INVESTIGADORES
BRECCIA Javier Dario
artículos
Título:
Specificity and mode of action of a thermostable xylanase from B. amyloliquefaciens. On-line monitoring of hydrolysis products
Autor/es:
BRECCIA JD,; TORTO N,; GORTON L,; SIÑERIZ F,; HATTI-KAUL R,
Revista:
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
Editorial:
Springer
Referencias:
Lugar: Netherlands; Año: 1998 vol. 69 p. 31 - 40
ISSN:
0273-2289
Resumen:
ß-1,4-Xylanase, produced extracellularly by Bacillus halodurans MIR32, was isolated directly from the culture broth by adsorption on a cation exchanger, Amberlite IRC-50, in fluidized bed with a low degree of expansion. The enzyme was eluted from the adsorbent by increase in pH, with a recovery of 82.3 % and purification of 5.3 fold. About 99.99 % of the colony forming units, 82% of the contaminating neutral protease activity, and 100 % of the reducing sugars present in the crude feed stock were removed at the end of the purification cycle.