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Characterization of galactose-induced extracellular and intracellular pectolytic activities from the exo-1 mutant strain of Neurospora crassa

Crotti, L.B. (Universidade de Sao Paulo, Ribeirao Preto, Sao Paulo, Brazil.) ; Terenzi, H.F ; Jorge, J.A ; Polizeli, M.L.T.M

Journal of industrial microbiology & biotechnology, 1998-03, Vol.20 (3/4), p.238-243 [Periódico revisado por pares]

Heidelberg: Springer

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  • Título:
    Characterization of galactose-induced extracellular and intracellular pectolytic activities from the exo-1 mutant strain of Neurospora crassa
  • Autor: Crotti, L.B. (Universidade de Sao Paulo, Ribeirao Preto, Sao Paulo, Brazil.) ; Terenzi, H.F ; Jorge, J.A ; Polizeli, M.L.T.M
  • Assuntos: Biological and medical sciences ; Biology of microorganisms of confirmed or potential industrial interest ; Biotechnology ; Enzymes ; ENZYMIC ACTIVITY ; Fundamental and applied biological sciences. Psychology ; LYASES ; Microbiology ; Miscellaneous ; Mission oriented research ; NEUROSPORA CRASSA ; PECTATE LYASE ; PECTIN LYASE ; POLYGALACTURONASE
  • É parte de: Journal of industrial microbiology & biotechnology, 1998-03, Vol.20 (3/4), p.238-243
  • Notas: F60
    1997089071
    ObjectType-Article-2
    SourceType-Scholarly Journals-1
    ObjectType-Feature-1
    content type line 23
  • Descrição: Pectolytic enzymes from the hyperproducer exo-1 mutant of Neurospora crassa are induced either by pectin or galactose. Galactose-induced pectinases, in contrast with pectin-induced enzymes, are not affected by glucose repression. Here, the pectolytic enzymes induced by galactose were purified and characterized. Extracellular pectolytic activities were separated into two main fractions. Pool I contained lyases, and a polygalacturonase (PG) copurifying as a complex of about 80 kDa (gel filtration). Pool II contained PG only. Under urea-SDS-PAGE the lyases and polygalacturonase from pool I migrated with an apparent MW of 56.2 kDa, and 34.3 kDa, respectively. PG from pool II exhibited an apparent MW of 44.7 kDa. Cell extracts contained PG free of lyase activities. Purified intracellular PG migrated (SDS-PAGE) as a single band of apparent MW of 31.5 kDa. All pectinases were glycoproteins (18.5-39% carbohydrate), with stability and optimum pH at 5-6 and 9-10 for PG and lyases, respectively. Temperature optima were 40-50 degrees C, respectively. All enzymes were inactivated at 60 degrees C, with a half-life from 1.5 to 5 min. Activation energy (Ea) values for extracellular and intracellular PG varied between 0.45 and 2.0 Kcal mol-1. Pool II and intracellular PG and lyases, exhibited a random mechanism of hydrolysis. Pool I PG exhibited an exo character
  • Editor: Heidelberg: Springer
  • Idioma: Inglês
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