ISSN:
0006-3592
Keywords:
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
The β-galactosidase from Escherichia coli ATTCC-26 was partially purified and characterized. It was found to be comparable to galactosidases from other E. coli strains in stability, pH and temperature maxima, and activity requirements, but it had a more favorable ratio of activity toward lactose versus synthetic substrates. The galactosidase was immobilized on porous glass beads by three covalent bonding methods. Kinetic data for the free and bound enzymes were determined using natural and synthetic substrates. Activity characteristics of the free and immobilized enzymes were comparable, however, the bound forms were less stable to heat.
Additional Material:
7 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/bit.260161206
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