ISSN:
0006-3592
Keywords:
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Aspergillus niger β-xylosidase was characterized when in soluble form and when immobilized to alkylamine porous silica with glutaraldehyde and to alumina with titanium tetrachloride. Energies of activation averaged 13.4 KcaL/mol for the soluble enzyme, 9.0 Kcal/mol when immobilized to alumina, and 8.0 Kcal/mol when bound to silica. The highest activity of all forms of β-xylosidase was found near pH 3. The soluble enzyme was highly stable at pH 4, where lowest rates of decay occurred, and temperature of 65°C and below. The decay rates of alumina-bound β-xylosidase and pH 4 and equivalent temperatures were approximately 10 times as high. Michaells constants were 0.200 and 0.262mM for o-nitrophenyl-β-D-xylopyranoside with soluble and alumina-bound β-xylosidase, respectively.
Additional Material:
6 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/bit.260220604
