Your browser doesn't support javascript.
loading
Purification of microbial (beta)-galactosidase from Kluyveromyces fragilis by bioaffinity partitioning
Silva, Maria Estela da; Franco, Telma Teixeira.
  • Silva, Maria Estela da; Universidade Estadual de Campinas. Faculdade de Engenharia de Alimento. Departamento de Tecnologia de Alimentos.
  • Franco, Telma Teixeira; Universidade Estadual de Campinas. Faculdade de Engenharia Química. Departamento de Processo Químicos.
Rev. microbiol ; 30(4): 324-31, out.-dez. 1999. ilus, tab, graf
Artículo en Inglés | LILACS | ID: lil-286786
ABSTRACT
This work investigated the partitioning of (beta)-galactosidase from "Kluyveromyces fragilis" in aqueous two-phase systems (ATPS) by bioaffinity. PEG 4000 was chemically activated with thresyl chloride, and the biospecific ligand p-aminophenyl 1-thio-(beta)-D-galactopyranoside (APGP) was attached to the activated PEG 4000. A new two-step method for extraction and purification of the enzyme (beta)-galactosidase from "Kluyveromyces fragilis" was developed. In the first step, a system composed of 6(per cent) PEG 4000-APGP and 8(per cent) dextran 505 was used, where (beta)-galactosidase was strongly partitioned to the top phase (K = 2.330). In the second step, a system formed of 13(per cent) Peg-APGP and 9(per cent) phosphate salt was used to revert the value of the partition coefficient of (beta)-galactosidase (K = 2.0E-5) in order to provide the purification and recovery of 39(per cent) of the enzyme in the bottom salt-rich phase
Asunto(s)
Texto completo: Disponible Índice: LILACS (Américas) Asunto principal: Kluyveromyces / Proteínas / Beta-Galactosidasa Idioma: Inglés Revista: Rev. microbiol Asunto de la revista: Microbiologia Año: 1999 Tipo del documento: Artículo País de afiliación: Brasil

Similares

MEDLINE

...
LILACS

LIS

Texto completo: Disponible Índice: LILACS (Américas) Asunto principal: Kluyveromyces / Proteínas / Beta-Galactosidasa Idioma: Inglés Revista: Rev. microbiol Asunto de la revista: Microbiologia Año: 1999 Tipo del documento: Artículo País de afiliación: Brasil