Purification of a heat-stable chitin deacetylase from Aspergillus nidulans and its role in cell wall degradation

An extracellular chitin deacetylase activity has been purified to homogeneity from autolyzed cultures of Aspergillus nidulans. This enzyme is an acidic glycoprotein with a pI of 2.75 and a 28% (wt/wt) carbohydrate content. The apparent Mr of the enzyme estimated by SDS/PAGE and Superose 12 (f.p.l.c....

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Bibliographic Details
Published inCurrent microbiology Vol. 30; no. 1; p. 49
Main Authors Alfonso, C. (C.S.I.C., Madrid, Spain.), Nuero, O.M, Santamaria, F, Reyes, F
Format Journal Article
LanguageEnglish
Published United States 01.01.1995
Subjects
ACTIVIDAD ENZIMATICA
ACTIVITE ENZYMATIQUE
AMIDE HYDROLASE
AMIDO HIDROLASA
Amidohydrolases - chemistry
Amidohydrolases - isolation & purification
Amidohydrolases - metabolism
ASPERGILLUS NIDULANS
Aspergillus nidulans - enzymology
Aspergillus nidulans - growth & development
Aspergillus nidulans - metabolism
Autolysis
BIODEGRADACION
BIODEGRADATION
CALOR
Cell Wall - metabolism
CHALEUR
Chitin - metabolism
CHITINE
Enzyme Stability
Hot Temperature
Hydrogen-Ion Concentration
Kinetics
Molecular Weight
PARED CELULAR
PAROI CELLULAIRE
PROPIEDADES FISICO-QUIMICAS
PROPRIETE PHYSICOCHIMIQUE
PURIFICACION
PURIFICATION
QUITINA
RESISTANCE A LA TEMPERATURE
RESISTENCIA A LA TEMPERATURA
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Summary:An extracellular chitin deacetylase activity has been purified to homogeneity from autolyzed cultures of Aspergillus nidulans. This enzyme is an acidic glycoprotein with a pI of 2.75 and a 28% (wt/wt) carbohydrate content. The apparent Mr of the enzyme estimated by SDS/PAGE and Superose 12 (f.p.l.c.) was around 27,000. The enzyme had an optimum pH at 7.0 and was stable in the pH range 4.0-7.5. Its optimum temperature of reaction was 50 degrees C, and it was stable from 30 degrees C to 100 degrees C after 1 h of preincubation. The enzyme hydrolyzed glycol chitin and oligomers of N-acetylglucosamine and to a lesser extent chitin, colloidal chitin, carboxymethylchitin, and an alpha-1 leads to 3, 1 leads to 6-N-acetylgalactosamine-galactan among other substances with amido groups, but the enzyme did not hydrolyze peptide bonds. The role of this enzyme could be deacetylation of chitin oligosaccharides during autolysis, after action of endochitinase on cell walls
Bibliography:F60
9548466
ISSN:0343-8651
1432-0991
DOI:10.1007/bf00294524