Influence of Carbohydrate Residues on Fundamental Properties of Glyco-enzyme.
Abstract
A procedure for isolation and purification of exo-beta-D-galactofuranosidase has been developed. This procedure provides an enzyme preparation that is free of contaminating proteases, phosphatases, other glycohydrolases, and 5'-nucleotidase. The enzyme binds relatively tightly to dextrans and to cellulose, a property which could be exploited in its removal from natural sources. It appears that several of the other acid hydrolases (proteases, phosphateses, 5'nucleotidases) also bind to these carbohydrate polymers. These data suggest that the release of lytic enzymes can be controlled by the addition of substances which buffer the pH between 3 and 4 and may be of practical significance in decreasing fungal destruction of clothing and other items which are subject to attack by these organisms.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jul 10, 1978
- Accession Number
- ADA057356
Entities
People
- J. E. Gander
Organizations
- University of Minnesota