelial localization of nitrogen limitation induced autolysis, Curr. Microbiol., 30, 337–343, 1995.
   Web of Science ®Google Scholar
• Bilbrey, R. E., Peniteiter, A. R., Gathman, A. C., and Lilly, W. W., Characterization of a novel phenylalanine-specific aminopeptidase from Schizophyllum commune, Mycol. Res., 100, 462–466, 1996.
   Google Scholar
• Chrzanowska, J., Kolaczkowska, M., and Polanowski, A., Production of extracellular proteolytic enzymes by various species of Penicillium, Enzyme Microb. Technol, 15, 140–143, 1993.
   Web of Science ®Google Scholar
• Bainbridge, B. W., Bull, A. T., Pirt, S. J., Rowley, B. I., and Trinci, A. P. J., Biochemical and structural changes in non-growing maintained and autolysing cultures of Aspergillus nidulans, Trans. Br. Mycol. Soc., 56, 371–385, 1971.
   Google Scholar
• McIntyre M., Berry, D.R., and McNeil B., Role of proteases in autolysis of Penicillium chrysogenum chemostat cultures in response to nutrient depletion, Appl. Microbiol. Biotechnol., 53(2), 235–42, 2000.
   PubMed Web of Science ®Google Scholar
• Nuero, O. M., Alfonso, C., Del Amo, F., and Reyes., F., Study of fl-1, 3–glucanase activity during autolysis of Aspergillus nidulans by FPLC ion-exchange chromatography, Lett. Appl. Microbiol., 17, 104–108, 1993.
   Web of Science ®Google Scholar
• Gooday, G. M., Cell walls, in The Growing Fungus, Gow, N. A. R. and Gadd, G. M., Eds., Chapman and Hall, London, U.K., 1995, 43–62.
   Google Scholar
• Perez-Leblic, M. I., Reyes, F., Lahoz, R., and Archer, S. A., Autolysis of Penicillium oxalicum with special reference to its cell walls, Can. J. Microbiol., 28, 1289–1295, 1982.
   Web of Science ®Google Scholar
• Polacheck, Y. and Rosenberger, R. F., Autolytic enzymes in hyphae of Aspergillus nidulans: their action on old and newly formed walls, J. Bacteriol., 121, 332–337, 1975.
   PubMed Web of Science ®Google Scholar
• Wessels, J. G. H., Cell wall synthesis and apical growth, Int. Rev. Cyto., 104, 37–79, 1986.
   Google Scholar
• Copa-Patino, J. L., Reyes, F., and Perez-Leblic, M. I., Purification and properties of a 1,3–β-glucanase from Penicillium oxalicum autolysates, FEMS Microbiol. Lett., 65, 285–292, 1989.
   Web of Science ®Google Scholar
• Pitson, S. M., Seviour, R. J., and McDougall, B. M., Effect of carbon source on extracellular β(1→3) and β(1→6)-glucanase production by Acremonium persicinum, Can. J. Microbiol., 43, 432–439, 1997.
   Web of Science ®Google Scholar
• Paul, G. C., Kent, C. A., and Thomas, C. R., Hyphal vacuolation and fragmentation in Penicillium chrysogenum, Biotechnol. Bioeng., 44, 655–660, 1994a.
   PubMed Web of Science ®Google Scholar
• Reyes, F., Lahoz, R., and Moreno, A. V., Synthesis of 1,3-β-glucanase and β-N-acetylglucosaminidase during autolysis of Neurospora crassa, J. Gen. Microbiol., 126, 347–353, 1981.
   Google Scholar
• Pitson, S., Seviour, R. J., Bott, J., and Stasinopoulos, S. J., Production and regulation of β-glucanases in Acremonium and Cephalosporium isolates, Mycol. Res., 95, 352–356, 1991.
   Web of Science ®Google Scholar
• Pitson, S. M., Seviour, R. J., and McDougall, B. M., Non-cellulolytic fungal β-glucanases: their physiology and regulation, Enzyme Microb. Technol., 15, 178–192, 1993.
   PubMed Web of Science ®Google Scholar
• Cabib, E., The synthesis and degradation of chitin, Adv. Enzymol., 59, 59–101, 1987.
   PubMedGoogle Scholar
• Alfonso, C., Martinez, M. J., and Reyes., F., Degradation of chitosan in the autolysis of Mucorales spp, Mycol. Res., 95, 217–219, 1991.
   Google Scholar
• Alfonso, C., Martinez M. J., and Reyes, F., Purification and properties of two endochitosanases from Mucor rouxii implicated in its cell wall degradation, FEMS Microbiol. Lett. 95, 187–194, 1992.
   Web of Science ®Google Scholar
• Reyes, F., Calatayud, J., and Martinez, M.J., Chitinolytic activity in the autolysis of Aspergillus nidulans, FEMS Microbiol. Lett., 49, 239–243, 1988.
   Web of Science ®Google Scholar
• Gooday, W. G., Physiology of microbial degradation of chitin and chitosan, Biodegradation, 1, 177–190, 1990.
   Web of Science ®Google Scholar
• Rodriguez, J., Santos, M. J., Copa-Patino, J. L., and Perez-Leblic, M. I., Chitinolytic activity produced by Penicillium oxalicum in different culture media, Lett. Appl. Microbiol., 16, 69–71, 1993.
   Web of Science ®Google Scholar
• Pusztahelyi, T., Pócsi, I., Kozma, J., and Szentirmai, A., In vitro and in vivo inhibition of the Penicillium chrysogenum N-acetyl-β-d-hexosaminidase, Acta Microbiologia et Immunologica Hungarica, 43, 252, 1996.
   Google Scholar
• Alfonso, C., Santamaria, F., Nuero, O. M., Pricto, A., Leal, J. A., and Reyes, F., Biochemical studies on the cell wall degradation of Fusarium oxysporum f.sp. lycopersici race 2 by its own lytic enzymes for its biocontrol, Lett. Appl. Microbiol, 20, 105–109, 1995.
   Web of Science ®Google Scholar
• Sandor, E., Pusztahelyi, T., Karaffa, L., Karanyi, Z., Biro, S., Szentirmai, A., and Pocsi, I., Allosamidin inhibits fragmentation of Acremonium chrysogenum but does not influence cephalosporin-C production, FEMS Microbiol. Lett., 164, 231–236, 1998.
   PubMed Web of Science ®Google Scholar
• Martinez, M. J., Vazquez, C., Guillen, F., and Reyes, F., β-Glucosidase from the cellulolytic system of Alternaria alternata autolyzed cultures, FEMS Microbiol. Lett., 55, 263–268, 1988.
   Web of Science ®Google Scholar
• Rodriguez, J., Copa-Patino, J. L., and Perez-Leblic, M. I., Purification and properties of a chitinase from Penicillium oxalicum autolysates, Lett. Appl. Microbiol., 20, 46–49, 1995.
   PubMed Web of Science ®Google Scholar
• Lejeune, R. and Barton, G. V., Simulation of growth of a filamentous fungus in three dimensions, Biotechnol. Bioeng., 53,139–150, 1997.
   PubMed Web of Science ®Google Scholar
• Trinci, A. P. J., The duplication cycle and branching in fungi, in Fungal Walls and Hyphal Growth, Burnett, J. H. and Trinci, A. P. J., Eds., Cambridge University Press, Cambridge, U.K., 1979, 319–357.
   Google Scholar
• Krabben, P. and Nielsen, J., Modeling the mycelium morphology of Pencillium species in submerged cultures, Adv. Biochem. Eng. Biotech., 60, 125–152, 1998.
   Google Scholar
• Christensen, L.H., Henricksen, C. M., Nielsen, J., Villadsen, J., and Egel-Mitani, M., Continuous cultivation of Penicillium chrysogenum. Growth on glucose and penicillin production, J. Biotechnol., 42, 95–107, 1995.
   PubMed Web of Science ®Google Scholar
• Cox, P. W., Paul, G. C., and Thomas, C. R., Image analysis of the morphology of filamentous micro-organisms, Microbiology, 144, 817–827, 1998.
   PubMed Web of Science ®Google Scholar
• Smith, J. J., Lilly, M. D., and Fox, R. I., The effect of agitation on the morphology and penicillin production of Penicillium chrysogenum, Biotechnol. Bioeng., 35, 1011–1023, 1990.
   PubMed Web of Science ®Google Scholar
• Cui, Y. Q., Van der Lans, R. G. J. M., and Luyben, K.C.A.M., Effects of dissolved oxygen tension and mechanical forces on fungal morphology in submerged fermentation, Biotechnol. Bioeng., 57, 409–419, 1998.
   PubMed Web of Science ®Google Scholar
• Agger, T., Spohr, A. B., Carlsen, M., and Nielsen. J., Growth and product formation of Aspergillus oryzae during submerged cultivations: verification of a morphologically structured model using fluorescent probes, Biotechnol. Bioeng., 57, 321–329, 1998.
   PubMed Web of Science ®Google Scholar
• Cui, Y. Q., Okkerse, W.J., Van der Lans, R G. J. M., and Luyben, K. C. A. M., Modeling and measurements of fungal growth and morphology in submerged fermentations, Biotechnol. Bioeng., 60, 216–229, 1998.
   PubMed Web of Science ®Google Scholar
• Justen, P., Paul, G. C., Nienow, A. W., and Thomas, C. R., A mathematical model for agitation-induced fragmentation of Penicillium chrysogenum, Bioprocess Eng., 18, 7–16, 1998.
   Google Scholar
• Nielsen, J. and Krabben, P., Hyphal growth and fragmentation of Penicillium chrysogenum in submerged cultures, Biotechnol. Bioeng., 46, 588–598, 1995.
   PubMed Web of Science ®Google Scholar
• Paul, G. C., Kent, C. A., and Thomas, C. R., Image analysis for characterizing differentiation of Penicillium chrysogenum, Trans. I. Chem. E., 72, 95–105, 1994b.
   Google Scholar
• Paul, G. C. and Thomas, C. R., A structured model for hyphal differentiation and penicillin production using Penicillium chrysogenum, Biotechnol. Bioeng., 51, 558–572, 1996.
   PubMed Web of Science ®Google Scholar
• Shamlou, A. P., Makagiansar, H. Y., Ison, A. P., Lilly, M. D., and Thomas, C. R., Turbulent breakage of filamentous micro-organisms in submerged culture in mechanically stirred bioreactors, Chem. Engineer. Sci., 49, 2621–2631, 1994.
   Web of Science ®Google Scholar
• Johansen, C. L., Coolen, L., and Hunik, J. H., Influence of morphology on product formation in Aspergillus awamori during submerged fermentations, Biotechnol. Prog., 14, 233–240, 1998.
   PubMed Web of Science ®Google Scholar
• White, S., Berry, D. R., and McNeil, B., Effect of phenylacetic acid feeding on the process of cellular autolysis in submerged batch cultures of Penicillium chrysogenum, J. Biotech., 75, 173–185, 1999.
   PubMed Web of Science ®Google Scholar
• Paul, G. C., Kent, C. A., and Thomas, C. R., An image processing method for the fully automatic measurement of vacuoles in filamentous fungi, Binary Comput. Microbiol., 5, 92–99, 1993.
   Google Scholar
• Paul, G. C., Kent, C. A., and Thomas, C. R., Quantitative characterization of vacuolization of Penicillium chrysogenum using automatic image analysis, Trans. I. Chem. E., 70, 13–20, 1992.
   Google Scholar
• Robinson, P. M., Ed., Practical Fungal Physiology, John Wiley and Sons, U.K., 1978, 87.
   Google Scholar
• King, R., Mathematical modeling of the morphology of Streptomyces species, Adv. Biochem. Eng. Biotech., 60, 95–123, 1998.
   Google Scholar
• Marek, S. M., Wu, J., Glass, N.L., Gilchrist, D. G., and Bostock, R. M., Programmed cell death in fungi: Heterokaryon incompatibility involves nuclear DNA degradation, 20th Fungal Genetics Conference, March 23–28, Pacific Grove, California, 1999.
   Google Scholar
• Anglade, P., Tsusi, S., and Vyas, S., Morphological diversity of programmed cell death: deciphering of triggering signals needs comprehensive classification, Biomed. Res., 18,1–6, 1997.
   Web of Science ®Google Scholar
• Wyllie, A. H., Kerr, J. F. R., and Currie, A. R. Cell death: the significance of apoptosis, Int. Rev. Cytol., 68, 251–306, 1980.
   PubMedGoogle Scholar
• Kerr, J. F. R., Wyllie, A. H., and Currie, A. R., Apoptosis: a basic biological phenomenon with wide ranging implications in tissue kinetics, Br. J. Cancer, 26, 239, 1972.
   PubMed Web of Science ®Google Scholar
• Reyes, F., Villanueva, P., and Alfonso, C., Nucleases in the autolysis of filamentous fungi, FEMS Microbiol. Lett., 69, 67–72, 1990.
   Web of Science ®Google Scholar
• Nohl, H., Involvement of free radicals in aging: a consequence of senescence, Br. Med. Bull., 49, 653–667, 1993.
   PubMed Web of Science ®Google Scholar
• Cheeseman, K. H. and Slater, T. F., An introduction to free radical biochemistry, Br. Med. Bull., 49, 481–493, 1993.
   PubMed Web of Science ®Google Scholar
• Diez, B., Schleissner, C., Moreno, M. A., Rodriguez, M., Collados, A., and Barredo, J.L., The manganese superoxide dismutase from the penicillin producer Penicillium chrysogenum, Curr. Genet., 33, 387–394, 1998.
   PubMed Web of Science ®Google Scholar
• Emri, T., Pocsi, I., and Szentirmai. A., Changes in the glutathione (GSH) metabolism of Penicillium chrysogenum grown on different nitrogen, sulphur and carbon sources, J.Basic Microbiol., 38, 3–8, 1998.
   Web of Science ®Google Scholar
• Sinclair, D. A., Mills, K., and Guarente, L. Accelerated aging and nuclear fragmentation in yeast sgsl mutants, Science, 277, 1313–1316, 1997.
   PubMed Web of Science ®Google Scholar
• Lombard, D. B. and Guarente, L., Cloning the gene for Werner syndrome : a disease with many symptoms of premature aging, Trends Genet., 12, 283–286, 1996.
   PubMed Web of Science ®Google Scholar
• Torres, L., Martin, H., Garcia-Saez, M. I., Arroyao, J., Molina, M., Sanchez, M., and Nombela, C., A protein kinase gene complements the lytic phenotype of Saccharomyces cerevisiae lyt2 mutants, Mol. Microbiol., 5, 2845, 1991.
   PubMed Web of Science ®Google Scholar
• Lundblad, V. and Szostak, J.W., A mutant with a defect in telomere elongation leads to senescence in yeast, Cell, 57, 633–643, 1989.
   PubMed Web of Science ®Google Scholar
• Schwartz, T. and Osiewacz, H. D., Telomere length does not change during senescence of the ascomycete Podospora anserina, Mut. Res., 316, 193–199, 1996.
   PubMedGoogle Scholar
• Osiewacz, H. D. and Esser, K., The mitochondrial plasmid of Podospora anserina — a mobile intron of a mitochondrial gene, Curr. Genet., 84, 299–305, 1984.
   Google Scholar
• Osiewacz, H. D., Molecular analysis of aging processes in fungi, Mut.Res., 237, 1–8, 1990.
   PubMedGoogle Scholar
• Jazwinski, S.M., An experimental system for the molecular analysis of the aging process: the budding yeast Saccharomyces cerevisiae, J. Gerontol., 45, B68–B74, 1990.
   PubMedGoogle Scholar
• Singh, R. P., Al-Rubeai, M., Gregory, C. D., and Emery, A. N., Cell death in bioreactors: a role for apoptosis, Biotechnol. Bioeng., 44, 720–726, 1994.
   PubMed Web of Science ®Google Scholar