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Physiology/Biochemistry

Screening wood- and bark-inhabiting Basidiomycetes for esterase activity in liquid stationary culture

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Pages 831-838 | Accepted 24 Apr 1996, Published online: 28 Aug 2018

LITERATURE CITED

  • Bonnen, A. M., and R. Hammerschmidt. 1989. Cutinolytic enzymes from Colletotrichum lagenarium. Physiol. Mol. Plant Pathol. 35: 463–474.
  • Davin, L. B., and N. G. Lewis. 1992. Phenylpropanoid metabolism: biosynthesis of monolignols, lignans and neolignans, lignins and suberins. Pp. 325–375. In: Phenolic metabolism in plants. Eds., H.A. Stafford and R.K. Ibrahim. Plenum Press, New York. 411 pp.
  • Dickman, M. B., and S. S. Patil. 1986. Cutinase deficient mutants of Colletotrichum gloeosporioides are nonpathogenic to papaya fruit. Physiol. Mol. Plant Pathol. 28: 235–242.
  • Dickman, M. B., and S. S. Patil, and P. E. Kolattukudy. 1982. Purification, characterization and role in infection of an extracellular cutinolytic enzyme from Colletotrichum gloeosporioides Penz. on Carica papaya L. Physiol. Plant Pathol. 20: 333–347.
  • Fahn, A. 1982. Plant anatomy, 3rd. Ed. Pergamon Press, Oxford, England. 544 pp.
  • Fernando, G., W. Zimmermann, and P. E. Kolattukudy. 1984. Suberin-grown Fusarium solani f. sp. pisi generates a cutinase-like esterase which depolymerizes the aliphatic components of suberin. Physiol. Pl. Pathol. 24: 143–155.
  • Gao, M., and G. P. Chamuris. 1993. Microstructural and histochemical changes in Acer platanoides rhytidome caused by Dendrothele acerina (Aphyllophorales) and Mycena meliigena (Agaricales). Mycologia 85: 987–995.
  • Hattersley, P. W., and A. G. Browning. 1981. Occurrence of suberized lamella in leaves of grasses of different photosynthetic types. I. In parenchymatous bundle sheaths and PCR (“Kranz”) sheaths. Protoplasma 109: 371–401.
  • Holloway, P.J. 1972. The composition of suberin from the corks of Quercus suber L. and Betula pendula Roth. Chem. Physiol. Lipids 9: 158–170.
  • Kirk, T. K., and R. L. Farrell. 1987. Enzymatic combustion: the microbial degradation of lignin. Ann. Rev. Microbiol. 41: 465–505.
  • Kolattukudy, P. E. 1981. Structure, biosynthesis, and biodegradation of cutin and suberin. Ann. Rev. Plant Physiol. 32: 539–567.
  • Kolattukudy, P. E.. 1984a. Fungal penetration of defensive barriers of plants. Pp. 302–343. In: Structure, function, and biosynthesis of plant cell watts. Eds., W.M. Dugger and S. Bartnicki-Garcia. American Society of Plant Physiologists, Rockville, Maryland. 507 pp.
  • Kolattukudy, P. E.. 1984b. Biochemistry and function of cutin and suberin. Canad. J. Bot. 62: 2918–2933.
  • Kolattukudy, P. E., and B. B. Dean. 1974. Structure, gas chromatographic measurement, and function of suberin synthesized by potato tuber tissue slices. Plant Physiol. 54: 116–121.
  • Koller, W. and D. M. Parker. 1989. Purification and characterization of cutinase from Venturia inaequalis. Phytopathology 79: 278–283.
  • Koller, W. and D. M. Parker, and C. M. Becker. 1991. Role of cutinase in the penetration of apple leaves by Venturia inaequalis. Phytopathology 81: 1375–1379.
  • Koller, W. and D. M. Parker, and C. M. Becker, C. Yao, F. Trail, and D. M. Parker. 1995. Role of cutinases in the invasion of plants. Canad. J. Bot. 73: S1109–S1118.
  • Lide, D. R., ed. 1990. Handbook of chemistry and physics, 71st. Ed. Chemical Rubber Company Press, Boca Raton.
  • Lin, T. S., and P. E. Kolattukudy. 1978. Induction of a polyester hydrolase (cutinase) by low levels of cutin monomers in Fusarium solani f. sp. pisi. J. Bacteriol. 133: 942–951.
  • Purdy, R. E. and P. E. Kolattukudy. 1973. Depolymerization of a hydroxy fatty acid biopolymer, cutin, by an extracellular enzyme from Fusarium solani f. pisi: isolation and some properties of the enzyme. Arch. Biochem. Biophys. 159: 61–69.
  • Purdy, R. E. and P. E. Kolattukudy. 1975a. Hydrolysis of plant cuticle by plant pathogens. Purification, amino acid composition and molecular weight of two isoenzymes of cutinase and a nonspecific esterase from Fusarium solani f. sp. pisi. Biochemistry 14: 2824–2831.
  • Purdy, R. E. and P. E. Kolattukudy. 1975b. Hydrolysis of plant cuticle by plant pathogens. Properties of cutinase I, cutinase II and a nonspecific esterase isolated from Fusarium solani pisi. Biochemistry 14: 2832–2840.
  • Tehon, L. R., and W. R. Jacks. 1933. Smooth patch, a bark lesion of white oak. J. Forestry 31: 430–433.
  • Trail, F., and W. Köller. 1990. Diversity of cutinases from plant pathogenic fungi: evidence for a relationship between enzyme properties and tissue specificity. Physiol. Mol. Plant Pathol. 36: 495–508.
  • van den Ende, G., and H. F. Linskens. 1974. Cutinolytic enzymes in relation to pathogenesis. Ann. Rev. Phytopathol. 12: 247–258.
  • Zimmermann, W., and E. Seemüller. 1984. Degradation of raspberry suberin by Fusarium solani f. sp. pisi and Armillaria mettea. Phytopath. Z. 110: 192–199.

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