Artículos de revistas
PURIFICATION AND CHARACTERIZATION OF THERMOSTABLE XYLANASES FROM THERMOPHILIC HUMICOLA SP AND THEIR APPLICATION IN PULP IMPROVEMENT
Registro en:
Revista De Microbiologia. Soc Brasileira Microbiologia, v. 25, n. 2, n. 112, n. 118, 1994.
0001-3714
WOS:A1994NX84600008
Autor
DASILVA, R
YIM, DK
PARK, YK
Institución
Resumen
A thermophilic Humicola sp. isolated from decayed wood produced thermostable extracellular xylanase at 50-degrees-C. Enzyme purification was done by DEAE-Sephadex and CM-Sephadex C-50 gel column chromatography and three protein fractions with xylanase activity were found. Optimal pH and temperature values for the three xylanases were pH 5.0 and 5.6 and 75-degrees-C. Other characteristics of the enzymes were investigated and it was found that xylanase I was an endoxylanase while xylanase II was a xylosidase (exoxylanase). Xylanase III was an endoxylanase and also showed arabinosidase and CMCase activities. Treatment of bleached Kraft eucalyptus pulp with purified and crude enzymes enhanced pulp brightness compared to untreated pulp. Xylanase I and crude xylanase increased pulp viscosity whereas xylanase II and III decreased it due to the presence of CMCase activity. 25 2 112 118