Artigo Acesso aberto Revisado por pares

Saccharomyces cerevisiae mutant defective in exo-1,3-beta-glucanase production

1979; American Society for Microbiology; Volume: 139; Issue: 2 Linguagem: Inglês

10.1128/jb.139.2.333-338.1979

ISSN

1098-5530

Autores

T Santos, Francisco del Rey, Jaime Conde, J. R. Villanueva, César Nombela,

Tópico(s)

Enzyme Production and Characterization

Resumo

Saccharomyces cerevisiae S288C produced two laminarinases (1,3-beta-glucanases) which were separated by diethylaminoethyl-Sephadex column chromatography; one was an endo-1,3-beta-glucanase, and the other was an exo-1,3-beta-glucanase active not only on laminarin but also on pustulan (1,6-beta-glucan) and on p-nitrophenyl-beta-D-glucoside. A mutant defective in the production of this last enzyme was isolated, and the mutation was named exb1-1. The selection procedure was based on the capacity of exo-1,3-beta-glucanase to hydrolyze synthetic glucosides. The level of endo-1,3-beta-glucanase in cell extracts of the mutant was normal, but the exo-1,3-beta-glucanase could not be detected by column chromatographic analysis of these extracts. The mutant phenotype, recessive in heterozygous diploids, was stable through successive meioses and showed a Mendelian segregation, indicating that the mutation affected a single gene, which was named EXB1. The lack of production of exo-1,3-beta-glucanase persisted through all the phases of growth, but growth itself was not impaired by the enzyme deficiency.

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