Open AccessPolyacrylamide-gel Electrophoresis of Enzymes during Morphogenesis of Sclerotia of Sclerotinia sclerotiorum
Author(s) -
A.-L. Wong,
H. J. Willetts
Publication year - 2000
Publication title -
microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.019
H-Index - 179
eISSN - 1465-2080
pISSN - 1350-0872
DOI - 10.1099/00221287-81-1-101
Subject(s) - sclerotinia sclerotiorum , mycelium , pentose phosphate pathway , dehydrogenase , biochemistry , glyceraldehyde , tyrosinase , enzyme , phosphogluconate dehydrogenase , biology , enzyme assay , acid phosphatase , glycolysis , chemistry , glucose 6 phosphate dehydrogenase , botany
Succinate dehydrogenase (SDH) and glucose-6-phosphate dehydrogenase (Glu-6-PDH) from Sclerotinia sclerotiorum (Lib.) de Bary were moderately active in submerged mycelium while in non-sclerotial aerial mycelium arylesterase and acid phosphatase were very active. In sclerotial initials, glyceraldehyde-3-phosphate dehydrogenase (Gly-3-PDH) and SDH were at their highest level of activity, Glu-6-PDH and phosphogluconate dehydrogenase (PGDH) were moderately active, laccase activity increased markedly, and tyrosinase was detected for the first time, its activity being moderate. In young compacting sclerotia, the activities of Glu-6-PDH and PGDH increased, Gly-3-PDH and SDH showed lowered activities, and laccase activity decreased. Suppression of the glycolytic Krebs-cycle pathway and the stimulation of the pentose phosphate pathway seem important during the compaction and maturation of sclerotia. Tyrosinase may be involved in sclerotial initiation.