Isolation of Beta-xylanase from whole broth of B. amyloliquefaciens by adsorption on a matrix in fluidized bed with low degree of expansion

BRECCIA JD,; HATTI-KAUL R,; CASTRO GR,; SIÑERIZ F,; BRECCIA, JD

BIOSEPARATION

Springer

Año: 1999 vol. 8 p. 273 - 279

0923-179X

Abstractß-1,4-Xylanase, produced extracellularly by Bacillus amyloliquefaciens MIR 32, 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 feedstock were removed at the end of the purification cycle.