ISSN:
0006-3592
Keywords:
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Endo-polygalacturonase (endo-PG) was immobilized on a wide range of natural and synthetic macromolecular supports and their modified derivatives representing many chemical classes, including esters, amides, phenols, alkyl- and arylamines, and carboxyl derivatives. The immobilization entailed methods of adsorption alone as well as covalent bond formation using glutaraldehyde or carbodiimide or via the diazo-coupling reaction. The most promising system proved to be immobilization on trimalehylchitosan (TMC) via adsorption followed by treatment with glutaraldehyde (GA). The binding capacity of the support is on the order of 13,000 IU/g, half of which is active. Various properties of immobilized endo-PG were evaluated. The optimum pH of the enzyme shifted to the alkaline side. The relative catalytic activity was considerably high even at room temperature and remained so above 70°C. The thermal stability at pH 3-4 was notably improved by immobilization, the half-time doubling. Finally, the apparent Km was greater for immobilized endo-PG than for native enzyme, while the Vmax was smaller for the immobilized enzyme.
Additional Material:
4 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/bit.260331006
